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Conserved domains on  [gi|1952775749|ref|XP_022277560|]
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dehydrogenase/reductase SDR family member 1 [Canis lupus familiaris]

Protein Classification

dehydrogenase/reductase SDR family member 1( domain architecture ID 10176799)

dehydrogenase/reductase SDR family member 1 (DHRS1) is an uncharacterized enzyme from the short-chain dehydrogenases/reductases (SDR) family of NAD(P)(H)-dependent oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 9.73e-160

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


:

Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 446.12  E-value: 9.73e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM-DTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVSY 163
Cdd:cd09763    81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvvvKNENTDDPLLKQLRSNFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763   161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLE---MPEDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                         250       260
                  ....*....|....*....|....*...
gi 1952775749 244 NILSLSGKVLPSCDLARRYSLQDVDGRP 271
Cdd:cd09763   238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 9.73e-160

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 446.12  E-value: 9.73e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM-DTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVSY 163
Cdd:cd09763    81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvvvKNENTDDPLLKQLRSNFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763   161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLE---MPEDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                         250       260
                  ....*....|....*....|....*...
gi 1952775749 244 NILSLSGKVLPSCDLARRYSLQDVDGRP 271
Cdd:cd09763   238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-242 1.27e-56

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 183.45  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNV 161
Cdd:COG1028    81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknenTDDPLLKQLRSN--FSSAETTEMSGKCVVAL 239
Cdd:COG1028   154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL-----GAEEVREALAARipLGRLGTPEEVAAAVLFL 228


                  ...
gi 1952775749 240 ATD 242
Cdd:COG1028   229 ASD 231
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-271 2.06e-55

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 182.12  E-value: 2.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM----------DTLQATAEEAQSRGGQCVPVVCDSSQESE 70
Cdd:PRK08303    2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  71 VQRLFEQVDQEqQGRLDVLVNNAYAGVPaiMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVIS 150
Cdd:PRK08303   82 VRALVERIDRE-QGRLDILVNDIWGGEK--LFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 151 ----SIGGLQYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV-VKNENTDDPLLKQlrSNFSS 225
Cdd:PRK08303  159 dgtaEYNATHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFgVTEENWRDALAKE--PHFAI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1952775749 226 AETTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYSLQDVDG-RP 271
Cdd:PRK08303  237 SETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-204 1.67e-45

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.77  E-value: 1.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVS-YGVG 166
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 7-203 2.58e-13

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 68.50  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGR-----HMDTLQATAEE----AQSRGGQCVPVVCDSSQESEVQRLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRAEldavAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  78 VdQEQQGRLDVLVNNA---YAGVPAimkninkafWESPASIWDDINNVGLRGhylcsVYG-ARLMVPA-------GQGLI 146
Cdd:TIGR04504  81 A-VERWGRLDAAVAAAgviAGGRPL---------WETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 147 VVISSIGGLQYFFNV-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:TIGR04504 146 VAVASAAATRGLPHLaAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-93 3.70e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.54  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749    8 KVCVVTGASRGIGRGIALQLCQAGA-TVYITGRH---MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIP-AVE 79

                           90
                   ....*....|
gi 1952775749   84 GRLDVLVNNA 93
Cdd:smart00822  80 GPLTGVIHAA 89
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 9.73e-160

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 446.12  E-value: 9.73e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM-DTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVSY 163
Cdd:cd09763    81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvvvKNENTDDPLLKQLRSNFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763   161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLE---MPEDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                         250       260
                  ....*....|....*....|....*...
gi 1952775749 244 NILSLSGKVLPSCDLARRYSLQDVDGRP 271
Cdd:cd09763   238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 5-271 2.10e-91

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 271.96  E-value: 2.10e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMD------------TLQATAEEAQSRGGQCVPVVCDSSQESEVQ 72
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngsakslpgTIEETAEEIEAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  73 RLFEQVDqEQQGRLDVLVNNAYAGVPAImkninkaFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSI 152
Cdd:cd05338    81 ALVEATV-DQFGRLDILVNNAGAIWLSL-------VEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 153 GGLQYFF-NVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTelvkevvvknentddpllkqlrsnfsSAETTEM 231
Cdd:cd05338   153 LSLRPARgDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIE--------------------------TPAATEL 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1952775749 232 SGKCVVALATDPNILSLSGKVLPSCDLARRYSLQDVDGRP 271
Cdd:cd05338   207 SGGSDPARARSPEILSDAVLAILSRPAAERTGLVVIDEEL 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-242 1.27e-56

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 183.45  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNV 161
Cdd:COG1028    81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknenTDDPLLKQLRSN--FSSAETTEMSGKCVVAL 239
Cdd:COG1028   154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL-----GAEEVREALAARipLGRLGTPEEVAAAVLFL 228


                  ...
gi 1952775749 240 ATD 242
Cdd:COG1028   229 ASD 231
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-271 2.06e-55

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 182.12  E-value: 2.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM----------DTLQATAEEAQSRGGQCVPVVCDSSQESE 70
Cdd:PRK08303    2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  71 VQRLFEQVDQEqQGRLDVLVNNAYAGVPaiMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVIS 150
Cdd:PRK08303   82 VRALVERIDRE-QGRLDILVNDIWGGEK--LFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 151 ----SIGGLQYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV-VKNENTDDPLLKQlrSNFSS 225
Cdd:PRK08303  159 dgtaEYNATHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFgVTEENWRDALAKE--PHFAI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1952775749 226 AETTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYSLQDVDG-RP 271
Cdd:PRK08303  237 SETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-204 3.07e-50

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 166.51  E-value: 3.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:COG4221     2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAA-VAEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYF-FNVS 162
Cdd:COG4221    78 GRLDVLVNN--AGV-----ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYpGGAV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:COG4221   151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSV 192
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-200 8.76e-49

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 163.12  E-value: 8.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAV-LARF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAimkninkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYF-FNVS 162
Cdd:COG0300    81 GPIDVLVNNAGVGGGG-------PFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLpGMAA 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:COG0300   154 YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-204 1.67e-45

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.77  E-value: 1.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVS-YGVG 166
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-204 2.42e-45

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 153.59  E-value: 2.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  10 CVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAeEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLDVL 89
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEA-LEEFGRLDIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  90 VNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNVSYGVGKA 168
Cdd:cd05233    79 VNN--AGI-----ARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRpLPGQAAYAASKA 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 169 ACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd05233   152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKL 187
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-204 3.28e-40

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 140.68  E-value: 3.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQvDQEQQ 83
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEA-AVEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGvpaimknIN--KAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFN 160
Cdd:PRK05653   81 GALDILVNN--AG-------ITrdALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTgNPGQ 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK05653  152 TNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGL 195
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 4-204 1.46e-37

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 133.78  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTL-QATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:PRK05557    2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKALAVQGDVSDAESVERAVDEA-KAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-V 161
Cdd:PRK05557   81 FGGVDILVNNA-----GITR--DNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGqA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK05557  154 NYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDAL 196
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-199 6.21e-37

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 132.27  E-value: 6.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITG-RHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQG 84
Cdd:PRK05565    4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIV-EKFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNVSY 163
Cdd:PRK05565   83 KIDILVNNA-----GISN--FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIgASCEVLY 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK05565  156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTE 191
PRK12826 PRK12826
SDR family oxidoreductase;
3-204 9.16e-37

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 131.96  E-value: 9.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQ 82
Cdd:PRK12826    2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGV-ED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNA-YAGvpaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ--YFF 159
Cdd:PRK12826   81 FGRLDILVANAgIFP--------LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvgYPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 160 NVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK12826  153 LAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL 197
PRK07035 PRK07035
SDR family oxidoreductase;
4-242 4.02e-36

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 130.14  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK07035    5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHI-RERH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAgvpaimkniNKAF---WESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ--YF 158
Cdd:PRK07035   84 GRLDILVNNAAA---------NPYFghiLDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSpgDF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 159 FNVsYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVkEVVVKNENTDDPLLKQLRSNfSSAETTEMSGkCVVA 238
Cdd:PRK07035  155 QGI-YSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFA-SALFKNDAILKQALAHIPLR-RHAEPSEMAG-AVLY 230


                  ....
gi 1952775749 239 LATD 242
Cdd:PRK07035  231 LASD 234
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-242 1.09e-34

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 126.68  E-value: 1.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEq 82
Cdd:cd05352     5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKD- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGlqYFFNV- 161
Cdd:cd05352    84 FGKIDILIAN--AGI-----TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSG--TIVNRp 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 162 ----SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPLLKQLRsnfsSAETTEMSGKCVV 237
Cdd:cd05352   155 qpqaAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKR----IALPEELVGAYLY 230


                  ....*
gi 1952775749 238 aLATD 242
Cdd:cd05352   231 -LASD 234
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-213 2.58e-34

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 125.55  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd05347     2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAI-EEDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAimkninkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVS- 162
Cdd:cd05347    81 GKIDILVNNAGIIRRH-------PAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPa 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDD 213
Cdd:cd05347   154 YAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDD 204
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-200 3.22e-34

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 125.22  E-value: 3.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVP---VVCDSSQESEVQRLFEQVdQE 81
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKillVVADLTEEEGQDRIISTT-LA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNayAGVPAIMKNINKafwesPASIWDDINNVGLRGHYLCSvygaRLMVP---AGQGLIVVISSI-GGLQY 157
Cdd:cd05364    80 KFGRLDILVNN--AGILAKGGGEDQ-----DIEEYDKVMNLNLRAVIYLT----KLAVPhliKTKGEIVNVSSVaGGRSF 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 158 FFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05364   149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-202 4.76e-34

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 124.83  E-value: 4.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:PRK08063    2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQID-EEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVpaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-VS 162
Cdd:PRK08063   81 GRLDVFVNNAASGV-------LRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENyTT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK08063  154 VGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALK 193
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-200 7.31e-33

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 121.62  E-value: 7.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK12939    1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAA-A 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:PRK12939   80 AALGGLDGLVNNA-----GITN--SKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPK 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 161 V-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK12939  153 LgAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-242 1.52e-32

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 120.95  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGR-HMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKE-F 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVPAimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMV-PAGQGLIVVISSIGglQYF---F 159
Cdd:cd05358    80 GTLDILVNN--AGLQG-----DASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSSVH--EKIpwpG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 160 NVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVvvknenTDDP-LLKQLRSN--FSSAETTEMSGKCV 236
Cdd:cd05358   151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEA------WDDPeQRADLLSLipMGRIGEPEEIAAAA 224


                  ....*.
gi 1952775749 237 VALATD 242
Cdd:cd05358   225 AWLASD 230
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 12-199 1.74e-32

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 120.53  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRH-MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQGRLDVLV 90
Cdd:cd05359     3 VTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVK-ERFGRLDVLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  91 NNAYAGVpaiMKNINKAFWESpasiWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-VSYGVGKAA 169
Cdd:cd05359    82 SNAAAGA---FRPLSELTPAH----WDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNyLAVGTAKAA 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1952775749 170 CDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05359   155 LEALVRYLAVELGPRGIRVNAVSPGVIDTD 184
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-194 9.26e-32

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 118.90  E-value: 9.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQG 84
Cdd:PRK08213   10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLER-FG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYA--GVPAImkninkafwESPASIWDDINNVGLRGHYLCS-VYGARLMVPAGQGLIVVISSIGGLQ----- 156
Cdd:PRK08213   89 HVDILVNNAGAtwGAPAE---------DHPVEAWDKVMNLNVRGLFLLSqAVAKRSMIPRGYGRIINVASVAGLGgnppe 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 157 YFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:PRK08213  160 VMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPG 197
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-204 1.47e-31

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 118.03  E-value: 1.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLD 87
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKV-EAEFGPVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-VSYGVG 166
Cdd:cd05333    80 ILVNN--AGI-----TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGqANYAAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd05333   153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDAL 190
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 17-204 2.61e-31

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 117.15  E-value: 2.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  17 RGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPvvCDSSQESEVQRLFEQVdQEQQGRLDVLVNNAyag 96
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLP--CDVTDEEQVEALVAAA-VEKFGRLDILVNNA--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  97 vpAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPagQGLIVVISSIGGLQYFFNVS-YGVGKAACDRLAA 175
Cdd:pfam13561  80 --GFAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE--GGSIVNLSSIGAERVVPNYNaYGAAKAALEALTR 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1952775749 176 DCAQELRRHG--VSYVSlwPGMVQTELVKEV 204
Cdd:pfam13561 156 YLAVELGPRGirVNAIS--PGPIKTLAASGI 184
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-212 3.07e-31

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 117.10  E-value: 3.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK07666    1 MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQL-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNayAGVPAIMKninkaFWESPASIWDDINNVGLRGHYlcsvYGARLMVPA----GQGLIVVISSIGGLQ 156
Cdd:PRK07666   80 NELGSIDILINN--AGISKFGK-----FLELDPAEWEKIIQVNLMGVY----YATRAVLPSmierQSGDIINISSTAGQK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952775749 157 YFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTD 212
Cdd:PRK07666  149 GAAVTSaYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPD 205
FabG-like PRK07231
SDR family oxidoreductase;
7-203 3.80e-30

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 114.54  E-value: 3.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSrGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK07231    5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVAAA-LERFGSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGV-PAimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-VSYG 164
Cdd:PRK07231   83 DILVNN--AGTtHR-----NGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGlGWYN 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK07231  156 ASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEA 194
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 5-201 4.42e-30

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 114.60  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYA-VETFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVpAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFfnvsyg 164
Cdd:PRK12429   81 GVDILVNN--AGI-QHVAPIE----DFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGS------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 165 VGKAACDR-------LAADCAQELRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK12429  148 AGKAAYVSakhgligLTKVVALEGATHGVTVNAICPGYVDTPLV 191
PRK05867 PRK05867
SDR family oxidoreductase;
5-202 5.20e-30

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 114.36  E-value: 5.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQG 84
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 rLDVLVNNayAGVPAImkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGlqYFFNVSY 163
Cdd:PRK05867   87 -IDIAVCN--AGIITV-----TPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSG--HIINVPQ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 164 GVG-----KAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK05867  157 QVShycasKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVE 200
PRK07326 PRK07326
SDR family oxidoreductase;
4-199 5.00e-29

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 111.26  E-value: 5.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK07326    3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAEL-NNKGNVLGLAADVRDEADVQRAVDAIVAA-F 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpAIMKNINkafwESPASIWDDINNVGLRGHYlcsvYGARLMVPA---GQGLIVVISSIGGLQYFFN 160
Cdd:PRK07326   81 GGLDVLIAN--AGV-GHFAPVE----ELTPEEWRLVIDTNLTGAF----YTIKAAVPAlkrGGGYIINISSLAGTNFFAG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 161 -VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK07326  150 gAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK06172 PRK06172
SDR family oxidoreductase;
1-200 5.83e-29

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 111.38  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK06172    1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQT-I 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAYAGVpaimknINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:PRK06172   80 AAYGRLDYAFNNAGIEI------EQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 161 VS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK06172  154 MSiYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 4-212 8.61e-29

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 111.00  E-value: 8.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd05329     3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVS- 162
Cdd:cd05329    83 GKLNILVNN--AGT-----NIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAp 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTD 212
Cdd:cd05329   156 YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLD 205
PRK06181 PRK06181
SDR family oxidoreductase;
7-202 2.54e-28

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 110.07  E-value: 2.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAA-VARFGGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAimkniNKAFWESPA-SIWDDINNVglrgHYLCSVYGARLMVP---AGQGLIVVISSIGGLQYFFNVS 162
Cdd:PRK06181   80 DILVNN--AGITM-----WSRFDELTDlSVFERVMRV----NYLGAVYCTHAALPhlkASRGQIVVVSSLAGLTGVPTRS 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 163 -YGVGKAA----CDRLAAdcaqELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK06181  149 gYAASKHAlhgfFDSLRI----ELADDGVAVTVVCPGFVATDIRK 189
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-202 3.11e-28

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 109.28  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQI-AEDFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpAIMKN-----------INKAFWESpasiWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSI 152
Cdd:PRK08217   82 QLNGLINNA-----GILRDgllvkakdgkvTSKMSLEQ----FQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 153 GGLQYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK08217  153 ARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA 202
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 4-181 7.78e-28

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 108.34  E-value: 7.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd08942     3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEEL-SAYGECIAIPADLSSEEGIEALVARV-AERS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAimkninkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ----GLIVVISSIGGL--QY 157
Cdd:cd08942    81 DRLDVLVNNAGATWGA-------PLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIvvSG 153

                         170       180
                  ....*....|....*....|....
gi 1952775749 158 FFNVSYGVGKAACDRLAADCAQEL 181
Cdd:cd08942   154 LENYSYGASKAAVHQLTRKLAKEL 177
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-205 8.05e-28

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 108.42  E-value: 8.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGR-HMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQvDQEQ 82
Cdd:PRK12825    3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAA-AVER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYlcsvYGARLMVP----AGQGLIVVISSIGGLQ-Y 157
Cdd:PRK12825   82 FGRIDILVNN--AGI-----FEDKPLADMSDDEWDEVIDVNLSGVF----HLLRAVVPpmrkQRGGRIVNISSVAGLPgW 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 158 FFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV 205
Cdd:PRK12825  151 PGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATI 198
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-200 9.80e-28

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 108.01  E-value: 9.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERT-VEALG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNINKAFWESPAsiwdDINNVGLrghylcsVYGAR----LMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:cd08934    80 RLDILVNNAGIMLLGPVEDADTTDWTRMI----DTNLLGL-------MYTTHaalpHHLLRNKGTIVNISSVAGRVAVRN 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 161 -VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd08934   149 sAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-242 1.03e-27

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 107.96  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEeaqSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVA---QIAGGALALRVDVTDEQQVAALFERA-VEEFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpAIMkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNVSY 163
Cdd:cd08944    77 GLDLLVNNA-----GAM-HLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSgDPGYGAY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDP-----LLKQLRSNFSSAEttEMSGkCVVA 238
Cdd:cd08944   151 GASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPggfhlLIHQLQGRLGRPE--DVAA-AVVF 227


