NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|296214664|ref|XP_002753722|]
View 

dehydrogenase/reductase SDR family member 1 [Callithrix jacchus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.36e-165

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: 460.38  E-value: 2.36e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM-DTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 83
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVPY 163
Cdd:cd09763   81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGlqdPVFKQLRSVFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763  161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237
                        250       260
                 ....*....|....*....|....*...
gi 296214664 244 NILSLSGKVLPSCDLARRYGLRDVDGRP 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 2.36e-165

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: 460.38  E-value: 2.36e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM-DTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 83
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVPY 163
Cdd:cd09763   81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGlqdPVFKQLRSVFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763  161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237
                        250       260
                 ....*....|....*....|....*...
gi 296214664 244 NILSLSGKVLPSCDLARRYGLRDVDGRP 271
Cdd:cd09763  238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-212 4.11e-55

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: 179.60  E-value: 4.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 82
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNV 161
Cdd:COG1028   81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQ 212
Cdd:COG1028  154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVRE 204
PRK08303 PRK08303
short chain dehydrogenase; Provisional
1-271 3.15e-53

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 176.34  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM----------DTLRVAAQEAQSLGGQCVPVVCDSSQESE 70
Cdd:PRK08303   2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  71 VRSLFEQVDREqQGRLDVLVNNAYAGvqTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVIS 150
Cdd:PRK08303  82 VRALVERIDRE-QGRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 151 ----SPGGLQYMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMA-KEEGLQDPVFKQLRsvFSS 225
Cdd:PRK08303 159 dgtaEYNATHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFGvTEENWRDALAKEPH--FAI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 226 AETTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYGLRDVDG-RP 271
Cdd:PRK08303 237 SETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
8-203 1.36e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.15  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   88 VLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-YGVG 166
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 296214664  167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
7-203 4.00e-14

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: 70.81  E-value: 4.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    7 GQVCVVTGASRGIGRGIALQLCKAGATVYIT---------GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavGYPLATRAELDAVAAACPDQVLPVIADVRDPAALAAAVAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   78 VdREQQGRLDVLVnnAYAGVqtILNTRskAFWETPASMWDDINNVGLRGhylcsVYG-ARLMVPA-------GRGLIVVI 149
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGV--IAGGR--PLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664  150 SSPGGLQYMFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
9-93 1.26e-03

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: 39.00  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664     9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRHMDTLRVAA---QEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAallAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80

                   ....*....
gi 296214664    85 RLDVLVNNA 93
Cdd:smart00822  81 PLTGVIHAA 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 2.36e-165

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: 460.38  E-value: 2.36e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM-DTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 83
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIlPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVPY 163
Cdd:cd09763   81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGlqdPVFKQLRSVFSSAETTEMSGKCVVALATDP 243
Cdd:cd09763  161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237
                        250       260
                 ....*....|....*....|....*...
gi 296214664 244 NILSLSGKVLPSCDLARRYGLRDVDGRP 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 4.36e-98

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: 288.91  E-value: 4.36e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM--------DTLRV----AAQEAQSLGGQCVPVVCDSSQESEVR 72
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTAsegdngsaKSLPGtieeTAEEIEAAGGQALPIVVDVRDEDQVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  73 SLFEQVDrEQQGRLDVLVNNAYAGVQTIlntrskaFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSP 152
Cdd:cd05338   81 ALVEATV-DQFGRLDILVNNAGAIWLSL-------VEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 153 GGLQYMF-NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTellkehmakeeglqdpvfkqlrsvfsSAETTEM 231
Cdd:cd05338  153 LSLRPARgDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIE--------------------------TPAATEL 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 296214664 232 SGKCVVALATDPNILSLSGKVLPSCDLARRYGLRDVDGRP 271
Cdd:cd05338  207 SGGSDPARARSPEILSDAVLAILSRPAAERTGLVVIDEEL 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-212 4.11e-55

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: 179.60  E-value: 4.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 82
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNV 161
Cdd:COG1028   81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQ 212
Cdd:COG1028  154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVRE 204
PRK08303 PRK08303
short chain dehydrogenase; Provisional
1-271 3.15e-53

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 176.34  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHM----------DTLRVAAQEAQSLGGQCVPVVCDSSQESE 70
Cdd:PRK08303   2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  71 VRSLFEQVDREqQGRLDVLVNNAYAGvqTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVIS 150
Cdd:PRK08303  82 VRALVERIDRE-QGRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 151 ----SPGGLQYMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMA-KEEGLQDPVFKQLRsvFSS 225
Cdd:PRK08303 159 dgtaEYNATHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFGvTEENWRDALAKEPH--FAI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 226 AETTEMSGKCVVALATDPNILSLSGKVLPSCDLARRYGLRDVDG-RP 271
Cdd:PRK08303 237 SETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
4-243 6.25e-47