                  ....
gi 1952775749 239 LATD 242
Cdd:cd08944   228 LLSD 231
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-199 7.58e-27

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 105.75  E-value: 7.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQS-RGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSaTGGRAHPIQCDVRDPEAVEAAVDETLKE-F 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWEspASIwdDINNVGlrGHYLCSVYGARLMVPAGQGLIVVISSIggLQYF---FN 160
Cdd:cd05369    80 GKIDILINNAAGNFLAPAESLSPNGFK--TVI--DIDLNG--TFNTTKAVGKRLIEAKHGGSILNISAT--YAYTgspFQ 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05369   152 VHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-221 1.05e-26

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 105.43  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKA-GDAFGRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAyAGVPAimkninKAFWESPASIWDDinnvGLRGHYLCSVYGARLMVPA----GQGLIVVISSIGGLQYF--FN 160
Cdd:cd05344    80 DILVNNA-GGPPP------GPFAELTDEDWLE----AFDLKLLSVIRIVRAVLPGmkerGWGRIVNISSLTVKEPEpnLV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 161 VSyGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE----LVKEVVVKNENTDDPLLKQLRS 221
Cdd:cd05344   149 LS-NVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTErvrrLLEARAEKEGISVEEAEKEVAS 212
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-199 1.10e-26

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 105.01  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQataEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQGRLD 87
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLE---SLGELLNDNLEVLELDVTDEESIKAAVKEVI-ERFGRID 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNayAGVPAIMkninkAFWESPAsiwDDINNVglrghYLCSVYG--------ARLMVPAGQGLIVVISSIGGLQYFF 159
Cdd:cd05374    77 VLVNN--AGYGLFG-----PLEETSI---EEVREL-----FEVNVFGplrvtrafLPLMRKQGSGRIVNVSSVAGLVPTP 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 160 NVS-YGVGKAACDRLaADC-AQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05374   142 FLGpYCASKAALEAL-SESlRLELAPFGIKVTIIEPGPVRTG 182
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-199 1.78e-26

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 104.13  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATaeeAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQGRLD 87
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAA---AAQELEGVLGLAGDVRDEADVRRAVDAME-EAFGGLD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNayAGVpAIMKNINKAfweSPASIWDDINNVgLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFF-NVSYGVG 166
Cdd:cd08929    77 ALVNN--AGV-GVMKPVEEL---TPEEWRLVLDTN-LTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKgGAAYNAS 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd08929   150 KFGLLGLSEAAMLDLREANIRVVNVMPGSVDTG 182
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 6-200 2.04e-26

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 104.28  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYItgrHMDTLQATAEEA----QSRGGQCVPVVCDSSQESEVQRLFEQVDqE 81
Cdd:cd05362     2 AGKVALVTGASRGIGRAIAKRLARDGASVVV---NYASSKAAAEEVvaeiEAAGGKAIAVQADVSDPSQVARLFDAAE-K 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNAYAGVPAIMKNINKAFwespasiWDDINNVGLRGHYLCSVYGARLMVPAGQgLIVVISSIGGLQYFFNV 161
Cdd:cd05362    78 AFGGVDILVNNAGVMLKKPIAETSEEE-------FDRMFTVNTKGAFFVLQEAAKRLRDGGR-IINISSSLTAAYTPNYG 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05362   150 AYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK08589 PRK08589
SDR family oxidoreductase;
5-242 2.11e-26

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 105.25  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVyITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEI-KEQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVPAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGqGLIVVISSIGGLQYFFNVS-Y 163
Cdd:PRK08589   82 RVDVLFNN--AGVDNAAGRIH----EYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSgY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknENTDDPLLKQLRSN------FSSAETTEMSGKCVV 237
Cdd:PRK08589  155 NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLT---GTSEDEAGKTFRENqkwmtpLGRLGKPEEVAKLVV 231


                  ....*
gi 1952775749 238 ALATD 242
Cdd:PRK08589  232 FLASD 236
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-242 2.87e-26

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 104.00  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd05341     2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTA-REAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKninkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGL----QYff 159
Cdd:cd05341    78 GRLDVLVNNAGILTGGTVE-------TTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLvgdpAL-- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 160 nVSYGVGKAACDRLAADCAQELRRH--GVSYVSLWPGMVQTELVKEVVVKNENTDDPllkQLRSNFSSAETTEMSGkCVV 237
Cdd:cd05341   149 -AAYNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGNY---PNTPMGRAGEPDEIAY-AVV 223


                  ....*
gi 1952775749 238 ALATD 242
Cdd:cd05341   224 YLASD 228
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-203 4.88e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 103.26  E-value: 4.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrggQCVPVVCDSSQESEVQRLFeqvdq 80
Cdd:PRK07060    3 MAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGET-----GCEPLRLDVGDDAAIRAAL----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQYF- 158
Cdd:PRK07060   73 AAAGAFDGLVNC--AGI-----ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVGLp 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK07060  146 DHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAE 190
PRK07814 PRK07814
SDR family oxidoreductase;
4-217 1.90e-25

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 102.16  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK07814    7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQA-VEAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESPASIwddinNVGlRGHYLcSVYGARLMV-PAGQGLIVVISSIGG--LQYFFn 160
Cdd:PRK07814   86 GRLDIVVNNVGGTMPNPLLSTSTKDLADAFTF-----NVA-TAHAL-TVAAVPLMLeHSGGGSVINISSTMGrlAGRGF- 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952775749 161 VSYGVGKAACD---RLAA-DCAQELRRHGVSyvslwPGMVQTELVkEVVVKNENTDDPLLK 217
Cdd:PRK07814  158 AAYGTAKAALAhytRLAAlDLCPRIRVNAIA-----PGSILTSAL-EVVAANDELRAPMEK 212
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-218 2.21e-25

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 102.07  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMD-TLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:cd05366     2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQA-VEKFGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNayAGVPAImkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSIGGLQYFFNVS-Y 163
Cdd:cd05366    81 FDVMVNN--AGIAPI-----TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGaY 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL---VKEVVVKNENTDDPLLKQ 218
Cdd:cd05366   154 SASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyIDEEVGEIAGKPEGEGFA 211
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-230 2.55e-25

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 101.18  E-value: 2.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE----AQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeANASGQKVSYISADLSDYEEVEQAFAQA-VEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNAYAGVPaimkninkAFWE--SPASIWDDINNVglrghYLCSVY----GARLMVPAGQGLIVVISSIGGLQ 156
Cdd:cd08939    80 GGPPDLVVNCAGISIP--------GLFEdlTAEEFERGMDVN-----YFGSLNvahaVLPLMKEQRPGHIVFVSSQAALV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 157 YFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvvvknENTDDPLLKQLRSNFSSAETTE 230
Cdd:cd08939   147 GIYGYSaYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEE-----ENKTKPEETKAIEGSSGPITPE 216
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-221 2.91e-25

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 101.21  E-value: 2.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGAT--VYITGRHMDTLQATAEEAQSrGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKL-DGER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMKNINKAfwespasiwdDINNvgLRGHYLCSVYGARLMVPA---------GQGLIVVISSIGGLQY 157
Cdd:cd05367    79 DLLINN--AGSLGPVSKIEFI----------DLDE--LQKYFDLNLTSPVCLTSTllrafkkrgLKKTVVNVSSGAAVNP 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 158 FFN-VSYGVGKAACDRLAADCAQELRrhGVSYVSLWPGMVQTELVKEVVvkNENTDDPLLKQLRS 221
Cdd:cd05367   145 FKGwGLYCSSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREIR--ETSADPETRSRFRS 205
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-205 3.57e-25

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 101.67  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAeeAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK12829    5 LLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATA--ARLPGAKVTATVADVADPAQVERVFDTA-V 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNA-YAGVPAIMKNInkafweSPASiWDDINNVGLRGHYlcsvYGARLMVPA-----GQGLIVVISSIGG 154
Cdd:PRK12829   82 ERFGGLDVLVNNAgIAGPTGGIDEI------TPEQ-WEQTLAVNLNGQF----YFARAAVPLlkasgHGGVIIALSSVAG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952775749 155 -LQYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV 205
Cdd:PRK12829  151 rLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVI 202
PRK06124 PRK06124
SDR family oxidoreductase;
4-199 1.50e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 99.79  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:PRK06124    8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARID-AEH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNInkafweSPASIWDDInNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG-LQYFFNVS 162
Cdd:PRK06124   87 GRLDILVNNVGARDRRPLAEL------DDAAIRALL-ETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGqVARAGDAV 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06124  160 YPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
PRK12743 PRK12743
SDR family oxidoreductase;
8-198 8.42e-24

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 97.80  E-value: 8.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRH-MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSdEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQR-LGRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAYAGVpaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQYFFNVS-YG 164
Cdd:PRK12743   82 DVLVNNAGAMT-------KAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSVHEHTPLPGASaYT 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK12743  155 AAKHALGGLTKAMALELVEHGILVNAVAPGAIAT 188
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-201 9.58e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 97.66  E-value: 9.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK13394    1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKV-A 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQ-YF 158
Cdd:PRK13394   80 ERFGSVDILVSN--AGI-----QIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEaSP 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK13394  153 LKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLV 195
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 5-205 1.75e-23

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 96.84  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFeQVDQEQQG 84
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALA-DFALSKLG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPaimkninKAFwESPAS--IWDDINNVGLRGHyLCSVyGARLMVPAGQGLIVVISSIGGLQYFFNV- 161
Cdd:PRK06113   88 KVDILVNNAGGGGP-------KPF-DMPMAdfRRAYELNVFSFFH-LSQL-VAPEMEKNGGGVILTITSMAAENKNINMt 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV 205
Cdd:PRK06113  158 SYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVI 201
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-200 1.82e-23

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 96.35  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:PRK12937    5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAA-ETAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAyagvpAIMKNINKAfwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQglIVVIS-SIGGLQYFFNVSYG 164
Cdd:PRK12937   84 IDVLVNNA-----GVMPLGTIA--DFDLEDFDRTIATNLRGAFVVLREAARHLGQGGR--IINLStSVIALPLPGYGPYA 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK12937  155 ASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK07454 PRK07454
SDR family oxidoreductase;
12-200 2.11e-23

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 96.18  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLDVLVN 91
Cdd:PRK07454   11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAEL-LEQFGCPDVLIN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NAYAGvpaimknINKAFWESPASIWDDINNVGLRGHYLCsvygARLMVPA----GQGLIVVISSIGGLQYFFNV-SYGVG 166
Cdd:PRK07454   90 NAGMA-------YTGPLLEMPLSDWQWVIQLNLTSVFQC----CSAVLPGmrarGGGLIINVSSIAARNAFPQWgAYCVS 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK07454  159 KAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 8-198 2.23e-23

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 95.89  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATaeeaQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRLD 87
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAAL----SASGGDVEAVPYDARDPEDARALVDALRDR-FGRID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPAIMKNINKAFWEspaSIWdDINnvglrghylcsVYGARLMV----PA----GQGLIVVISSI-GGLQYF 158
Cdd:cd08932    76 VLVHNAGIGRPTTLREGSDAELE---AHF-SIN-----------VIAPAELTrallPAlreaGSGRVVFLNSLsGKRVLA 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:cd08932   141 GNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDT 180
PRK07774 PRK07774
SDR family oxidoreductase;
6-208 2.41e-23

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 96.35  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:PRK07774    5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADAT-VSAFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAyagvpAIMKNINKAFWES-PASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYffNVSYG 164
Cdd:PRK07774   84 IDYLVNNA-----AIYGGMKLDLLITvPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLY--SNFYG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKN 208
Cdd:PRK07774  157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKE 200
PRK08278 PRK08278
SDR family oxidoreductase;
3-193 2.79e-23

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 96.51  E-value: 2.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGR----HMD---TLQATAEEAQSRGGQCVPVVCDSSQESEVQRlf 75
Cdd:PRK08278    2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaepHPKlpgTIHTAAEEIEAAGGQALPLVGDVRDEDQVAA-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  76 eQVDQ--EQQGRLDVLVNNAYAgvpaimknINKA-FWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVIS-- 150
Cdd:PRK08278   80 -AVAKavERFGGIDICVNNASA--------INLTgTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpp 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 151 -SIGGLQYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWP 193
Cdd:PRK08278  151 lNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 8-251 6.29e-23

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 94.61  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGA-TVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFV-EEKYGGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMKNINKAFWESPASIWdDINnvglrghylcsVYGAR--------LMVPAGQGLIVVISSIGGLQyf 158
Cdd:cd05324    80 DILVNN--AGIAFKGFDDSTPTREQARETM-KTN-----------FFGTVdvtqallpLLKKSPAGRIVNVSSGLGSL-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 159 fNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELvkevvvknentddpllkqlrSNFSSAETTEMSGKCVVA 238
Cdd:cd05324   144 -TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDM--------------------GGGKAPKTPEEGAETPVY 202

                         250
                  ....*....|...
gi 1952775749 239 LATDPNILSLSGK 251
Cdd:cd05324   203 LALLPPDGEPTGK 215
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 4-234 6.98e-23

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 95.46  E-value: 6.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlqataeEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK06171    6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIH---------GGDGQHENYQFVPTDVSSAEEVNHTVAEI-IEKF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIM--KNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNV 161
Cdd:PRK06171   76 GRIDGLVNNAGINIPRLLvdEKDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQ 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 162 S-YGVGKAACDRLAADCAQELRRHGVSYVSLWPG-MVQTEL-VKEVVVKNENTDDPLLKQLRSNFSSAETTEM--SGK 234
Cdd:PRK06171  156 ScYAATKAALNSFTRSWAKELGKHNIRVVGVAPGiLEATGLrTPEYEEALAYTRGITVEQLRAGYTKTSTIPLgrSGK 233
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
7-186 8.29e-23

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 98.76  E-value: 8.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRgGQCVPVVCDSSQESEVQRLFEQVDQEQQGrL 86
Cdd:PRK08324  422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP-DRALGVACDVTDEAAVQAAFEEAALAFGG-V 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIgglQYFF----NV 161
Cdd:PRK08324  500 DIVVSN--AGI-----AISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASK---NAVNpgpnFG 569

                         170       180
                  ....*....|....*....|....*
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGV 186
Cdd:PRK08324  570 AYGAAKAAELHLVRQLALELGPDGI 594
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-245 1.63e-22

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 94.12  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCV-PVVCDSSQESEVQRLFEQVDQEQQG 84
Cdd:cd05343     5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAIRTQHQG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 rLDVLVNNAYAGVPaimkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLM--VPAGQGLIVVISSIGG----LQYF 158
Cdd:cd05343    85 -VDVCINNAGLARP-------EPLLSGKTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININSMSGhrvpPVSV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 159 FNVsYGVGKAACDRLAADCAQELR--RHGVSYVSLWPGMVQTELvkevVVKNENTDDPLLKQLRSNFSSAETTEMSGKCV 236
Cdd:cd05343   157 FHF-YAATKHAVTALTEGLRQELReaKTHIRATSISPGLVETEF----AFKLHDNDPEKAAATYESIPCLKPEDVANAVL 231


                  ....*....
gi 1952775749 237 VALATDPNI 245
Cdd:cd05343   232 YVLSTPPHV 240
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 9-206 1.71e-22

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 93.79  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLDV 88
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKAT-VSQFGGITI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  89 LVNNAYAG------VPAIMKNINKAFWESPASIWddinnvglRGHYLCsvygARLMVPAGQGLIVVISSIGGLQYFFNV- 161
Cdd:cd05365    80 LVNNAGGGgpkpfdMPMTEEDFEWAFKLNLFSAF--------RLSQLC----APHMQKAGGGAILNISSMSSENKNVRIa 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVV 206
Cdd:cd05365   148 AYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLT 192
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-264 7.49e-22

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 92.67  E-value: 7.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCD-SSQESeVQRLFEQVdQEQQ 83
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikKETGNAKVEVIQLDlSSLAS-VRQFAEEF-LARF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAyagvpAIMkniNKAFWESPasiwDDIN-----NvglrghYLCSVYGARLMVPA----GQGLIVVISSIGG 154
Cdd:cd05327    79 PRLDILINNA-----GIM---APPRRLTK----DGFElqfavN------YLGHFLLTNLLLPVlkasAPSRIVNVSSIAH 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 155 LQYFFNVS---------------YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknentdDPLLKQL 219
Cdd:cd05327   141 RAGPIDFNdldlennkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNG-------SFFLLYK 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 220 RSNFSSAETTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYSL 264
Cdd:cd05327   214 LLRPFLKKSPEQGAQTALYAATSPELEGVSGKYFSDCKIKMSSSE 258
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 1-213 1.39e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 92.17  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK05875    1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEieALKGAGAVRYEPADVTDEDQVARAVDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 dQEQQGRLDVLVNNAyAGVPAI--MKNINKAFWESPAsiwdDINnvgLRGHYLCSVYGARLMVPAGQGLIVVISSIGG-- 154
Cdd:PRK05875   81 -TAWHGRLHGVVHCA-GGSETIgpITQIDSDAWRRTV----DLN---VNGTMYVLKHAARELVRGGGGSFVGISSIAAsn 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952775749 155 LQYFFNvSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDD 213
Cdd:PRK05875  152 THRWFG-AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSAD 209
PRK09242 PRK09242
SDR family oxidoreductase;
4-218 1.59e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 91.35  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQVdQE 81
Cdd:PRK09242    6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDElaEEFPEREVHGLAADVSDDEDRRAILDWV-ED 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNayAGVpaimkNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN- 160
Cdd:PRK09242   85 HWDGLHILVNN--AGG-----NIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSg 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvVVKNENTDDPLLKQ 218
Cdd:PRK09242  158 APYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSG-PLSDPDYYEQVIER 214
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 6-194 1.66e-21