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: 158.04  E-value: 6.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:COG4221    2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAE---LGGRALAVPLDVTDEAAVEAAVAAA-VAEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNVP 162
Cdd:COG4221   78 GRLDVLVNN--AGV-----ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRpYPGGAV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLRSVfssaeTTEMSGKCVVALATD 242
Cdd:COG4221  151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPL-----TPEDVAEAVLFALTQ 225

                 .
gi 296214664 243 P 243
Cdd:COG4221  226 P 226
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
10-209 4.61e-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: 153.21  E-value: 4.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  10 CVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAqEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVL 89
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEA-LEEFGRLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  90 VNNayAGVQtilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNVPYGVGKA 168
Cdd:cd05233   79 VNN--AGIA-----RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRpLPGQAAYAASKA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 169 ACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEE 209
Cdd:cd05233  152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEA 192
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
5-200 6.43e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 150.79  E-value: 6.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAV-LARFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYM-FNVPY 163
Cdd:COG0300   82 PIDVLVNN--AGV-----GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLpGMAAY 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:COG0300  155 AASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
8-203 1.36e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.15  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   88 VLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-YGVG 166
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 296214664  167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-209 7.37e-38

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 134.52  E-value: 7.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAV-EAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNVPY 163
Cdd:PRK05653  82 ALDILVNN--AGI-----TRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTgNPGQTNY 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE--HMAKEE 209
Cdd:PRK05653 155 SAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGlpEEVKAE 202
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-202 7.07e-35

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 126.88  E-value: 7.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYItgrHMDTLRVAAQEAQ----SLGGQCVPVVCDSSQESEVRSLFEQVDrE 81
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVI---AYDINEEAAQELLeeikEEGGDAIAVKADVSSEEDVENLVEQIV-E 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN- 160
Cdd:PRK05565  80 KFGKIDILVNN--AGISNF-----GLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCe 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK05565 153 VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
5-213 2.55e-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: 2.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEED-FG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQtilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-Y 163
Cdd:cd05347   82 KIDILVNN--AGII-----RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPaY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQD 213
Cdd:cd05347  155 AASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDD 204
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-213 1.13e-33

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 123.68  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQID-EE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNAYAGVQtilntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP 162
Cdd:PRK08063  80 FGRLDVFVNNAASGVL-------RPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 296214664 163 Y-GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQD 213
Cdd:PRK08063 153 TvGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLED 204
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
5-200 1.47e-32

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 120.68  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQS-LGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGaLGGKALAVQGDVSDAESVERAVDEA-KAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VP 162
Cdd:PRK05557  82 GGVDILVNN--AGI-----TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGqAN 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK05557 155 YAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
PRK12826 PRK12826
SDR family oxidoreductase;
3-203 8.98e-32

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 118.87  E-value: 8.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 82
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGV-ED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ--YMFN 160
Cdd:PRK12826  81 FGRLDILVAN--AGI-----FPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvgYPGL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:PRK12826 154 AHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN 196
PRK07035 PRK07035
SDR family oxidoreductase;
5-242 1.38e-31

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 118.19  E-value: 1.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHI-RERHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQ--TILNTRSKAFWETpasmWDdinnVGLRGHYLCSVYGARLMVPAGRGLIVVISS-----PGGLQY 157
Cdd:PRK07035  85 RLDILVNNAAANPYfgHILDTDLGAFQKT----VD----VNIRGYFFMSVEAGKLMKEQGGGSIVNVASvngvsPGDFQG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MfnvpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTElLKEHMAKEEGLQDPVFKQ--LRSVfssAETTEMSGkC 235
Cdd:PRK07035 157 I----YSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTK-FASALFKNDAILKQALAHipLRRH---AEPSEMAG-A 227

                 ....*..
gi 296214664 236 VVALATD 242
Cdd:PRK07035 228 VLYLASD 234
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
5-242 1.39e-31

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: 118.25  E-value: 1.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQ 83
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAI-KEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVQtilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMV-PAGRGLIVVISS-----PgglqY 157
Cdd:cd05358   80 GTLDILVNN--AGLQ-----GDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSSvhekiP----W 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDpvfkQLRSV-FSSAETTEMSGKCV 236
Cdd:cd05358  149 PGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRAD----LLSLIpMGRIGEPEEIAAAA 224

                 ....*.
gi 296214664 237 VALATD 242
Cdd:cd05358  225 AWLASD 230
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
5-242 2.04e-31

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: 117.82  E-value: 2.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 83
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKD-F 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqYMFNVP- 162
Cdd:cd05352   85 GKIDILIAN--AGI-----TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSG--TIVNRPq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 163 ----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLRsvfsSAETTEMSGKCVVa 238
Cdd:cd05352  156 pqaaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKR----IALPEELVGAYLY- 230

                 ....
gi 296214664 239 LATD 242
Cdd:cd05352  231 LASD 234
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-200 2.46e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 115.07  E-value: 2.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAA-A 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSP----GGLQ 156
Cdd:PRK12939  80 AALGGLDGLVNN--AGI-----TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDtalwGAPK 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296214664 157 YMfnvPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK12939 153 LG---AYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
12-213 4.29e-30