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 91.64  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQC--VPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:PRK12384    1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGmaYGFGADATSEQSVLALSRGVD-EIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpAIMKNInkafWESPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSIGG-LQYFFNV 161
Cdd:PRK12384   80 GRVDLLVYN--AGI-AKAAFI----TDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGkVGSKHNS 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:PRK12384  153 GYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-186 3.74e-21

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 90.14  E-value: 3.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGqCVPVVCDSSQESEVQRLFEQVDQEQQGrL 86
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPR-ALGVQCDVTSEAQVQSAFEQAVLEFGG-L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVpAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSIGGLQYFFN-VSYG 164
Cdd:cd08943    79 DIVVSN--AGI-ATSSPIA----ETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNaAAYS 151

                         170       180
                  ....*....|....*....|..
gi 1952775749 165 VGKAACDRLAADCAQELRRHGV 186
Cdd:cd08943   152 AAKAAEAHLARCLALEGGEDGI 173
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 5-119 3.77e-21

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 90.22  E-value: 3.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaqsrggqcVP----VVCDSSQESEVQRLFEQVdQ 80
Cdd:COG3967     3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAA--------NPglhtIVLDVADPASIAALAEQV-T 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952775749  81 EQQGRLDVLVNNAyagvpAIMKNINkafWESPASIWDDI 119
Cdd:COG3967    74 AEFPDLNVLINNA-----GIMRAED---LLDEAEDLADA 104
PRK06947 PRK06947
SDR family oxidoreductase;
8-200 4.45e-21

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 90.25  E-value: 4.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSA-FGRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAimkninkafwesPASIWDDINNVGLR--------GHYLCSVYGARLMVPA---GQGLIVVISSIGGL 155
Cdd:PRK06947   82 DALVNN--AGIVA------------PSMPLADMDAARLRrmfdtnvlGAYLCAREAARRLSTDrggRGGAIVNVSSIASR 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 156 -----QYffnVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK06947  148 lgspnEY---VDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK12746 PRK12746
SDR family oxidoreductase;
4-224 6.04e-21

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 89.71  E-value: 6.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYI-TGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQ 82
Cdd:PRK12746    3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGR-----LDVLVNNAYAGVPAIMKNINKafwespaSIWDDINNVGLRGHYLcsVYGARLMVPAGQGLIVVISSIG-GLQ 156
Cdd:PRK12746   83 QIRvgtseIDILVNNAGIGTQGTIENTTE-------EIFDEIMAVNIKAPFF--LIQQTLPLLRAEGRVINISSAEvRLG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 157 YFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknentDDPLLKQLRSNFS 224
Cdd:PRK12746  154 FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL------DDPEIRNFATNSS 215
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 5-205 6.44e-21

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 89.95  E-value: 6.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVV-CDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVpLDMSDLEDAEQVVEEA-LKLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayagvpAIMKNINKaFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG-LQYFFNVS 162
Cdd:cd05332    80 GGLDILINN------AGISMRSL-FHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGkIGVPFRTA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1952775749 163 YGVGKAAcdrLAA--DCAQ-ELRRHGVSYVSLWPGMVQTELVKEVV 205
Cdd:cd05332   153 YAASKHA---LQGffDSLRaELSEPNISVTVVCPGLIDTNIAMNAL 195
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 6-194 6.60e-21

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 89.70  E-value: 6.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG-QCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESY-LEKFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVpaimKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGL--------- 155
Cdd:cd08930    80 RIDILINNAYPSP----KVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriye 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 156 --QYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:cd08930   156 ntQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-199 9.14e-21

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 89.09  E-value: 9.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVvcDSSQESEVQRLFEQVdQ 80
Cdd:PRK12828    1 MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEV-N 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAYAGVpaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:PRK12828   78 RQFGRLDALVNIAGAFV-------WGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 161 VS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK12828  151 MGaYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTP 190
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-202 1.03e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 89.33  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK06841   12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLL---GGNAKGLVCDVSDSQSVEAAVAAV-ISAF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVPAIMKNInkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISS---IGGLQYffN 160
Cdd:PRK06841   88 GRIDILVNS--AGVALLAPAE-----DVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASqagVVALER--H 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK06841  159 VAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK 200
PRK07832 PRK07832
SDR family oxidoreductase;
8-238 1.13e-20

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 89.33  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQcVP--VVCDSSQESEVQRLFEQVDQEqQGR 85
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGT-VPehRALDISDYDAVAAFAADIHAA-HGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNayAGVpaimkninkAFWESPASI----WDDINNVGLRGhylcSVYGARLMVP----AGQ-GLIVVISSIGGLQ 156
Cdd:PRK07832   79 MDVVMNI--AGI---------SAWGTVDRLtheqWRRMVDVNLMG----PIHVIETFVPpmvaAGRgGHLVNVSSAAGLV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 157 YF-FNVSYGVGK----AACDRLAADcaqeLRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPLLKQLRSNFSS-AETTE 230
Cdd:PRK07832  144 ALpWHAAYSASKfglrGLSEVLRFD----LARHGIGVSVVVPGAVKTPLVNTVEIAGVDREDPRVQKWVDRFRGhAVTPE 219


                  ....*...
gi 1952775749 231 MSGKCVVA 238
Cdd:PRK07832  220 KAAEKILA 227
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-242 1.21e-20

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 89.05  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPvvCDSSQESEVQRLfeqVDQ--EQ 82
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVH--CDVTVEADVRAA---VDTavAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNA-YAGVPAimkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG-LQYFFN 160
Cdd:cd05326    77 FGRLDIMFNNAgVLGAPC------YSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGvVGGLGP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPLLKQLRSNFSSAETTEMSGKCVVALA 240
Cdd:cd05326   151 HAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYLA 230


                  ..
gi 1952775749 241 TD 242
Cdd:cd05326   231 SD 232
PRK07201 PRK07201
SDR family oxidoreductase;
7-93 1.96e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 91.55  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK07201  371 GKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAE-HGHV 449


                  ....*..
gi 1952775749  87 DVLVNNA 93
Cdd:PRK07201  450 DYLVNNA 456
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 12-200 2.42e-20

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 87.77  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRLDVLVN 91
Cdd:cd05350     3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAE-LGGLDLVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NAYAGVPAimkNINKAFWESPASIWdDINNVGlrghylcSVYGARLMVPA----GQGLIVVISSIGGLQYFFN-VSYGVG 166
Cdd:cd05350    82 NAGVGKGT---SLGDLSFKAFRETI-DTNLLG-------AAAILEAALPQfrakGRGHLVLISSVAALRGLPGaAAYSAS 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05350   151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-199 2.48e-20

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 88.11  E-value: 2.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE-AQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQgRL 86
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADElGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR-DI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAyagvpAIMKNINKAfWESPASIWD---DINNVGLrghylcsVYGARLMVPA----GQGLIVVISSIGGLQYFF 159
Cdd:cd05346    80 DILVNNA-----GLALGLDPA-QEADLEDWEtmiDTNVKGL-------LNVTRLILPImiarNQGHIINLGSIAGRYPYA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 160 NVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05346   147 GGNvYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-198 2.72e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 91.06  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK06484  269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEAL---GDEHLSVQADITDEAAVESAFAQI-QARWGRL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMKninKAFWESPASIwDDINNVGLRGHYLCSVYGARLMvpAGQGLIVVISSIGGLQYFF-NVSYGV 165
Cdd:PRK06484  345 DVLVNN--AGIAEVFK---PSLEQSAEDF-TRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPpRNAYCA 416

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 166 GKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK06484  417 SKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-200 3.72e-20

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 87.47  E-value: 3.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITG-RHMDTLQATAEEAQSRGGQCVPVVCDSSQEsEVQRLFEQVDQEQ 82
Cdd:PRK06077    3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGGEGIGVLADVSTR-EGCETLAKATIDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNAYAGvpaimknINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQglIVVISSIGGLQYFFNVS 162
Cdd:PRK06077   82 YGVADILVNNAGLG-------LFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGA--IVNIASVAGIRPAYGLS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 163 -YGVGKAA----CDRLAADCAQELRRHGVSyvslwPGMVQTEL 200
Cdd:PRK06077  153 iYGAMKAAvinlTKYLALELAPKIRVNAIA-----PGFVKTKL 190
PRK05855 PRK05855
SDR family oxidoreductase;
7-202 4.19e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.43  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK05855  315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAE-HGVP 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAYAGVPAimkninkAFWESPASIWDDINNVGLRGhylcSVYGARL----MVPAGQ-GLIVVISSIGGLQYFFNV 161
Cdd:PRK05855  394 DIVVNNAGIGMAG-------GFLDTSAEDWDRVLDVNLWG----VIHGCRLfgrqMVERGTgGHIVNVASAAAYAPSRSL 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 162 S-YGVGKAACDRLaADCAQ-ELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK05855  463 PaYATSKAAVLML-SECLRaELAAAGIGVTAICPGFVDTNIVA 504
PRK06123 PRK06123
SDR family oxidoreductase;
8-200 6.35e-20

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 86.76  E-value: 6.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRH-MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRE-LGRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVP--AGQ-GLIVVISSIGGL-----QYf 158
Cdd:PRK06123   82 DALVNN--AGILEAQMRLE----QMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRgGAIVNVSSMAARlgspgEY- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 159 fnVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK06123  155 --IDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK07074 PRK07074
SDR family oxidoreductase;
8-210 6.37e-20

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 87.13  E-value: 6.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAeeAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQqGRLD 87
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFA--DALGDARFVPVACDLTDAASLAAALANAAAER-GPVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPAIMKninkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVSYGVGK 167
Cdd:PRK07074   80 VLVANAGAARAASLH-------DTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAK 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 168 AACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNEN 210
Cdd:PRK07074  153 AGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQ 195
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-204 6.73e-20

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 87.13  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLD 87
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINdLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQA-WEDFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPAiMKNINKAFWESpasiWDDINNVGLRGHYLCSVYGARLMV-----PAG-QGLIVVISSIGGLQYFFN- 160
Cdd:cd05337    82 CLVNNAGIAVRP-RGDLLDLTEDS----FDRLIAINLRGPFFLTQAVARRMVeqpdrFDGpHRSIIFVTSINAYLVSPNr 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd05337   157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV 200
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 4-201 7.41e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 87.30  E-value: 7.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrgGQCVPVVCDSSQESEVQRLFEQVDQeQQ 83
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEA-DL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGhylcSVYGARL----MVPAGQGLIVVISSIGGLQYFF 159
Cdd:PRK07825   77 GPIDVLVNNA-----GVMP--VGPFLDEPDAVTRRILDVNVYG----VILGSKLaaprMVPRGRGHVVNVASLAGKIPVP 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 160 N-VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK07825  146 GmATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 4-212 8.87e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 86.73  E-value: 8.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK08085    6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKD-I 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVvisSIGGLQYFFN--- 160
Cdd:PRK08085   85 GPIDVLINNA-----GIQR--RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKII---NICSMQSELGrdt 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 161 -VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTD 212
Cdd:PRK08085  155 iTPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFTA 207
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-203 9.61e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.52  E-value: 9.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQeQQGR 85
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRN---VERARERADSLGPDHHALAMDVSDEAQIREGFEQLHR-EFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAyagvpAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGL-IVVISSIGGLQYFFN-VSY 163
Cdd:PRK06484   80 IDVLVNNA-----GVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKrTAY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK06484  155 SASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAE 194
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-194 9.67e-20

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 86.54  E-value: 9.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK12823    2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAA-V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAYAGVPAimkninKAFWE-SPASIWDDINNVGLRGHYLCSvygARL--MVPAGQGLIVVISSI--GGL 155
Cdd:PRK12823   80 EAFGRIDVLINNVGGTIWA------KPFEEyEEEQIEAEIRRSLFPTLWCCR---AVLphMLAQGGGAIVNVSSIatRGI 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 156 QyffNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:PRK12823  151 N---RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 6-199 1.05e-19

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 86.43  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:cd08937     3 EGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAA-VERFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVpaimknINKAFWESP-ASIWDDINNVGLRGHYLCSVYGARlMVPAGQGLIVVISSI---GGLQyffnV 161
Cdd:cd08937    81 VDVLINNVGGTI------WAKPYEHYEeEQIEAEIRRSLFPTLWCCRAVLPH-MLERQQGVIVNVSSIatrGIYR----I 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd08937   150 PYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-257 1.14e-19

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 86.20  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCD-SSQESEVqRLFEQVdQEQQGRL 86
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDvTSWEQLA-AAFKKA-IEKFGRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAyagvpAIMKNINKAFWESPASIWDDINNVGLRGhylcSVYGARLMVPA-------GQGLIVVISSIGGLQ--Y 157
Cdd:cd05323    79 DILINNA-----GILDEKSYLFAGKLPPPWEKTIDVNLTG----VINTTYLALHYmdknkggKGGVIVNIGSVAGLYpaP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 158 FFNVsYGVGKAAC---DRLAADCAqeLRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPLLKQlrsnfssaeTTEMSGK 234
Cdd:cd05323   150 QFPV-YSASKHGVvgfTRSLADLL--EYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQ---------SPEVVAK 217

                         250       260
                  ....*....|....*....|...
gi 1952775749 235 CVVALATDPnilSLSGKVLPSCD 257
Cdd:cd05323   218 AIVYLIEDD---EKNGAIWIVDG 237
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 6-219 1.55e-19

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 85.96  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmDTLQATAEEAQSRGGQCVPVV---CDSSQESEVQRLFEQVdQEQ 82
Cdd:cd08940     1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFG-DAAEIEAVRAGLAAKHGVKVLyhgADLSKPAAIEDMVAYA-QRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVPAIMKninkaFWESPASIWDDINNVGLRGhylcSVYGARLMVPA----GQGLIVVISSIGGLQYF 158
Cdd:cd08940    79 FGGVDILVNN--AGIQHVAP-----IEDFPTEKWDAIIALNLSA----VFHTTRLALPHmkkqGWGRIINIASVHGLVAS 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749 159 FNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVV----VKNENTDDPLLKQL 219
Cdd:cd08940   148 ANKSaYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQIsalaQKNGVPQEQAAREL 213
PRK06138 PRK06138
SDR family oxidoreductase;
5-212 2.02e-19

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 85.59  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSrGGQCVPVVCDSSQESEVQRLFEQVDQEqQG 84
Cdd:PRK06138    3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAAR-WG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNINKAfwespasIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISS----IGGLQyffN 160
Cdd:PRK06138   81 RLDVLVNNAGFGCGGTVVTTDEA-------DWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASqlalAGGRG---R 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTD 212
Cdd:PRK06138  151 AAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPE 202
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 11-200 2.80e-19

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 84.65  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAG-ATVYITGRHMDTLQATAEEAQSRGGQCVPVVcDSSqeSEVQRLFEQVDQE-QQGRLDV 88
Cdd:cd05325     2 LITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILEL-DVT--DEIAESAEAVAERlGDAGLDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  89 LVNNAyagvpAIMKNINKAFWESPASiWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVIS----SIGGLQYFFNVSYG 164
Cdd:cd05325    79 LINNA-----GILHSYGPASEVDSED-LLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISsrvgSIGDNTSGGWYSYR 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05325   153 ASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDM 188
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-199 3.44e-19

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 85.17  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITgRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK06935   12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIIT-THGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEA-LEEF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpaimknINKA-FWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSI----GGLqyf 158
Cdd:PRK06935   90 GKIDILVNN--AGT------IRRApLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMlsfqGGK--- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06935  159 FVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-193 3.93e-19

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 84.80  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMD-------TLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQ 77
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  78 VdQEQQGRLDVLVNNAYAgvpaimknIN-KAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ 156
Cdd:cd09762    81 A-VEKFGGIDILVNNASA--------ISlTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLN 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 157 --YFFN-VSYGVGKAACDRLAADCAQELRRHGVSYVSLWP 193
Cdd:cd09762   152 pkWFKNhTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 4-204 4.06e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 85.11  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK07097    7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKE-V 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAyagvpAIMKNInkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIG---GLQyffN 160
Cdd:PRK07097   86 GVIDILVNNA-----GIIKRI--PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMselGRE---T 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 161 VS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMV---QTELVKEV 204
Cdd:PRK07097  156 VSaYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIatpQTAPLREL 203
PRK06182 PRK06182
short chain dehydrogenase; Validated
 5-199 5.73e-19

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 84.63  E-value: 5.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaqsrGGQCVPVvcDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK06182    1 MQKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL----GVHPLSL--DVTDEASIKAAVDTI-IAEEG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVpaimkninkafwespasiWDDINNVGL---RGHYLCSVYG-ARL-------MVPAGQGLIVVISSIG 153
Cdd:PRK06182   74 RIDVLVNNAGYGS------------------YGAIEDVPIdeaRRQFEVNLFGaARLtqlvlphMRAQRSGRIINISSMG 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 154 GLQY-FFNVSYGVGKAACDRLaADCAQ-ELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06182  136 GKIYtPLGAWYHATKFALEGF-SDALRlEVAPFGIDVVVIEPGGIKTE 182
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-208 7.94e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 84.01  E-value: 7.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVvcDSSQESEVQRLFEQVDq 80
Cdd:PRK06057    1 LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEV---GGLFVPT--DVTDEDAVNALFDTAA- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAYAGVPAimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSigglqyFFN 160
Cdd:PRK06057   75 ETYGSVDIAFNNAGISPPE-----DDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTAS------FVA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749 161 V--------SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKN 208
Cdd:PRK06057  144 VmgsatsqiSYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKD 199
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-151 9.80e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 84.97  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQ 80
Cdd:PRK07109    2 MLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EqQGRLDVLVNNAYAGVPAIMKNIN-----KAFwespasiwdDINnvglrghYLCSVYGA----RLMVPAGQGLIVVISS 151
Cdd:PRK07109   82 E-LGPIDTWVNNAMVTVFGPFEDVTpeefrRVT---------EVT-------YLGVVHGTlaalRHMRPRDRGAIIQVGS 144
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-244 1.01e-18

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 83.74  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRG-GQCVPVVCDSSQESEVQRLFEqVD 79
Cdd:cd08933     3 SGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLIS-VT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  80 QEQQGRLDVLVNNAYAGVPaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYgARLMVPAGQGLIVVISS-IGGLQYF 158
Cdd:cd08933    82 VERFGRIDCLVNNAGWHPP------HQTTDETSAQEFRDLLNLNLISYFLASKY-ALPHLRKSQGNIINLSSlVGSIGQK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPL----LKQLRSNFSsaeTTEMSGK 234
Cdd:cd08933   155 QAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIkegeLAQLLGRMG---TEAESGL 231

                         250
                  ....*....|
gi 1952775749 235 CVVALATDPN 244
Cdd:cd08933   232 AALFLAAEAT 241
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-211 1.01e-18

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 84.05  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd08935     2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEI-VAQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPA-------IMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ 156
Cdd:cd08935    81 GTVDILINGAGGNHPDattdpehYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749 157 YFFNV-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENT 211
Cdd:cd08935   161 PLTKVpAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPDGS 216
PRK09730 PRK09730
SDR family oxidoreductase;
8-200 1.29e-18

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 83.36  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRH-MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQeQQGRL 86
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQnLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMKNINKAFWESpasiwddINNV---GLRGHYLCSVYGARLMV--PAGQ-GLIVVISSIGGL----- 155
Cdd:PRK09730   81 AALVNN--AGILFTQCTVENLTAER-------INRVlstNVTGYFLCCREAVKRMAlkHGGSgGAIVNVSSAASRlgapg 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 156 QYffnVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK09730  152 EY---VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 3-204 1.32e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 83.23  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRH----MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEqV 78
Cdd:PRK12827    2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHpmrgRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALD-A 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 DQEQQGRLDVLVNNayAGVPAimkniNKAFWESPASIWDDINNVGLRGHY-LCSVYGARLMVPAGQGLIVVISSIGGLQ- 156
Cdd:PRK12827   81 GVEEFGRLDILVNN--AGIAT-----DAAFAELSIEEWDDVIDVNLDGFFnVTQAALPPMIRARRGGRIVNIASVAGVRg 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 157 YFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK12827  154 NRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNA 201
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-186 1.36e-18

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 83.14  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYI---------TGRHMDTLQATAEEAQSRGGQCVPvvcDSSQESEVQRL 74
Cdd:cd05353     2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVA---NYDSVEDGEKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  75 FEQVdQEQQGRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG 154
Cdd:cd05353    79 VKTA-IDAFGRVDILVNNA-----GILR--DRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAG 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 155 LQ-YFFNVSYGVGKAACDRLAADCAQELRRHGV 186
Cdd:cd05353   151 LYgNFGQANYSAAKLGLLGLSNTLAIEGAKYNI 183
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-131 1.59e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 83.19  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQGRL 86
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQID-EKFGRI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749  87 DVLVNNAyAG---VPAIMKNINKafwespasiWDDINNVGLRGHYLCS 131
Cdd:PRK07677   80 DALINNA-AGnfiCPAEDLSVNG---------WNSVIDIVLNGTFYCS 117
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 4-204 1.69e-18

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 83.13  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:PRK12935    3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEA-VNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNAYAGVPAIMKNINKAFWESpasiwddINNVGLRGHYLCSVYGARLMVPAGQGLIVVISS-IGGLQYFFNV 161
Cdd:PRK12935   82 FGKVDILVNNAGITRDRTFKKLNREDWER-------VIDVNLSSVFNTTSAVLPYITEAEEGRIISISSiIGQAGGFGQT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK12935  155 NYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV 197
PRK07063 PRK07063
SDR family oxidoreductase;
1-201 1.78e-18

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 83.18  E-value: 1.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK07063    1 MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAiaRDVAGARVLAVPADVTDAASVAAAVAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 dQEQQGRLDVLVNNAYAGV---PAIMKNINkafwespasiWDDINNVGLRGHYlcsvYGARL----MVPAGQGLIVVISS 151
Cdd:PRK07063   81 -EEAFGPLDVLVNNAGINVfadPLAMTDED----------WRRCFAVDLDGAW----NGCRAvlpgMVERGRGSIVNIAS 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 152 IGGlqyfFNV-----SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK07063  146 THA----FKIipgcfPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-186 1.86e-18

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 82.82  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATA-EEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRLD 87
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLvDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEE-IGPLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPaimkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIV---VISSIGGLQYFfnVSYG 164
Cdd:cd05373    80 VLVYNAGANVW-------FPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIftgATASLRGRAGF--AAFA 150

                         170       180
                  ....*....|....*....|..
gi 1952775749 165 VGKAACDRLAADCAQELRRHGV 186
Cdd:cd05373   151 GAKFALRALAQSMARELGPKGI 172
PRK07856 PRK07856
SDR family oxidoreductase;
6-200 2.00e-18

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 82.67  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlqaTAEEAQSRGGQCVPvvCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:PRK07856    5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR------APETVDGRPAEFHA--ADVRDPDQVAALVDAI-VERHGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVPAIMKNINKAFWESpasiwddINNVGLRGHYLCSVYGARLMVP-AGQGLIVVISSIGGLQYF-FNVSY 163
Cdd:PRK07856   76 LDVLVNNAGGSPYALAAEASPRFHEK-------IVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPSpGTAAY 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 164 GVGKAACDRLAADCAQELRRHgVSYVSLWPGMVQTEL 200
Cdd:PRK07856  149 GAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQ 184
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 7-202 2.20e-18

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 82.27  E-value: 2.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG-QCVPVVCDSSQESEV-QRLFEQVDQeqqg 84
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGvETKTIAADFSAGDDIyERIEKELEG---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 rLDV--LVNNAyagvpAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYF-FNV 161
Cdd:cd05356    77 -LDIgiLVNNV-----GISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTpLLA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:cd05356   151 TYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-204 3.52e-18

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 82.12  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGR-HMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRL 86
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFsGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEE-EGPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGlrghyLCSVYG-ARLMVPA----GQGLIVVISSIGGLQ-YFFN 160
Cdd:PRK12824   82 DILVNNA-----GITR--DSVFKRMSHQEWNDVINTN-----LNSVFNvTQPLFAAmceqGYGRIINISSVNGLKgQFGQ 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK12824  150 TNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQM 193
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-214 4.03e-18

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 82.16  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEqVDQEQQG 84
Cdd:PRK08226    4 LTGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGHRCTAVVADVRDPASVAAAIK-RAKEKEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVPAImkninKAFWESPASIWDDINNVGLRGHYlcSVYGARL--MVPAGQGLIVVISSIGG--LQYFFN 160
Cdd:PRK08226   82 RIDILVNN--AGVCRL-----GSFLDMSDEDRDFHIDINIKGVW--NVTKAVLpeMIARKDGRIVMMSSVTGdmVADPGE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVkEVVVKNENTDDP 214
Cdd:PRK08226  153 TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMA-ESIARQSNPEDP 205
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 4-215 4.55e-18

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 81.20  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQataeEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLA----EAKKELPNIHTIVLDVGDAESVEALAEALLSEYP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 gRLDVLVNNAyagvpAIMKNINkafWESPASIWDDIN---NVGLRGhylcSVYGARLMVP----AGQGLIVVISS-IGGL 155
Cdd:cd05370    78 -NLDILINNA-----GIQRPID---LRDPASDLDKADteiDTNLIG----PIRLIKAFLPhlkkQPEATIVNVSSgLAFV 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 156 QYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPL 215
Cdd:cd05370   145 PMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKM 204
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-210 4.63e-18

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 81.52  E-value: 4.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRLDV 88
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKE-VGDVTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  89 LVNNayAGVPAimkniNKAFWESPASIWDDINNVGLRGHYlcSVYGARL--MVPAGQGLIVVISSIGGLQYFFNVS-YGV 165
Cdd:cd05339    80 LINN--AGVVS-----GKKLLELPDEEIEKTFEVNTLAHF--WTTKAFLpdMLERNHGHIVTIASVAGLISPAGLAdYCA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 166 GKAACDRLAADCAQELRRH---GVSYVSLWPGMVQTELVKEVVVKNEN 210
Cdd:cd05339   151 SKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTGMFQGVKTPRPL 198
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-200 5.31e-18

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 81.55  E-value: 5.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITG-RHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAA-QAAWGRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNayAGVPAIMK-NINKAFWESpasiWDDINNVGLRGHYLCSVYGARLMV------PAGQGLIVVISSIGGLQYFF 159
Cdd:PRK12745   82 DCLVNN--AGVGVKVRgDLLDLTPES----FDRVLAINLRGPFFLTQAVAKRMLaqpepeELPHRSIVFVSSVNAIMVSP 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 160 N-VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK12745  156 NrGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-199 5.32e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 81.98  E-value: 5.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGAT-VYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqE 81
Cdd:PRK06198    2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAAD-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNayAGVPAimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSI---GGlQY 157
Cdd:PRK06198   81 AFGRLDALVNA--AGLTD-----RGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMsahGG-QP 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 158 FFnVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06198  153 FL-AAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-204 7.33e-18

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 81.43  E-value: 7.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd08945     1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAA-VARYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNA---YAGVPAIMKNinkafwespaSIWDDINNVGLRGHYLCS--VYGARLMVPAGQGLIVVISSIGGLQYFF 159
Cdd:cd08945    80 PIDVLVNNAgrsGGGATAELAD----------ELWLDVVETNLTGVFRVTkeVLKAGGMLERGTGRIINIASTGGKQGVV 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1952775749 160 NVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd08945   150 HAApYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASV 195
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 5-225 7.44e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 81.27  E-value: 7.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYI-TGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GR-----LDVLVNNAYAGVPAIMKNINKAFWespasiwDDINNVGLRGHYLcsVYGARLMVPAGQGLIVVISSIG---GL 155
Cdd:PRK12747   82 NRtgstkFDILINNAGIGPGAFIEETTEQFF-------DRMVSVNAKAPFF--IIQQALSRLRDNSRIINISSAAtriSL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 156 QYFfnVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknentDDPLLKQLRSNFSS 225
Cdd:PRK12747  153 PDF--IAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELL------SDPMMKQYATTISA 214
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 9-155 8.79e-18

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 80.50  E-value: 8.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLfEQVDQEQQGRLDV 88
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERA-ADTAVERFGRIDT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952775749  89 LVNNayAGVPAIMKninkaFWESPASIWDDINNVGLRGHylcsVYGARLMVP----AGQGLIVVISSIGGL 155
Cdd:cd05360    81 WVNN--AGVAVFGR-----FEDVTPEEFRRVFDVNYLGH----VYGTLAALPhlrrRGGGALINVGSLLGY 140
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 1-198 1.13e-17

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 80.93  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGR-HMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVD 79
Cdd:PRK08936    1 MYSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  80 QEqQGRLDVLVNNAYAGVPAIMKninkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIG-GLQY 157
Cdd:PRK08936   81 KE-FGTLDVMINNAGIENAVPSH-------EMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkGNIINMSSVHeQIPW 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952775749 158 FFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK08936  153 PLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 5-244 1.62e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 80.72  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlqatAEEAQSRGGqcVP-VVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK06179    2 SNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRN-------PARAAPIPG--VElLELDVTDDASVQAAVDEV-IARA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGV--PAIMKNINKAfwespASIWdDINNVGLrghylcsVYGARLMVP----AGQGLIVVISSI-GGLQ 156
Cdd:PRK06179   72 GRIDVLVNNAGVGLagAAEESSIAQA-----QALF-DTNVFGI-------LRMTRAVLPhmraQGSGRIINISSVlGFLP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 157 YFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELvkevVVKNENTDDPL----------LKQLRSNFSSA 226
Cdd:PRK06179  139 APYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF----DANAPEPDSPLaeydreravvSKAVAKAVKKA 214

                         250
                  ....*....|....*...
gi 1952775749 227 ETTEMSGKCVVALATDPN 244
Cdd:PRK06179  215 DAPEVVADTVVKAALGPW 232
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-199 1.97e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 80.71  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK08277    7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI-LEDF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVP-AIMKNIN-------KAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGL 155
Cdd:PRK08277   86 GPCDILINGAGGNHPkATTDNEFhelieptKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAF 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 156 QYFFNV-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK08277  166 TPLTKVpAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-258 2.18e-17

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 80.20  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQg 84
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEirRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpAIMKninkafweSPASIWDD-------INNVglrGHYLCSVYGARLMVPAGQGLIVVISSI---GG 154
Cdd:cd09807    80 RLDVLINNA-----GVMR--------CPYSKTEDgfemqfgVNHL---GHFLLTNLLLDLLKKSAPSRIVNVSSLahkAG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 155 LQYF----FNVSYGVGKAAC-DRLA-----ADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTdDPLLKQLRSNFs 224
Cdd:cd09807   144 KINFddlnSEKSYNTGFAYCqSKLAnvlftRELARRLQGTGVTVNALHPGVVRTELGRHTGIHHLFL-STLLNPLFWPF- 221

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1952775749 225 sAETTEMSGKCVVALATDPNILSLSGKVLPSCDL 258
Cdd:cd09807   222 -VKTPREGAQTSIYLALAEELEGVSGKYFSDCKL 254
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 5-204 2.91e-17

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 79.37  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGAT-VYITGRHMDTLQATAEEAQSRggqCVPVVCDSSQESEVQRLFEQVDQeqq 83
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGDK---VVPLRLDVTDPESIKAAAAQAKD--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 grLDVLVNNayAGVpAIMKNINKAFWESPASIWDDINNVGLRGhyLCSVYgARLMVPAGQGLIVVISSIGGLQYFFNVS- 162
Cdd:cd05354    75 --VDVVINN--AGV-LKPATLLEEGALEALKQEMDVNVFGLLR--LAQAF-APVLKANGGGAIVNLNSVASLKNFPAMGt 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd05354   147 YSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGA 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-242 5.06e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 79.06  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTlqaTAEEAQSRGGQCVPvvCDSSQESEVQRLFEQVdQ 80
Cdd:PRK06463    1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKGVFTIK--CDVGNRDQVKKSKEVV-E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNayAGVPAIMkninkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGL----- 155
Cdd:PRK06463   75 KEFGRVDVLVNN--AGIMYLM-----PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaae 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 156 -QYFfnvsYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELvkevVVKNENTDDplLKQLRSNFSSAETTEMSGK 234
Cdd:PRK06463  148 gTTF----YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM----TLSGKSQEE--AEKLRELFRNKTVLKTTGK 217

                         250
                  ....*....|....
gi 1952775749 235 ------CVVALATD 242
Cdd:PRK06463  218 pedianIVLFLASD 231
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-186 5.39e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 79.83  E-value: 5.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVyITGRHMDTLQA--TAEEAQSRGGQCVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK07792    6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATV-VVNDVASALDAsdVLDEIRAAGAKAVAVAGDISQRATADELVATA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 DqeQQGRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGA---RLMVPAGQ----GLIVVISS 151
Cdd:PRK07792   85 V--GLGGLDIVVNNA-----GITR--DRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGgpvyGRIVNTSS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 152 IGGL-----QyffnVSYGVGKAACDRLAADCAQELRRHGV 186
Cdd:PRK07792  156 EAGLvgpvgQ----ANYGAAKAGITALTLSAARALGRYGV 191
PRK05650 PRK05650
SDR family oxidoreductase;
11-200 6.11e-17

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 78.93  E-value: 6.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRlFEQVDQEQQGRLDVLV 90
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTA-LAQACEEKWGGIDVIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  91 NNayAGVPAimkniNKAFWESPASIWD---DINNVGLrghylcsVYGARLMVPA----GQGLIVVISSIGGL-QYFFNVS 162
Cdd:PRK05650   83 NN--AGVAS-----GGFFEELSLEDWDwqiAINLMGV-------VKGCKAFLPLfkrqKSGRIVNIASMAGLmQGPAMSS 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK05650  149 YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNL 186
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 1-200 6.48e-17

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 78.67  E-value: 6.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSrggqCVPVVCDSSQESEVQRLFEQVdq 80
Cdd:cd05351     1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG----IEPVCVDLSDWDATEEALGSV-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 eqqGRLDVLVNNayAGVPaimknINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSIGGLQYFF 159
Cdd:cd05351    75 ---GPVDLLVNN--AAVA-----ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALT 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 160 NVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05351   145 NHTvYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-194 6.63e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 78.85  E-value: 6.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK07890    3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALA-LERFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAgVPAiMKNINKAFWESpasiWDDINNVglrghylcSVYGA----RLMVPA---GQGLIVVISS--IGGL 155
Cdd:PRK07890   82 RVDALVNNAFR-VPS-MKPLADADFAH----WRAVIEL--------NVLGTlrltQAFTPAlaeSGGSIVMINSmvLRHS 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 156 QYFFNvSYGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:PRK07890  148 QPKYG-AYKMAKGALLAASQSLATELGPQGIRVNSVAPG 185
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-204 8.63e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 78.53  E-value: 8.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVDqEQQG 84
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAV-ERFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpAI--MKNINKAFWESpasiWDDINNVGLRGHYLCSVYGARLMVPAGQG-LIVVISSIGGLQYFFNV 161
Cdd:PRK07067   80 GIDILFNNA-----ALfdMAPILDISRDS----YDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 162 S-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK07067  151 ShYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV 194
PRK06949 PRK06949
SDR family oxidoreductase;
1-200 9.07e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 78.27  E-value: 9.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAAS--MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK06949    1 MGRSinLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 DQEqQGRLDVLVNNayAGVPAIMKNINKafweSPASiWDDINNVGLRGHYLCSVYGARLMV--------PAGQGLIVVIS 150
Cdd:PRK06949   81 ETE-AGTIDILVNN--SGVSTTQKLVDV----TPAD-FDFVFDTNTRGAFFVAQEVAKRMIarakgagnTKPGGRIINIA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952775749 151 SIGGLQYFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK06949  153 SVAGLRVLPQIGlYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-201 1.25e-16

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 77.95  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMdtlqatAEEAQSRGgqcvpVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE------PSYNDVDY-----FKVDVSNKEQVIKGIDYV-ISKYG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNA----YAGVPAImkninkafwesPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:PRK06398   72 RIDILVNNAgiesYGAIHAV-----------EEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRN 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1952775749 161 VS-YGVGKAA----CDRLAADCAQELRRHGVSyvslwPGMVQTELV 201
Cdd:PRK06398  141 AAaYVTSKHAvlglTRSIAVDYAPTIRCVAVC-----PGSIRTPLL 181
PRK09072 PRK09072
SDR family oxidoreductase;
6-93 1.56e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 77.67  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaQSRGGQCVPVVCDSSQESEVQRLFEQVdqEQQGR 85
Cdd:PRK09072    4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAAR-LPYPGRHRWVVADLTSEAGREAVLARA--REMGG 80


                  ....*...
gi 1952775749  86 LDVLVNNA 93
Cdd:PRK09072   81 INVLINNA 88
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-241 2.12e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 78.09  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGqCVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:PRK05872    6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDR-VLTVVADVTDLAAMQAAAEEAV-ERF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESPAsiwdDINNVGlrghylcSVYGARLMVPA---GQGLIVVISSiggLQYFFN 160
Cdd:PRK05872   84 GGIDVVVANAGIASGGSVAQVDPDAFRRVI----DVNLLG-------VFHTVRATLPAlieRRGYVLQVSS---LAAFAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 161 V----SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVvvkneNTDDPLLKQLRSNFS-SAETTEMSGKC 235
Cdd:PRK05872  150 ApgmaAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDA-----DADLPAFRELRARLPwPLRRTTSVEKC 224


                  ....*.
gi 1952775749 236 VVALAT 241
Cdd:PRK05872  225 AAAFVD 230
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-215 2.82e-16

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 77.17  E-value: 2.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVpVVCDSSQESEVQRlfeQVD--QEQQG 84
Cdd:PLN02253   18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCF-FHCDVTVEDDVSR---AVDftVDKFG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNINKAFwespaSIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIV----VISSIGGLQYFfn 160
Cdd:PLN02253   94 TLDIMVNNAGLTGPPCPDIRNVEL-----SEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVslcsVASAIGGLGPH-- 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 161 vSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDPL 215
Cdd:PLN02253  167 -AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDAL 220
PRK06114 PRK06114
SDR family oxidoreductase;
4-211 6.56e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 75.97  E-value: 6.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDT-LQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEq 82
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAE- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVpaimKNINKAFwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG-------L 155
Cdd:PRK06114   84 LGALTLAVNA--AGI----ANANPAE-EMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGiivnrglL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952775749 156 QYFFNVSygvgKAACDRLAADCAQELRRHGVSYVSLWPGMVQT------ELVKEVVVKNENT 211
Cdd:PRK06114  157 QAHYNAS----KAGVIHLSKSLAMEWVGRGIRVNSISPGYTATpmntrpEMVHQTKLFEEQT 214
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 3-203 7.36e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 75.74  E-value: 7.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:PRK07478    2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALA-VER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVPAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFF--N 160
Cdd:PRK07478   81 FGGLDIAFNN--AGTLGEMGPVA----EMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFpgM 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK07478  155 AAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRA 197
PRK06194 PRK06194
hypothetical protein; Provisional
 6-198 7.88e-16

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 76.21  E-value: 7.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:PRK06194    5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAA-LERFGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVPAIMkninkafWESPASIWDDINNVGLRGhylcSVYGARLMVP----------AGQGLIVVISSIGGL 155
Cdd:PRK06194   84 VHLLFNNAGVGAGGLV-------WENSLADWEWVLGVNLWG----VIHGVRAFTPlmlaaaekdpAYEGHIVNTASMAGL 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 156 QYFFNVS-YGVGKAAC----DRLAADCAQELRRHGVSYvsLWPGMVQT 198
Cdd:PRK06194  153 LAPPAMGiYNVSKHAVvsltETLYQDLSLVTDQVGASV--LCPYFVPT 198
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 5-193 9.84e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 75.86  E-value: 9.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYI---------TGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLf 75
Cdd:PRK07791    4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  76 eqVDQ--EQQGRLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGA---RLMVPAGQGL---IV 147
Cdd:PRK07791   83 --VDAavETFGGLDVLVNNA-----GILR--DRMIANMSEEEWDAVIAVHLKGHFATLRHAAaywRAESKAGRAVdarII 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952775749 148 VISSIGGLQYffNV---SYGVGKAACDRLAADCAQELRRHGVSYVSLWP 193
Cdd:PRK07791  154 NTSSGAGLQG--SVgqgNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-220 9.93e-16

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 75.27  E-value: 9.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd08936     8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA-VNLHG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpaimknINKAFW----ESPASIWDDINNVGLRGHYLCSvygaRLMVPA----GQGLIVVISSIGGLQ 156
Cdd:cd08936    87 GVDILVSNA----------AVNPFFgnilDSTEEVWDKILDVNVKATALMT----KAVVPEmekrGGGSVVIVSSVAAFH 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 157 YFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKeVVVKNENTDDPLLKQLR 220
Cdd:cd08936   153 PFPGLGpYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSS-ALWMDKAVEESMKETLR 216
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 6-218 1.97e-15

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 74.63  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYItgrhMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALA-KAKFGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNayAGVPAIMKNIN-KAFWESPASIWDDINNVGLRGHYLCSVYGARLMV-----PAGQ-GLIVVISSIGGlqyf 158
Cdd:cd05371    76 LDIVVNC--AGIAVAAKTYNkKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGknepdQGGErGVIINTASVAA---- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 159 F-----NVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTddpLLKQ 218
Cdd:cd05371   150 FegqigQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDF---LAKQ 211
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 5-254 3.28e-15

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 74.09  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRG--GQCVPVVCDSSQESEVQRlFEQVDQEQ 82
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEA-YVDATVEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVPAiMKNINKAFwesPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNVS 162
Cdd:cd05330    80 FGRIDGFFNN--AGIEG-KQNLTEDF---GADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 163 -YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEvVVKNENTDDPllKQLRSNFSSAETTEMSGK-----CV 236
Cdd:cd05330   154 gYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEG-SLKQLGPENP--EEAGEEFVSVNPMKRFGEpeevaAV 230

                         250
                  ....*....|....*....
gi 1952775749 237 VA-LATDPNILsLSGKVLP 254
Cdd:cd05330   231 VAfLLSDDAGY-VNAAVVP 248
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 7-186 3.82e-15

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 75.72  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQ--CVPVVCDSSQESEVQRLFEQVDQEQQG 84
Cdd:COG3347   425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGAdaVDATDVDVTAEAAVAAAFGFAGLDIGG 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAImkninkafWESPASIWDDINNVGLRGHYLCSVYGARLMvpAGQGLIVVISSIGGLQyFFNVSYG 164
Cdd:COG3347   505 SDIGVANAGIASSSPE--------EETRLSFWLNNFAHLSTGQFLVARAAFQGT--GGQGLGGSSVFAVSKN-AAAAAYG 573

                         170       180
                  ....*....|....*....|....*..
gi 1952775749 165 VGKAACD-----RLAADCAQELRRHGV 186
Cdd:COG3347   574 AAAAATAkaaaqHLLRALAAEGGANGI 600
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 4-199 6.75e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 73.41  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK06180    1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALH---PDRALARLLDVTDFDAIDAVVADAEAT-F 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKninkafwESPASiwddinnvGLRGHYLCSVYGARLMVPA--------GQGLIVVISSIGGL 155
Cdd:PRK06180   77 GPIDVLVNNAGYGHEGAIE-------ESPLA--------EMRRQFEVNVFGAVAMTKAvlpgmrarRRGHIVNITSMGGL 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749 156 QYFFNVSYGVG-KAACDRLAADCAQELRRHGVSYVSLWPG----------MVQTE 199
Cdd:PRK06180  142 ITMPGIGYYCGsKFALEGISESLAKEVAPFGIHVTAVEPGsfrtdwagrsMVRTP 196
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-203 6.78e-15

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 73.00  E-value: 6.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITgrHMDTlQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA--DIDE-ERGADFAEAEGPNLFFVHGDVADETLVKFVVYAM-LEKLGRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAYAGVPAIMKninkafwESPASIWDDINNVGLRGHYLCSVYGARLMVpAGQGLIVVISSIGGLQYFFNV-SYGV 165
Cdd:cd09761    77 DVLVNNAARGSKGILS-------SLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSeAYAA 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 166 GKAACDRLAADCAQELRRHgVSYVSLWPGMVQTELVKE 203
Cdd:cd09761   149 SKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQE 185
PRK07831 PRK07831
SDR family oxidoreductase;
5-148 9.82e-15

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 72.76  E-value: 9.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGAS-RGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQVdQE 81
Cdd:PRK07831   15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADElaAELGLGRVEAVVCDVTSEAQVDALIDAA-VE 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952775749  82 QQGRLDVLVNNAYAGVpaimkniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVV 148
Cdd:PRK07831   94 RLGRLDVLVNNAGLGG-------QTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIV 153
PRK08264 PRK08264
SDR family oxidoreductase;
4-213 1.13e-14

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 72.23  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGAT-VYITGRHMDTLQAtaeeaqsRGGQCVPVVCDSSQESEVQRLFEQVdqeq 82
Cdd:PRK08264    3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVTD-------LGPRVVPLQLDVTDPASVAAAAEAA---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 qGRLDVLVNNayAGVpaimkninkafwESPASIWDDINNVGLRGHYLCSVYG----ARLMVPA----GQGLIVVISSIGG 154
Cdd:PRK08264   72 -SDVTILVNN--AGI------------FRTGSLLLEGDEDALRAEMETNYFGplamARAFAPVlaanGGGAIVNVLSVLS 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 155 LQYF-FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDD 213
Cdd:PRK08264  137 WVNFpNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAPKASPAD 196
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 6-242 1.50e-14

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 71.73  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITgrhmdTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqeqqgR 85
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIAT-----DINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEG-----R 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNayAGVPAImkninKAFWESPASIWDDINNVGLRGHYLcsVYGARL--MVPAGQGLIVVISSIGGlqYFFNV-- 161
Cdd:cd05368    71 IDVLFNC--AGFVHH-----GSILDCEDDDWDFAMNLNVRSMYL--MIKAVLpkMLARKDGSIINMSSVAS--SIKGVpn 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 162 --SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTD----DPLLKQLRSNFSSAEttEMSGKC 235
Cdd:cd05368   140 rfVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEealkAFAARQPLGRLATPE--EVAALA 217


                  ....*..
gi 1952775749 236 VVaLATD 242
Cdd:cd05368   218 VY-LASD 223
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-204 1.90e-14

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 71.64  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVY-ITGRHMDTLQATAEEaqsRGGQCVPVVCDSSQESEVQRLFEQV-DQEQQGRLD- 87
Cdd:PRK06924    5 IITGTSQGLGEAIANQLLEKGTHVIsISRTENKELTKLAEQ---YNSNLTFHSLDLQDVHELETNFNEIlSSIQEDNVSs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 -VLVNNayAGVPAIMKNINKAFWESpasiwddinnvgLRGHY---------LCSVYGARLMVPAGQGLIVVISSIGGLQ- 156
Cdd:PRK06924   82 iHLINN--AGMVAPIKPIEKAESEE------------LITNVhlnllapmiLTSTFMKHTKDWKVDKRVINISSGAAKNp 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 157 YFFNVSYGVGKAACDRL--AADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK06924  148 YFGWSAYCSSKAGLDMFtqTVATEQEEEEYPVKIVAFSPGVMDTNMQAQI 197
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-213 1.99e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 71.68  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGR 85
Cdd:PRK08643    1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQV-VDTFGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVPAIMKNINKafwespaSIWDDINNVGLRGhylcSVYGARLMVPA----GQ-GLIVVISSIGGLQYFFN 160
Cdd:PRK08643   80 LNVVVNNAGVAPTTPIETITE-------EQFDKVYNINVGG----VIWGIQAAQEAfkklGHgGKIINATSQAGVVGNPE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952775749 161 VS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV---VVKNENTDD 213
Cdd:PRK08643  149 LAvYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIahqVGENAGKPD 205
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 5-198 2.03e-14

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 71.45  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG---QCVPVVCDSSQESEVQRLFEQVDQE 81
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGrqpQWFILDLLTCTSENCQQLAQRIAVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 qQGRLD-VLVNNAYAGVPAIMKninkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN 160
Cdd:cd05340    82 -YPRLDgVLHNAGLLGDVCPLS-------EQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 161 V-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:cd05340   154 WgAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK06139 PRK06139
SDR family oxidoreductase;
1-154 2.37e-14

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 72.45  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK06139    1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQA-A 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749  81 EQQGRLDVLVNNayAGVPAIMKninkaFWESPASIWDDINNVGLRGHylcsVYGARLMVP----AGQGLIVVISSIGG 154
Cdd:PRK06139   80 SFGGRIDVWVNN--VGVGAVGR-----FEETPIEAHEQVIQTNLIGY----MRDAHAALPifkkQGHGIFINMISLGG 146
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-203 2.77e-14

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 71.27  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd05345     2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI---GEAAIAIQADVTKRADVEAMVEAA-LSKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpaimKNINKAFWESPASIWDDINNVGLRGHYLcsvyGARLMVP----AGQGLIVVISSIGGLQ--- 156
Cdd:cd05345    78 GRLDILVNN--AGI----THRNKPMLEVDEEEFDRVFAVNVKSIYL----SAQALVPhmeeQGGGVIINIASTAGLRprp 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952775749 157 --YFFNVSYGVGKAACDRLAAdcaqELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:cd05345   148 glTWYNASKGWVVTATKAMAV----ELAPRNIRVNCLCPVAGETPLLSM 192
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-198 5.33e-14

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 70.29  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATvyITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK08993    7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCD--IVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE-F 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNayAGVpaIMKNINKAFWESPasiWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQYFFNV- 161
Cdd:PRK08993   84 GHIDILVNN--AGL--IRREDAIEFSEKD---WDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVp 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK08993  157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 5-200 5.60e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 70.84  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaqsRGGQCVPVVCDSSQESEVqrlFEQVDQ--EQ 82
Cdd:PRK08263    1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEK---YGDRLLPLALDVTDRAAV---FAAVETavEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNA-YAGVPAImkninKAFWESPAsiwddinnvglRGHYLCSVYGARLMVPA--------GQGLIVVISSIG 153
Cdd:PRK08263   75 FGRLDIVVNNAgYGLFGMI-----EEVTESEA-----------RAQIDTNFFGALWVTQAvlpylreqRSGHIIQISSIG 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 154 GLQYFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK08263  139 GISAFPMSGiYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDW 186
PRK09134 PRK09134
SDR family oxidoreductase;
8-93 6.06e-14

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 70.34  E-value: 6.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYI-TGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK09134   10 RAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARA-SAALGPI 88


                  ....*..
gi 1952775749  87 DVLVNNA 93
Cdd:PRK09134   89 TLLVNNA 95
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-194 6.81e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 70.42  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEeaqSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:PRK08265    2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAA---SLGERARFIATDITDDAAIERAVATV-VAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNAYAGVPAIMKninkafweSPASIWDDINNVGLRGHYLcSVYGARLMVPAGQGLIVVISSIGGlqyffNVS 162
Cdd:PRK08265   78 FGRVDILVNLACTYLDDGLA--------SSRADWLAALDVNLVSAAM-LAQAAHPHLARGGGAIVNFTSISA-----KFA 143

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 163 ------YGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:PRK08265  144 qtgrwlYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-199 8.67e-14

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 69.93  E-value: 8.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATvyITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGAD--IVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQA-VEVMG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVpaIMKNINKAFWESPasiWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQYFFNV-S 162
Cdd:PRK12481   83 HIDILINN--AGI--IRRQDLLEFGNKD---WDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVpS 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK12481  156 YTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK08628 PRK08628
SDR family oxidoreductase;
1-186 1.31e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 69.22  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLqATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK08628    1 MDLNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDD-EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQT-V 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNA--------YAGVPAIMKNINKAFWespasiwddinnvglrgHYLCSVYGARLMVPAGQGLIVVISSI 152
Cdd:PRK08628   79 AKFGRIDGLVNNAgvndgvglEAGREAFVASLERNLI-----------------HYYVMAHYCLPHLKASRGAIVNISSK 141

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1952775749 153 GGLQYFFNVS-YGVGKAACDRLAADCAQELRRHGV 186
Cdd:PRK08628  142 TALTGQGGTSgYAAAKGAQLALTREWAVALAKDGV 176
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-199 1.43e-13

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 69.02  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEA---GERAIAIQADVRDRDQVQAMIEEA-KNHFGPV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNAYAGVPaIMKNINKAFWESPasiWDDINN---VGLRGHYLCSVYGARLMVPAGQGLIVVISS---IGGLQYFFN 160
Cdd:cd05349    77 DTIVNNALIDFP-FDPDQRKTFDTID---WEDYQQqleGAVKGALNLLQAVLPDFKERGSGRVINIGTnlfQNPVVPYHD 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 161 vsYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05349   153 --YTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-199 1.76e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 68.92  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPV-VCDSSQESEVQRLFEQVd 79
Cdd:PRK06125    1 MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVhALDLSSPEAREQLAAEA- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  80 qeqqGRLDVLVNNAYAgVPA-IMKNINKAFWESPasiWDdinnVGLRGH-YLCSVYGARlMVPAGQGLIVVISSIGGLQY 157
Cdd:PRK06125   80 ----GDIDILVNNAGA-IPGgGLDDVDDAAWRAG---WE----LKVFGYiDLTRLAYPR-MKARGSGVIVNVIGAAGENP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 158 FFNvsYGVGKAACDRLAA-DCA--QELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06125  147 DAD--YICGSAGNAALMAfTRAlgGKSLDDGVRVVGVNPGPVATD 189
PRK05866 PRK05866
SDR family oxidoreductase;
5-202 2.02e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 69.39  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK05866   38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADV-EKRIG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAyagvpaiMKNINKAFWESpASIWDDINNVGLRGHY--LCSVYG-ARLMVPAGQGLIVVISSIG---GLQYF 158
Cdd:PRK05866  117 GVDILINNA-------GRSIRRPLAES-LDRWHDVERTMVLNYYapLRLIRGlAPGMLERGDGHIINVATWGvlsEASPL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 159 FNVsYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK05866  189 FSV-YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIA 231
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-93 2.14e-13

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 68.86  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYIT--GRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEq 82
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKE- 102

                          90
                  ....*....|.
gi 1952775749  83 QGRLDVLVNNA 93
Cdd:cd05355   103 FGKLDILVNNA 113
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-204 2.40e-13

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 68.41  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI---GPAACAISLDVTDQASIDRCVAAL-VDRWG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAgvpAIMKNINKAFWESpasiWDDINNVGLRGHYLCSVYGARLMVPAGQ-GLIVVISSIGGLQYFFNVS- 162
Cdd:cd05363    77 SIDILVNNAAL---FDLAPIVDITRES----YDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMASQAGRRGEALVGv 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:cd05363   150 YCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGV 191
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 7-203 2.58e-13

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 68.50  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGR-----HMDTLQATAEE----AQSRGGQCVPVVCDSSQESEVQRLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRAEldavAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  78 VdQEQQGRLDVLVNNA---YAGVPAimkninkafWESPASIWDDINNVGLRGhylcsVYG-ARLMVPA-------GQGLI 146
Cdd:TIGR04504  81 A-VERWGRLDAAVAAAgviAGGRPL---------WETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952775749 147 VVISSIGGLQYFFNV-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:TIGR04504 146 VAVASAAATRGLPHLaAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 12-200 4.20e-13

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 67.16  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGgqcvpVVCDSSQESEVQRLFEQVdqeqqGRLDVLVN 91
Cdd:cd11730     3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA-----RPADVAAELEVWALAQEL-----GPLDLLVY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NAYAGVPaimkninKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIvvissIGGLQYFFNV----SYGVGK 167
Cdd:cd11730    73 AAGAILG-------KPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVF-----LGAYPELVMLpglsAYAAAK 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 168 AACDRLAADCAQELRrhGVSYVSLWPGMVQTEL 200
Cdd:cd11730   141 AALEAYVEVARKEVR--GLRLTLVRPPAVDTGL 171
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 4-214 4.31e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 67.87  E-value: 4.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQ 83
Cdd:PRK07523    7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAE-I 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNInkafwesPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSI-GGLQYFFNVS 162
Cdd:PRK07523   86 GPIDILVNNAGMQFRTPLEDF-------PADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVqSALARPGIAP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVvknentDDP 214
Cdd:PRK07523  159 YTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALV------ADP 204
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 6-199 7.91e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 67.24  E-value: 7.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHM-DTLQATAEEaqsrggqcvpVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:PRK06523    8 AGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRpDDLPEGVEF----------VAADLTTAEGCAAVARAV-LERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYA------GVPAImkninkafwesPASIWDDINNVGLrghyLCSVYGARLMVPA----GQGLIVVISSIGG 154
Cdd:PRK06523   77 GVDILVHVLGGssapagGFAAL-----------TDEEWQDELNLNL----LAAVRLDRALLPGmiarGSGVIIHVTSIQR 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1952775749 155 L--QYFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06523  142 RlpLPESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK09291 PRK09291
SDR family oxidoreductase;
7-198 8.51e-13

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 66.95  E-value: 8.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAG----ATVYITGrhmdtlQATA--EEAQSRGGqcvpvvcdssqESEVQRL--FEQV 78
Cdd:PRK09291    2 SKTILITGAGSGFGREVALRLARKGhnviAGVQIAP------QVTAlrAEAARRGL-----------ALRVEKLdlTDAI 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 DQEQQGRL--DVLVNNAYAGVPAimkninkAFWESPASIwddinnvgLRGHYLCSVYG--------ARLMVPAGQGLIVV 148
Cdd:PRK09291   65 DRAQAAEWdvDVLLNNAGIGEAG-------AVVDIPVEL--------VRELFETNVFGpleltqgfVRKMVARGKGKVVF 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952775749 149 ISSIGGLQYFFNV-SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK09291  130 TSSMAGLITGPFTgAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-200 8.85e-13

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 66.83  E-value: 8.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVyiTGrhMDTlqataEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK08220    2 NAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKV--IG--FDQ-----AFLTQEDYPFATFVLDVSDAAAVAQVCQRL-L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNayAGVPAiMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGlqyffN 160
Cdd:PRK08220   72 AETGPLDVLVNA--AGILR-MGATD----SLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAA-----H 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 161 V------SYGVGKAACDRLAADCAQELRRHGV--SYVSlwPGMVQTEL 200
Cdd:PRK08220  140 VprigmaAYGASKAALTSLAKCVGLELAPYGVrcNVVS--PGSTDTDM 185
PRK07806 PRK07806
SDR family oxidoreductase;
3-101 1.20e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 66.28  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGR-HMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQE 81
Cdd:PRK07806    2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTA-RE 80

                          90       100
                  ....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNAYAGVPAIM 101
Cdd:PRK07806   81 EFGGLDALVLNASGGMESGM 100
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 6-194 2.21e-12

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 65.95  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSR-GGQCVPVVCDSSQESEVQRLFEQVDQEqQG 84
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEI-FK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNInkafwesPASIWDDINNVGLRGHYLCSVYGARLMVPAG-QGLIVVISSIGG-LQYFFNVS 162
Cdd:cd05322    80 RVDLLVYSAGIAKSAKITDF-------ELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGkVGSKHNSG 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPG 194
Cdd:cd05322   153 YSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
PRK05693 PRK05693
SDR family oxidoreductase;
8-202 6.55e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 64.81  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaqsrGGQCVPVvcDSSQESEVQRLFEQVDQEQQGrLD 87
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA----GFTAVQL--DVNDGAALARLAEELEAEHGG-LD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNA-YAGVPAIMkninkafwespasiwdDINNVGLRGHYLCSVYG----ARLMVPA---GQGLIVVISSIGG-LQYF 158
Cdd:PRK05693   75 VLINNAgYGAMGPLL----------------DGGVEAMRRQFETNVFAvvgvTRALFPLlrrSRGLVVNIGSVSGvLVTP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 159 FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK05693  139 FAGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK12742 PRK12742
SDR family oxidoreductase;
6-200 7.36e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 64.01  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITgrHMDTLQATAEEAQSRGGQCVPVvcDSSQESEVqrlFEQVDQEqqGR 85
Cdd:PRK12742    5 TGKKVLVLGGSRGIGAAIVRRFVTDGANVRFT--YAGSKDAAERLAQETGATAVQT--DSADRDAV---IDVVRKS--GA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVPAIMKNINKafwespasiwDDIN---NVGLRGHYLCSVYGARLMVPAGQglIVVISSIGGLQYFFN-- 160
Cdd:PRK12742   76 LDILVVNAGIAVFGDALELDA----------DDIDrlfKINIHAPYHASVEAARQMPEGGR--IIIIGSVNGDRMPVAgm 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK12742  144 AAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK08703 PRK08703
SDR family oxidoreductase;
4-98 8.03e-12

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 63.80  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQ---CVPVVCDSSQESEVQRLFEQVDQ 80
Cdd:PRK08703    3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPepfAIRFDLMSAEEKEFEQFAATIAE 82

                          90       100
                  ....*....|....*....|.
gi 1952775749  81 EQQGRLDVLVNNA---YAGVP 98
Cdd:PRK08703   83 ATQGKLDGIVHCAgyfYALSP 103
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-214 8.70e-12

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 64.02  E-value: 8.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLC---QAGATVYITGRHMDTLQATAEEAQSRGGQCVPV----VCDSsqESEVQrlfeQVDQ 80
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETlqldVCDS--KSVAA----AVER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQGRLDVLVNNAYAGVPAIMKNINKafwespasiwDDINNVglrghYLCSVYGARLMVPA--------GQGLIVVISSI 152
Cdd:cd09806    75 VTERHVDVLVCNAGVGLLGPLEALSE----------DAMASV-----FDVNVFGTVRMLQAflpdmkrrGSGRILVTSSV 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 153 GGLQ-YFFNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEVVVKNENTDDP 214
Cdd:cd09806   140 GGLQgLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDR 202
PRK09135 PRK09135
pteridine reductase; Provisional
 4-193 1.54e-11

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 63.41  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRH-MDTLQATAEE-AQSRGGQCVPVVCDSSQESEVQRLFEQVDQe 81
Cdd:PRK09135    3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAElNALRPGSAAALQADLLDPDALPELVAACVA- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNAYAGVPAIMKNINKAfwespasIWDDINNVGLRGHYLCSVYGARLMVPAgQGLIVVISSIGGLQYFFN- 160
Cdd:PRK09135   82 AFGRLDALVNNASSFYPTPLGSITEA-------QWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHAERPLKGy 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 161 VSYGVGKAA----CDRLAADCAQELRRHGVSY-VSLWP 193
Cdd:PRK09135  154 PVYCAAKAAlemlTRSLALELAPEVRVNAVAPgAILWP 191
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-198 1.62e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 63.27  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKGKVCVVTGASR--GIGRGIALQLCQAGATVYIT-----------GRHMDTLQATAEEAQSRGGQCVPVVCDSSQES 69
Cdd:PRK12859    2 NQLKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTywtaydkempwGVDQDEQIQLQEELLKNGVKVSSMELDLTQND 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  70 EVQRLFEQVdQEQQGRLDVLVNNAYAGVPAIMKNINkafwespASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVI 149
Cdd:PRK12859   82 APKELLNKV-TEQLGYPHILVNNAAYSTNNDFSNLT-------AEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINM 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 150 SSIGGLQYF-FNVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK12859  154 TSGQFQGPMvGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDT 203
PRK08219 PRK08219
SDR family oxidoreductase;
5-205 1.75e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 62.64  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLcQAGATVYITGRHMDTLQATAEEAQSrggqCVPVVCDSSQESEVQRLFEQVDqeqqg 84
Cdd:PRK08219    1 MERPTALITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAAELPG----ATPFPVDLTDPEAIAAAVEQLG----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVpAIMKNINkafwESPASIWddinnvglRGHYLCSVYGA----RLMVP---AGQGLIVVISSIGGLQ- 156
Cdd:PRK08219   71 RLDVLVHN--AGV-ADLGPVA----ESTVDEW--------RATLEVNVVAPaeltRLLLPalrAAHGHVVFINSGAGLRa 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 157 YFFNVSYGVGK----AACDRLAADCAQELRrhgVSyvSLWPGMVQTELVKEVV 205
Cdd:PRK08219  136 NPGWGSYAASKfalrALADALREEEPGNVR---VT--SVHPGRTDTDMQRGLV 183
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 12-200 2.00e-11

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 62.87  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVyiTGrhmdtLQATAEEAQSRGGQCVPVVCDSSQESEVQrlfEQVDQ--EQQGRLDVL 89
Cdd:cd05331     3 VTGAAQGIGRAVARHLLQAGATV--IA-----LDLPFVLLLEYGDPLRLTPLDVADAAAVR---EVCSRllAEHGPIDAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  90 VNnaYAGVpAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFNV-SYGVGKA 168
Cdd:cd05331    73 VN--CAGV-LRPGATD----PLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMaAYGASKA 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1952775749 169 ACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd05331   146 ALASLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
PRK06720 PRK06720
hypothetical protein; Provisional
 1-93 4.06e-11

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 60.76  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEqVDQ 80
Cdd:PRK06720   10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVIS-ITL 88

                          90
                  ....*....|...
gi 1952775749  81 EQQGRLDVLVNNA 93
Cdd:PRK06720   89 NAFSRIDMLFQNA 101
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 8-193 4.08e-11

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 61.91  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYItgrHMDTLQATAEEAQ----SRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVV---HYNRSEAEAQRLKdelnALRNSAVLVQADLSDFAACADLVAAA-FRAF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPaimkniNKAFwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFFN-VS 162
Cdd:cd05357    77 GRCDVLVNNASAFYP------TPLG-QGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGyFA 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 163 YGVGKAACDRL----AADCAQELRRHGVSY-VSLWP 193
Cdd:cd05357   150 YCMSKAALEGLtrsaALELAPNIRVNGIAPgLILLP 185
PRK07062 PRK07062
SDR family oxidoreductase;
1-93 4.78e-11

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 61.98  E-value: 4.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSR--GGQCVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK07062    2 MQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAV 81

                          90
                  ....*....|....*
gi 1952775749  79 dQEQQGRLDVLVNNA 93
Cdd:PRK07062   82 -EARFGGVDMLVNNA 95
PRK08267 PRK08267
SDR family oxidoreductase;
12-202 5.97e-11

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 61.88  E-value: 5.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAeeAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQGRLDVLVN 91
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALA--AELGAGNAWTGALDVTDRAAWDAALADFAAATGGRLDVLFN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NA---YAG------VPAIMKNInkafwespasiwdDINNVGLrghylcsVYGARLMVP----AGQGLIVVISSIGGLqyf 158
Cdd:PRK08267   84 NAgilRGGpfedipLEAHDRVI-------------DINVKGV-------LNGAHAALPylkaTPGARVINTSSASAI--- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952775749 159 fnvsYGVGkaacdRLAADCAQ-------------ELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK08267  141 ----YGQP-----GLAVYSATkfavrgltealdlEWRRHGIRVADVMPLFVDTAMLD 188
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-187 9.29e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 60.87  E-value: 9.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDtlQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQGRLD 87
Cdd:PRK08642    6 QTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSE--DAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKPIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVpaimkNINKAFWESPASI-WDDINNvGLRGhylcSVYGARL--------MVPAGQGLIVVIssigGLQYF 158
Cdd:PRK08642   84 TVVNNALADF-----SFDGDARKKADDItWEDFQQ-QLEG----SVKGALNtiqaalpgMREQGFGRIINI----GTNLF 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1952775749 159 FNV-----SYGVGKAACDRLAADCAQELRRHGVS 187
Cdd:PRK08642  150 QNPvvpyhDYTTAKAALLGLTRNLAAELGPYGIT 183
PRK08416 PRK08416
enoyl-ACP reductase;
1-202 9.95e-11

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 60.94  E-value: 9.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYIT-GRHMDTLQATAEEAQSRGG---QCVPV-VCDSSQESEvqrLF 75
Cdd:PRK08416    2 MSNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKYGikaKAYPLnILEPETYKE---LF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  76 EQVDQEQQgRLDVLVNNAYAGVPAIMKNINKAFWESPASiwddINNVglrghYLCSVY--------GARLMVPAGQGLIV 147
Cdd:PRK08416   79 KKIDEDFD-RVDFFISNAIISGRAVVGGYTKFMRLKPKG----LNNI-----YTATVNafvvgaqeAAKRMEKVGGGSII 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749 148 VISSIGGLQYFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:PRK08416  149 SLSSTGNLVYIENYAgHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALK 204
PRK07069 PRK07069
short chain dehydrogenase; Validated
 12-201 1.35e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 60.49  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITG-RHMDTLQATAEEAQSRGGQCV--PVVCDSSQESEVQRLFEQVDQEQQGrLDV 88
Cdd:PRK07069    4 ITGAAGGLGRAIARRMAEQGAKVFLTDiNDAAGLDAFAAEINAAHGEGVafAAVQDVTDEAQWQALLAQAADAMGG-LSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  89 LVNNAYAGVPAIMKNINKAFWESPASIwdDINNVglrghylcsVYGAR----LMVPAGQGLIVVISSIGGLQYFFN-VSY 163
Cdd:PRK07069   83 LVNNAGVGSFGAIEQIELDEWRRVMAI--NVESI---------FLGCKhalpYLRASQPASIVNISSVAAFKAEPDyTAY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 164 GVGKAACDRL----AADCAQelRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK07069  152 NASKAAVASLtksiALDCAR--RGLDVRCNSIHPTFIRTGIV 191
PRK06500 PRK06500
SDR family oxidoreductase;
5-200 1.50e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 60.35  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLqataEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQG 84
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASL----EAARAELGESALVIRADAGDVAAQKALAQALAEAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNINKAFwespasiWDDINNVGLRGHYLcsVYGARLMVPAGQGLIVVISSIG---GLQyffNV 161
Cdd:PRK06500   80 RLDAVFINAGVAKFAPLEDWDEAM-------FDRSFNTNVKGPYF--LIQALLPLLANPASIVLNGSINahiGMP---NS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 162 S-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK06500  148 SvYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 7-99 1.99e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 60.35  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK07576    9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI-ADEFGPI 87

                          90
                  ....*....|...
gi 1952775749  87 DVLVNNAYAGVPA 99
Cdd:PRK07576   88 DVLVSGAAGNFPA 100
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 5-122 2.03e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 59.89  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG-QCVPVVCD--SSQESEVQRLFEQVdQE 81
Cdd:PRK08945   10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGpQPAIIPLDllTATPQNYQQLADTI-EE 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952775749  82 QQGRLDVLVNNA-YAGVPAIMKNInkafwesPASIWDDINNV 122
Cdd:PRK08945   89 QFGRLDGVLHNAgLLGELGPMEQQ-------DPEVWQDVMQV 123
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-201 2.33e-10

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 60.35  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQeQQGRL 86
Cdd:PRK05876    6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFR-LLGHV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNA--YAGVPAIMKNINKAFWESPASIWDDINNVglrghylcSVYGARLMVPAGQGLIVVISSIGGLQYFFNV-SY 163
Cdd:PRK05876   85 DVVFSNAgiVVGGPIVEMTHDDWRWVIDVDLWGSIHTV--------EAFLPRLLEQGTGGHVVFTASFAGLVPNAGLgAY 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELV 201
Cdd:PRK05876  157 GVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLV 194
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-154 3.99e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 59.23  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQ---CVpVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklSL-VELDITDQESLEEFLSKS-A 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749  81 EQQGRLDVLVNNAYagvPAiMKNINKAFWE-SPASIWDDINNvGLRGHYLCSVYGARLMVPAGQGLIVVISSIGG 154
Cdd:PRK09186   79 EKYGKIDGAVNCAY---PR-NKDYGKKFFDvSLDDFNENLSL-HLGSSFLFSQQFAKYFKKQGGGNLVNISSIYG 148
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-93 4.17e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 59.66  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYIT--GRHMDTlQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQ 82
Cdd:PRK06701   44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVylDEHEDA-NETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEET-VRE 121

                          90
                  ....*....|.
gi 1952775749  83 QGRLDVLVNNA 93
Cdd:PRK06701  122 LGRLDILVNNA 132
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-204 4.42e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 58.87  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYI-TGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQq 83
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAyagvpAIMKNInkAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNVS 162
Cdd:PRK12938   80 GEIDVLVNNA-----GITRDV--VFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKgQFGQTN 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 163 YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK12938  153 YSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAI 194
PRK06914 PRK06914
SDR family oxidoreductase;
5-198 4.63e-10

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 59.27  E-value: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRggqcvpvvcDSSQESEVQRL----FEQVDQ 80
Cdd:PRK06914    1 MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQL---------NLQQNIKVQQLdvtdQNSIHN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQ-----GRLDVLVNNA-YAgvpaimkniNKAFWEspasiwdDINNVGLRGHYLCSVYGA----RLMVP----AGQGLI 146
Cdd:PRK06914   72 FQLvlkeiGRIDLLVNNAgYA---------NGGFVE-------EIPVEEYRKQFETNVFGAisvtQAVLPymrkQKSGKI 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 147 VVISSIGGLQYFFNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK06914  136 INISSISGRVGFPGLSpYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-207 5.28e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 58.93  E-value: 5.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASR--GIGRGIALQLCQAGATVYIT---------GRHMDTLQAT--AEEAQSRGGQCVPVVCDSSQESEVQR 73
Cdd:PRK12748    5 KKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmPWGMHDKEPVllKEEIESYGVRCEHMEIDLSQPYAPNR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  74 LFEQVdQEQQGRLDVLVNNAYAGVPAIMKNINkafwespASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIG 153
Cdd:PRK12748   85 VFYAV-SERLGDPSILINNAAYSTHTRLEELT-------AEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQ 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 154 GLQYFFN-VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT-----ELVKEVVVK 207
Cdd:PRK12748  157 SLGPMPDeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTgwiteELKHHLVPK 216
PRK08862 PRK08862
SDR family oxidoreductase;
5-98 6.07e-10

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 58.20  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPV-VCDSSQESeVQRLFEQVDQEQQ 83
Cdd:PRK08862    3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFqLKDFSQES-IRHLFDAIEQQFN 81

                          90
                  ....*....|....*
gi 1952775749  84 GRLDVLVNNaYAGVP 98
Cdd:PRK08862   82 RAPDVLVNN-WTSSP 95
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 5-200 1.80e-09

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 57.23  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRgGQCVPVvcDSSQESEVQRLFEQVDQEQQG 84
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGER-VKIFPA--NLSDRDEVKALGQKAEADLEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 rLDVLVNNAyagvpAIMKniNKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQ-YFFNVSY 163
Cdd:PRK12936   81 -VDILVNNA-----GITK--DGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTgNPGQANY 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK12936  153 CASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAM 189
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 3.74e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 57.15  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYItgrhMDTLQA---TAEEAQSRGGqcVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:PRK08261  210 GKVALVTGAARGIGAAIAEVLARDGAHVVC----LDVPAAgeaLAAVANRVGG--TALALDITAPDAPARIAEHLA-ERH 282

                          90
                  ....*....|
gi 1952775749  84 GRLDVLVNNA 93
Cdd:PRK08261  283 GGLDIVVHNA 292
PRK07102 PRK07102
SDR family oxidoreductase;
12-198 5.35e-09

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 55.70  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPV-VCDSSQESEVQRLFEQVdqeqQGRLD-VL 89
Cdd:PRK07102    6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSThELDILDTASHAAFLDSL----PALPDiVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  90 VNNAYAG--------VPAIMKNINKAFwESPASIWDDInnvglrghylcsvygARLMVPAGQGLIVVISSIGG-----LQ 156
Cdd:PRK07102   82 IAVGTLGdqaaceadPALALREFRTNF-EGPIALLTLL---------------ANRFEARGSGTIVGISSVAGdrgraSN 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952775749 157 YFfnvsYGVGKAAcdrLAADCA---QELRRHGVSYVSLWPGMVQT 198
Cdd:PRK07102  146 YV----YGSAKAA---LTAFLSglrNRLFKSGVHVLTVKPGFVRT 183
PRK06196 PRK06196
oxidoreductase; Provisional
 5-263 5.43e-09

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 56.23  E-value: 5.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDtlqaTAEEAqSRGGQCVPVV-CDSSQESEVQRLFEQVDQEQQ 83
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPD----VAREA-LAGIDGVEVVmLDLADLESVRAFAERFLDSGR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 gRLDVLVNNayAGVPAIMKNINKAFWESPASiwddINNVglrGHYLCSVYGARLMVPAGQGLIVVISSIG---------G 154
Cdd:PRK06196   99 -RIDILINN--AGVMACPETRVGDGWEAQFA----TNHL---GHFALVNLLWPALAAGAGARVVALSSAGhrrspirwdD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 155 LQYFFN----VSYGVGKAA-------CDRLAADcaqelrrHGVSYVSLWPGMVQTELVKEV----------VVKNENTDD 213
Cdd:PRK06196  169 PHFTRGydkwLAYGQSKTAnalfavhLDKLGKD-------QGVRAFSVHPGGILTPLQRHLpreeqvalgwVDEHGNPID 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952775749 214 PLLKqlrsnfssaeTTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYS 263
Cdd:PRK06196  242 PGFK----------TPAQGAATQVWAATSPQLAGMGGLYCEDCDIAEPTP 281
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 7-90 6.66e-09

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 55.67  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGAS--RGIGRGIALQLCQAGATVYITG---RHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVdQE 81
Cdd:cd05372     1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYqpeALRKRVEKLAERL---GESALVLPCDVSNDEEIKELFAEV-KK 76


                  ....*....
gi 1952775749  82 QQGRLDVLV 90
Cdd:cd05372    77 DWGKLDGLV 85
PRK12744 PRK12744
SDR family oxidoreductase;
4-198 8.87e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 55.13  E-value: 8.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   4 SMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEA----QSRGGQCVPVVCDSSQESEVQRLFEQVD 79
Cdd:PRK12744    5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETvaavKAAGAKAVAFQADLTTAAAVEKLFDDAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  80 QEqQGRLDVLVNnayagvpAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYFF 159
Cdd:PRK12744   85 AA-FGRPDIAIN-------TVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGKIVTLVTSLLGAFTPFY 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 160 NvSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK12744  157 S-AYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDT 194
PRK07024 PRK07024
SDR family oxidoreductase;
5-198 1.17e-08

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 54.94  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVcVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG-QCVPV-VCDSSQESEVQRLFEQvdqeQ 82
Cdd:PRK07024    1 MPLKV-FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARvSVYAAdVRDADALAAAAADFIA----A 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNNayAGVPAIMKNINKAFWESPASIWdDINNVGLRGHYLCSVYGarlMVPAGQGLIVVISSIGGlqyffnV- 161
Cdd:PRK07024   76 HGLPDVVIAN--AGISVGTLTEEREDLAVFREVM-DTNYFGMVATFQPFIAP---MRAARRGTLVGIASVAG------Vr 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1952775749 162 ------SYGVGKAA----CDRLAAdcaqELRRHGVSYVSLWPGMVQT 198
Cdd:PRK07024  144 glpgagAYSASKAAaikyLESLRV----ELRPAGVRVVTIAPGYIRT 186
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-203 1.19e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 54.77  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLqATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQG 84
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKL-KRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVN-NAYAGVPAimkninkafwESPASIWDDINNvGLRGHYLCSVYGARLMVPAGQglIVVISSIGGL--QYFFNV 161
Cdd:PRK05786   82 IDGLVVTvGGYVEDTV----------EEFSGLEEMLTN-HIKIPLYAVNASLRFLKEGSS--IVLVSSMSGIykASPDQL 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK05786  149 SYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPE 190
PRK07041 PRK07041
SDR family oxidoreductase;
11-93 1.59e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 54.27  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGqCVPVVCDSSQESEVQRLFEQVdqeqqGRLDVLV 90
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAP-VRTAALDITDEAAVDAFFAEA-----GPFDHVV 74


                  ...
gi 1952775749  91 NNA 93
Cdd:PRK07041   75 ITA 77
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-90 1.93e-08

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 54.26  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGA--SRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGgqCVPVV-CDSSQESEVQRLFEQVdQE 81
Cdd:COG0623     3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELG--SALVLpCDVTDDEQIDALFDEI-KE 79


                  ....*....
gi 1952775749  82 QQGRLDVLV 90
Cdd:COG0623    80 KWGKLDFLV 88
PRK05993 PRK05993
SDR family oxidoreductase;
3-199 2.24e-08

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 54.26  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   3 ASMKgKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATaeeaQSRGGQCVPVvcDSSQESEVQRLFEQVDQEQ 82
Cdd:PRK05993    1 MDMK-RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAAL----EAEGLEAFQL--DYAEPESIAALVAQVLELS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  83 QGRLDVLVNN-AYAGVPAImkninkafwespasiwDDINNVGLRGHYLCSVYG----ARLMVPA----GQGLIVVISSIG 153
Cdd:PRK05993   74 GGRLDALFNNgAYGQPGAV----------------EDLPTEALRAQFEANFFGwhdlTRRVIPVmrkqGQGRIVQCSSIL 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1952775749 154 GL-QYFFNVSYGVGKAACDRLAADCAQELRRHGVsYVSLW-PGMVQTE 199
Cdd:PRK05993  138 GLvPMKYRGAYNASKFAIEGLSLTLRMELQGSGI-HVSLIePGPIETR 184
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 12-202 6.58e-08

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 52.45  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAeeAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEQQGRLDVLVN 91
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALA--AELGAENVVAGALDVTDRAAWAAALADFAAATGGRLDALFN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NAYAGVPAimkninkAFWESPASIWDDINNVGLRGhylcSVYGARLMVP-----AGQGLIVVISSIGGLQYFFNVSYGVG 166
Cdd:cd08931    83 NAGVGRGG-------PFEDVPLAAHDRMVDINVKG----VLNGAYAALPylkatPGARVINTASSSAIYGQPDLAVYSAT 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952775749 167 KAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVK 202
Cdd:cd08931   152 KFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILT 187
PRK07775 PRK07775
SDR family oxidoreductase;
11-198 9.74e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.45  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRLDVLV 90
Cdd:PRK07775   14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQA-EEALGEIEVLV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  91 NNA---YAGVPAIMkninkafweSPASIWDDInNVGLRGHYlcSVYGARL--MVPAGQGLIVVISS-IGGLQYFFNVSYG 164
Cdd:PRK07775   93 SGAgdtYFGKLHEI---------STEQFESQV-QIHLVGAN--RLATAVLpgMIERRRGDLIFVGSdVALRQRPHMGAYG 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK07775  161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 12-196 1.34e-07

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 51.68  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAqsrGGQCVPVVCDSSQESEVQRLFEQVDQEQQgRLDVLVN 91
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL---GDNLYIAQLDVRNRAAIEEMLASLPAEWR-NIDVLVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NayAGVPAIMKNINKAFWESpasiWD---DINNVGLrghylcsVYGARL----MVPAGQGLIVVI-SSIGGLQYFFNVSY 163
Cdd:PRK10538   81 N--AGLALGLEPAHKASVED----WEtmiDTNNKGL-------VYMTRAvlpgMVERNHGHIINIgSTAGSWPYAGGNVY 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952775749 164 GVGKAACDRLAADCAQELRRHGVSYVSLWPGMV 196
Cdd:PRK10538  148 GATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLV 180
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-196 1.36e-07

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 51.90  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHmdtlqATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdqeqqgrlDVLV 90
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRS-----PPGAANLAALPGVEFVRGDLRDPEALAAALAGV--------DAVV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  91 NNA-YAGVPAimkninkafwESPASIWdDINNVGLRghylcSVygARLMVPAGQGLIVVISSI---GGLQYFFNVS---- 162
Cdd:COG0451    70 HLAaPAGVGE----------EDPDETL-EVNVEGTL-----NL--LEAARAAGVKRFVYASSSsvyGDGEGPIDEDtplr 131

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1952775749 163 ----YGVGKAACDRLAADCAqelRRHGVSYVSLWPGMV 196
Cdd:COG0451   132 pvspYGASKLAAELLARAYA---RRYGLPVTILRPGNV 166
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 5-141 1.92e-07

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 51.49  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYItgrhMDTLQATAEEAQSRGGQCVPVVC-DSSQESEVQRLfeqVDQ--E 81
Cdd:PRK06200    4 LHGQVALITGGGSGIGRALVERFLAEGARVAV----LERSAEKLASLRQRFGDHVLVVEgDVTSYADNQRA---VDQtvD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  82 QQGRLDVLVNNayAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLcsvyGARLMVPA 141
Cdd:PRK06200   77 AFGKLDCFVGN--AGIWDYNTSLVDIPAETLDTAFDEIFNVNVKGYLL----GAKAALPA 130
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-93 2.49e-07

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 51.06  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlQATAEEAQSR-----GGQCVPV-VCDSSQESEVQRLFEQVDQ 80
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRN----QTRAEEARKEietesGNQNIFLhIVDMSDPKQVWEFVEEFKE 76

                          90
                  ....*....|...
gi 1952775749  81 EQQgRLDVLVNNA 93
Cdd:cd09808    77 EGK-KLHVLINNA 88
PRK07577 PRK07577
SDR family oxidoreductase;
5-203 2.62e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 50.50  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlqaTAEEAQSRGGQCvpVVCDSSQESEVQRlfeqvDQEQQG 84
Cdd:PRK07577    1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFAC--DLADIEQTAATLA-----QINEIH 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNAYAGVPAIMKNInkafweSPASIWD--DIN---NVGLRGHYLCSvygarlMVPAGQGLIVVISSIGGLQYFF 159
Cdd:PRK07577   68 PVDAIVNNVGIALPQPLGKI------DLAALQDvyDLNvraAVQVTQAFLEG------MKLREQGRIVNICSRAIFGALD 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 160 NVSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKE 203
Cdd:PRK07577  136 RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQ 179
PRK05854 PRK05854
SDR family oxidoreductase;
7-97 4.12e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 50.83  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHmdtlQATAEEAQSRGGQCVPVV------CDSSQESEVQRLFEQVDQ 80
Cdd:PRK05854   14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRN----RAKGEAAVAAIRTAVPDAklslraLDLSSLASVAALGEQLRA 89

                          90
                  ....*....|....*...
gi 1952775749  81 EqqGR-LDVLVNNayAGV 97
Cdd:PRK05854   90 E--GRpIHLLINN--AGV 103
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-220 4.13e-07

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 50.30  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQA----GATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLF----EQV 78
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEigAERSGLRVVRVSLDLGAEAGLEQLLkalrELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  79 DQEQQGRLdVLVNNayAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGLQYF 158
Cdd:TIGR01500  82 RPKGLQRL-LLINN--AGTLGDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVVNISSLCAIQPF 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 159 FNVS-YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELvkEVVVKNENTDDPLLKQLR 220
Cdd:TIGR01500 159 KGWAlYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM--QQQVREESVDPDMRKGLQ 219
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-200 5.57e-07

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 49.97  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITgrhmdTLQATAEEAQSRGGQCVP----VVCDSSQESEVQRLFEQVDQEQQ 83
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAG-----CLTKNGPGAKELRRVCSDrlrtLQLDVTKPEQIKRAAQWVKEHVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GR-LDVLVNNAyaGVPAImknINKAFWeSPASIWDDINNVGLRGhyLCSVYGARL-MVPAGQGLIVVISSIGG-LQYFFN 160
Cdd:cd09805    76 EKgLWGLVNNA--GILGF---GGDEEL-LPMDDYRKCMEVNLFG--TVEVTKAFLpLLRRAKGRVVNVSSMGGrVPFPAG 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952775749 161 VSYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:cd09805   148 GAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187
PRK06128 PRK06128
SDR family oxidoreductase;
5-93 8.07e-07

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 49.86  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITgrHMDTLQATAEEA----QSRGGQCVPVVCDSSQESEVQRLFEQVdQ 80
Cdd:PRK06128   53 LQGRKALITGADSGIGRATAIAFAREGADIALN--YLPEEEQDAAEVvqliQAEGRKAVALPGDLKDEAFCRQLVERA-V 129

                          90
                  ....*....|...
gi 1952775749  81 EQQGRLDVLVNNA 93
Cdd:PRK06128  130 KELGGLDILVNIA 142
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-93 1.41e-06

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 49.29  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLC-QAGATVYITGRH-----MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVd 79
Cdd:cd08953   204 PGGVYLVTGGAGGIGRALARALArRYGARLVLLGRSplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKV- 282

                          90
                  ....*....|....
gi 1952775749  80 QEQQGRLDVLVNNA 93
Cdd:cd08953   283 RERYGAIDGVIHAA 296
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 11-199 1.51e-06

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 48.34  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYItgrhMDTLQATAEEAQSRGGQCVPVVCDSSQESEvqRLFEQVdQEQQGRLDVLV 90
Cdd:cd05361     5 LVTHARHFAGPASAEALTEDGYTVVC----HDASFADAAERQAFESENPGTKALSEQKPE--ELVDAV-LQAGGAIDVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  91 NNAYagVPAIMKNINKAfweSPASIWDDINNVGLRGHYLCSVYGARlMVPAGQGLIVVISSIGGLQYFFNVS-YGVGKAA 169
Cdd:cd05361    78 SNDY--IPRPMNPIDGT---SEADIRQAFEALSIFPFALLQAAIAQ-MKKAGGGSIIFITSAVPKKPLAYNSlYGPARAA 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1952775749 170 CDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:cd05361   152 AVALAESLAKELSRDNILVYAIGPNFFNSP 181
PRK08340 PRK08340
SDR family oxidoreductase;
11-93 2.11e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 48.26  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGqCVPVVCDSSQESEVQRLFEQVdQEQQGRLDVLV 90
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEA-WELLGGIDALV 81


                  ...
gi 1952775749  91 NNA 93
Cdd:PRK08340   82 WNA 84
PRK06482 PRK06482
SDR family oxidoreductase;
12-199 2.34e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 48.19  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRHmdtLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGRLDVLVN 91
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRVAATVRR---PDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAA-LGRIDVVVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  92 NAYAGVpaimknINKAFWESPASIWDDI--NNVGlrghylcSVYGARLMVP----AGQGLIVVISSIGGLQYFFNVS-YG 164
Cdd:PRK06482   83 NAGYGL------FGAAEELSDAQIRRQIdtNLIG-------SIQVIRAALPhlrrQGGGRIVQVSSEGGQIAYPGFSlYH 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1952775749 165 VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTE 199
Cdd:PRK06482  150 ATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTN 184
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 5-253 3.75e-06

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 47.35  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEaqsRGGQCVPVVCDSSQESEVQRLFEQVdQEQQG 84
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRAD---FGDAVVGVEGDVRSLADNERAVARC-VERFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  85 RLDVLVNNayAGVPAIMKNINKAFWESPASIWDDINNVGLRGHYLcsvyGARLMVPA---GQGLIVVISSIGGlqyFF-- 159
Cdd:cd05348    78 KLDCFIGN--AGIWDYSTSLVDIPEEKLDEAFDELFHINVKGYIL----GAKAALPAlyaTEGSVIFTVSNAG---FYpg 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749 160 --NVSYGVGKAAC----DRLAADCAQELRRHGVSyvslwPGMVQTEL-------VKEVVVKNENTDDpLLKQLRSNFSSA 226
Cdd:cd05348   149 ggGPLYTASKHAVvglvKQLAYELAPHIRVNGVA-----PGGMVTDLrgpaslgQGETSISTPPLDD-MLKSILPLGFAP 222

                         250       260
                  ....*....|....*....|....*..
gi 1952775749 227 ETTEMSGKCVVaLATDPNILSLSGKVL 253
Cdd:cd05348   223 EPEDYTGAYVF-LASRGDNRPATGTVI 248
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 5-204 5.81e-06

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 46.77  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   5 MKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVP-VVCDSSQESEVQRLFEQVdqEQQ 83
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSyIVADLTKREDLERTVKEL--KNI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  84 GRLDVLVNNAYAGVPAIMKNINKAFWESpasiwddinnvGLRGHYLCSVYGARLMVPA----GQGLIVVISSIGGLQYFF 159
Cdd:PRK08339   84 GEPDIFFFSTGGPKPGYFMEMSMEDWEG-----------AVKLLLYPAVYLTRALVPAmerkGFGRIIYSTSVAIKEPIP 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1952775749 160 NVSYG-VGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTELVKEV 204
Cdd:PRK08339  153 NIALSnVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQL 198
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 11-156 6.91e-06

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 46.72  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYitgrHMDTLQATAEeaqsrggqcvpvvCDSSQESEVQRLFEQVDQEQQGRLDVLV 90
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVI----GIDLREADVI-------------ADLSTPEGRAAAIADVLARCSGVLDGLV 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749  91 NNAYAGVPAIMKNINKafwespasiwddINNVGLRgHYLCSVygARLMVPAGQGLIVVISSIGGLQ 156
Cdd:cd05328    66 NCAGVGGTTVAGLVLK------------VNYFGLR-ALMEAL--LPRLRKGHGPAAVVVSSIAGAG 116
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-98 7.23e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 46.78  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG--QCVPVVCDSSQESE--VQRLFEQVDQEQ 82
Cdd:PLN02780   53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSktQIKTVVVDFSGDIDegVKRIKETIEGLD 132

                          90
                  ....*....|....*.
gi 1952775749  83 QGrldVLVNNAYAGVP 98
Cdd:PLN02780  133 VG---VLINNVGVSYP 145
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 10-110 1.03e-05

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 46.61  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  10 CVVTGASRGIGRGIALQLCQAGAT-VYITGRHMDTLQATAEEAQSRGGQCVPVV--CDSSQESEVQRLFEQVDQEQQgrL 86
Cdd:cd05274   153 YLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLRAGGARVSVvrCDVTDPAALAALLAELAAGGP--L 230

                          90       100
                  ....*....|....*....|....
gi 1952775749  87 DVLVNNAYAGVPAIMKNINKAFWE 110
Cdd:cd05274   231 AGVIHAAGVLRDALLAELTPAAFA 254
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 9-98 1.39e-05

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 45.69  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   9 VCVVTGASRGIGRGIALQLCQAGATVYITGRHM--DTLQATAEEAQSRGGQCVPVVCDSSQESEV-QRLFEQVDQ--EQQ 83
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSaaAASTLAAELNARRPNSAVTCQADLSNSATLfSRCEAIIDAcfRAF 82

                          90
                  ....*....|....*
gi 1952775749  84 GRLDVLVNNAYAGVP 98
Cdd:TIGR02685  83 GRCDVLVNNASAFYP 97
PRK05717 PRK05717
SDR family oxidoreductase;
7-151 1.85e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 45.27  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITgrHMDTlQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQGRL 86
Cdd:PRK05717   10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLA--DLDR-ERGSKVAKALGENAWFIAMDVADEAQVAAGVAEV-LGQFGRL 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952775749  87 DVLVNNAyagvpAIMKNINKAFWESPASIWDDINNVGLRGHYL----CSVYgarlmVPAGQGLIVVISS 151
Cdd:PRK05717   86 DALVCNA-----AIADPHNTTLESLSLAHWNRVLAVNLTGPMLlakhCAPY-----LRAHNGAIVNLAS 144
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-155 2.38e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 44.95  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQAtaeeaqsrgGQCVPVVCDSSQESEvqRLFEQVdqeqqGR 85
Cdd:PRK06550    4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS---------GNFHFLQLDLSDDLE--PLFDWV-----PS 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNayAGVPAIMKNINkafwESPASIWDDINNVGLRGHYLCSVYGARLMVPAGQGLIVVISSIGGL 155
Cdd:PRK06550   68 VDILCNT--AGILDDYKPLL----DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASF 131
PRK08251 PRK08251
SDR family oxidoreductase;
8-200 5.78e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQVDQEqQGR 85
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAEllARYPGIKVAVAALDVNDHDQVFEVFAEFRDE-LGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLVNNAYAGVPAimkNINKA-FWESPASIwdDINNVGLrghyLCSVYGA-RLMVPAGQGLIVVISSIGGLQYF--FNV 161
Cdd:PRK08251   82 LDRVIVNAGIGKGA---RLGTGkFWANKATA--ETNFVAA----LAQCEAAmEIFREQGSGHLVLISSVSAVRGLpgVKA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952775749 162 SYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK08251  153 AYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
PRK08177 PRK08177
SDR family oxidoreductase;
12-200 6.29e-05

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 43.48  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRhmdtlqataEEAQSRGGQCVPVV----CDSSQESEVQRLFEQVdQEQqgRLD 87
Cdd:PRK08177    6 IIGASRGLGLGLVDRLLERGWQVTATVR---------GPQQDTALQALPGVhiekLDMNDPASLDQLLQRL-QGQ--RFD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPAImkninkafwESPASIwdDINNVG--LRGHYLCSVYGARLMVP---AGQGLIVVISSI-GGLQyfFNV 161
Cdd:PRK08177   74 LLFVNAGISGPAH---------QSAADA--TAAEIGqlFLTNAIAPIRLARRLLGqvrPGQGVLAFMSSQlGSVE--LPD 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952775749 162 S-----YGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQTEL 200
Cdd:PRK08177  141 GgemplYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 11-81 8.09e-05

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 42.55  E-value: 8.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGA-TVYITGRHM---DTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQE 81
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAaprPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAE 78
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 1-56 8.27e-05

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 42.77  E-value: 8.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952775749   1 MAASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGG 56
Cdd:cd01078    22 MGKDLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFG 77
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 6-97 1.82e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 42.32  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   6 KGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEE--AQSRGGQCVPVVCDSSQESEVQRLFEQVdQEQQ 83
Cdd:PRK06197   15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARitAATPGADVTLQELDLTSLASVRAAADAL-RAAY 93

                          90
                  ....*....|....
gi 1952775749  84 GRLDVLVNNayAGV 97
Cdd:PRK06197   94 PRIDLLINN--AGV 105
PRK08017 PRK08017
SDR family oxidoreductase;
8-204 1.86e-04

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 42.38  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLqataEEAQSRGGQCVPVVCDSSQesEVQRLFEQVDQEQQGRLD 87
Cdd:PRK08017    3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV----ARMNSLGFTGILLDLDDPE--SVERAADEVIALTDNRLY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  88 VLVNNAYAGVPAIMKNINKAFWESPASiwddINNVGLrgHYLCSvygaRL---MVPAGQGLIVVISSIGGLqyffnVS-- 162
Cdd:PRK08017   77 GLFNNAGFGVYGPLSTISRQQMEQQFS----TNFFGT--HQLTM----LLlpaMLPHGEGRIVMTSSVMGL-----IStp 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1952775749 163 ----YGVGKAACDRLAADCAQELRRHGVSyVSLW-PGMVQTELVKEV 204
Cdd:PRK08017  142 grgaYAASKYALEAWSDALRMELRHSGIK-VSLIePGPIRTRFTDNV 187
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 11-93 2.32e-04

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.41  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQataeeaqsrggqcvpvvCDSSQESEVQRLFEQVdqeqqGRLDVLV 90
Cdd:cd11731     2 IVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ-----------------VDITDEASIKALFEKV-----GHFDAIV 59


                  ...
gi 1952775749  91 NNA 93
Cdd:cd11731    60 STA 62
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 12-93 3.10e-04

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 41.71  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  12 VTGASRGIGRGIALQLCQAGATVYITGRhmDTLQATAEEAQSRGGQCVpVVCDSSQESEVQRLFEQVDqeQQGRLDVLVN 91
Cdd:cd08951    12 ITGSSDGLGLAAARTLLHQGHEVVLHAR--SQKRAADAKAACPGAAGV-LIGDLSSLAETRKLADQVN--AIGRFDAVIH 86


                  ..
gi 1952775749  92 NA 93
Cdd:cd08951    87 NA 88
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 2-79 3.52e-04

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 41.99  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   2 AASMKGKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEeaqsrgGQCVPVVC---DSSQESEVQRLFEQV 78
Cdd:PRK07424  173 ALSLKGKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKITLEIN------GEDLPVKTlhwQVGQEAALAELLEKV 246


                  .
gi 1952775749  79 D 79
Cdd:PRK07424  247 D 247
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-93 3.70e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.54  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749    8 KVCVVTGASRGIGRGIALQLCQAGA-TVYITGRH---MDTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDqEQQ 83
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIP-AVE 79

                           90
                   ....*....|
gi 1952775749   84 GRLDVLVNNA 93
Cdd:smart00822  80 GPLTGVIHAA 89
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
7-96 3.73e-04

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 41.24  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGAS--RGIGRGIALQLCQAGATVYIT------GRHMDTLQATAEEAQSRggqcVPVVCDSSQESEVQRLFEQV 78
Cdd:PRK07370    6 GKKALVTGIAnnRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPLNPS----LFLPCDVQDDAQIEETFETI 81

                          90
                  ....*....|....*....
gi 1952775749  79 dQEQQGRLDVLVNN-AYAG 96
Cdd:PRK07370   82 -KQKWGKLDILVHClAFAG 99
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
1-198 6.35e-04

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 40.48  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGAS--RGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGGQCVPVV-CDSSQESEVQRLFEQ 77
Cdd:PRK08594    1 MMLSLEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFTYAGERLEKEVRELADTLEGQESLLLpCDVTSDEEITACFET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  78 VDqEQQGRLDVLVNN-AYAgvpaimkniNKAFwespasiwddinnvgLRGHYL------------CSVYG-------ARL 137
Cdd:PRK08594   81 IK-EEVGVIHGVAHCiAFA---------NKED---------------LRGEFLetsrdgfllaqnISAYSltavareAKK 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952775749 138 MVPAGqGLIVVISSIGGLQYF--FNVsYGVGKAACDRLAADCAQELRRHGVSYVSLWPGMVQT 198
Cdd:PRK08594  136 LMTEG-GSIVTLTYLGGERVVqnYNV-MGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRT 196
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 11-81 1.21e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 39.96  E-value: 1.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGA-TVYITGRHM--DTLQATAEEAQSRGGQCVPVVCDSSQESEVQRLFEQVDQE 81
Cdd:cd08955   153 LITGGLGGLGLLVAEWLVERGArHLVLTGRRApsAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRAS 226
PRK05884 PRK05884
SDR family oxidoreductase;
11-99 1.57e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 39.02  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  11 VVTGASRGIGRGIALQLCQAGATVYITGRHMDTLQATAEEAQSRGgqcvpVVCDSSQESEVQRLFEQVDQEqqgrLDVLV 90
Cdd:PRK05884    4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDA-----IVCDNTDPASLEEARGLFPHH----LDTIV 74


                  ....*....
gi 1952775749  91 NnayagVPA 99
Cdd:PRK05884   75 N-----VPA 78
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-198 1.77e-03

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 38.84  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGrhmdtlQATAEEAqsrgGQCVPVVCDSSQESEVQRLFEQVDqEQQGRL 86
Cdd:cd05334     1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASID------LAENEEA----DASIIVLDSDSFTEQAKQVVASVA-RLSGKV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  87 DVLVNNA--YAGVPAIMKNINKAfwespasiWDDINNVGLRGHYLCSVYGARLMVPAgqGLIVVISSIGGLQYFFN-VSY 163
Cdd:cd05334    70 DALICVAggWAGGSAKSKSFVKN--------WDLMWKQNLWTSFIASHLATKHLLSG--GLLVLTGAKAALEPTPGmIGY 139

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952775749 164 GVGKAACDRLAADCAQELR--RHGVSYVSLWPGMVQT 198
Cdd:cd05334   140 GAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDT 176
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 7-200 3.27e-03

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 38.73  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   7 GKVCVVTGASRGIGRGIALQLCQAGATVYITGRHMdtlqATAEEAQSR------GGQCVPVVCDSSQESEVQRLFEQVDQ 80
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNM----SRASAAVSRileewhKARVEAMTLDLASLRSVQRFAEAFKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  81 EQQgRLDVLVNNayAGVPAIMKNINKAFWESPASiwddINNVglrGHYLCSVYGARLMVPAGQGLIVVISSIGglQYFFN 160
Cdd:cd09809    77 KNS-PLHVLVCN--AAVFALPWTLTEDGLETTFQ----VNHL---GHFYLVQLLEDVLRRSAPARVIVVSSES--HRFTD 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952775749 161 VSYGVGKAACDRL-----------------------AADCAQELRRHGVSYVSLWPG-MVQTEL 200
Cdd:cd09809   145 LPDSCGNLDFSLLsppkkkywsmlaynraklcnilfSNELHRRLSPRGITSNSLHPGnMMYSSI 208
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-187 3.31e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   1 MAASMKGKVCVVTGAS--RGIGRGIALQLCQAGATV---YITGRHMDTLQATAEEAQSRggqcvpVVCDSSQESEVQRLF 75
Cdd:PRK06079    1 MSGILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATViytYQNDRMKKSLQKLVDEEDLL------VECDVASDESIERAF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  76 EQVdQEQQGRLDVLVNN-AYAgvpaimkninkafweSPASIWDDINNVGLRGHYLC---SVYGARLMVPAGQGLIVVISS 151
Cdd:PRK06079   75 ATI-KERVGKIDGIVHAiAYA---------------KKEELGGNVTDTSRDGYALAqdiSAYSLIAVAKYARPLLNPGAS 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952775749 152 IGGLQYF--------FNVsYGVGKAACDR----LAADCAQE-LRRHGVS 187
Cdd:PRK06079  139 IVTLTYFgseraipnYNV-MGIAKAALESsvryLARDLGKKgIRVNAIS 186
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 8-196 3.45e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749   8 KVCVVtGASRGIGRGIALQLCQAGATVYI--TGRHMDTLQATAEEaqsrggqcvpVVCDSSQESEVQRLFEQVDqeqqgr 85
Cdd:cd05265     2 KILII-GGTRFIGKALVEELLAAGHDVTVfnRGRTKPDLPEGVEH----------IVGDRNDRDALEELLGGED------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952775749  86 LDVLV-NNAYagvpaimkninkafweSPASIWDDINNVGLR-GHYL----CSVYGARLMV-----PAGQGLIVVISSIGg 154
Cdd:cd05265    65 FDVVVdTIAY----------------TPRQVERALDAFKGRvKQYIfissASVYLKPGRVitestPLREPDAVGLSDPW- 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952775749 155 lqyffnvSYGVGKAACDRLAAdcaqelRRHGVSYVSLWPGMV 196
Cdd:cd05265   128 -------DYGRGKRAAEDVLI------EAAAFPYTIVRPPYI 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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