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: 113.99  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVA-AQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 90
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEvAAEIEELGGKAVVVRADVSQPQDVEEMFAAV-KERFGRLDVLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYAGVQtilntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGVGKAA 169
Cdd:cd05359   82 SNAAAGAF-------RPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNyLAVGTAKAA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296214664 170 CDKLAADCAHELRRYGVSYVSLWPGIVQTELLKeHMAKEEGLQD 213
Cdd:cd05359  155 LEALVRYLAVELGPRGIRVNAVSPGVIDTDALA-HFPNREDLLE 197
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
8-203 4.29e-30

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: 114.18  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLD 87
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAE-FGPVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGVG 166
Cdd:cd05333   80 ILVNN--AGI-----TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGqANYAAS 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:cd05333  153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189
PRK05867 PRK05867
SDR family oxidoreductase;
5-237 1.13e-29

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 113.21  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 84
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 rLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGlqYMFNVPY 163
Cdd:PRK05867  87 -IDIAVCN--AGIITV-----TPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSG--HIINVPQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVG-----KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLkEHMAKEEGLQDPVF--------KQLRSVF---SSAE 227
Cdd:PRK05867 157 QVShycasKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELV-EPYTEYQPLWEPKIplgrlgrpEELAGLYlylASEA 235
                        250
                 ....*....|
gi 296214664 228 TTEMSGKCVV 237
Cdd:PRK05867 236 SSYMTGSDIV 245
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
17-202 1.65e-29

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: 112.52  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   17 RGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdREQQGRLDVLVNNayAG 96
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLP--CDVTDEEQVEALVAAA-VEKFGRLDILVNN--AG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   97 vqtILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRglIVVISSPGGLQYMFNV-PYGVGKAACDKLAA 175
Cdd:pfam13561  81 ---FAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGS--IVNLSSIGAERVVPNYnAYGAAKAALEALTR 155
                         170       180
                  ....*....|....*....|....*....
gi 296214664  176 DCAHELRRYG--VSYVSlwPGIVQTELLK 202
Cdd:pfam13561 156 YLAVELGPRGirVNAIS--PGPIKTLAAS 182
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-214 3.30e-29

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 111.88  E-value: 3.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQvDREQ 82
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAA-AVER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYlcsvYGARLMVP----AGRGLIVVISSPGGLQ-Y 157
Cdd:PRK12825  82 FGRIDILVNN--AGI-----FEDKPLADMSDDEWDEVIDVNLSGVF----HLLRAVVPpmrkQRGGRIVNISSVAGLPgW 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDP 214
Cdd:PRK12825 151 PGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDA 207
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
5-214 3.53e-29

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: 111.81  E-value: 3.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDtlrvAAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQq 83
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG----AAQAvVAQIAGGALALRVDVTDEQQVAALFERAVEEF- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAyaGVQTIlntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQymfNVP- 162
Cdd:cd08944   76 GGLDLLVNNA--GAMHL----TPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQS---GDPg 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 163 ---YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDP 214
Cdd:cd08944  147 ygaYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGP 201
FabG-like PRK07231
SDR family oxidoreductase;
7-206 6.35e-29

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 111.08  E-value: 6.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVAAA-LERFGSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVqtilNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGV 165
Cdd:PRK07231  83 DILVNN--AGT----THRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGlGWYNA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 166 GKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMA 206
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMG 197
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
5-200 1.26e-28

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: 110.58  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVP---VVCDSSQESEVRSLFEQVdRE 81
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKillVVADLTEEEGQDRIISTT-LA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAYAGVQtilntrsKAFWETPASMWDDINNVGLRGHYLCSvygaRLMVP---AGRGLIVVISS-PGGLQY 157
Cdd:cd05364   80 KFGRLDILVNNAGILAK-------GGGEDQDIEEYDKVMNLNLRAVIYLT----KLAVPhliKTKGEIVNVSSvAGGRSF 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05364  149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
5-222 9.14e-28

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: 108.06  E-value: 9.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSL-GGQCVPVVCDSSQESEVRSLFEQVDREqQ 83
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKE-F 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAyAGvqtilNtrskafWETPASM-----WDDINNVGLRGHYLCS-VYGARLMVPAGRGLIVVISSPG---G 154
Cdd:cd05369   80 GKIDILINNA-AG-----N------FLAPAESlspngFKTVIDIDLNGTFNTTkAVGKRLIEAKHGGSILNISATYaytG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296214664 155 LQYMfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEllkEHMAKEEGLQDPVFKQLRSV 222
Cdd:cd05369  148 SPFQ--VHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT---EGMERLAPSGKSEKKMIERV 210
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
7-243 1.84e-27

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: 107.48  E-value: 1.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQsLGGQCVPVVCDSSQESEVRSLFEQVDREQQGrL 86
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ-GGPRALGVQCDVTSEAQVQSAFEQAVLEFGG-L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVQTilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRG--LIVVIS------SPGglqym 158
Cdd:cd08943   79 DIVVSN--AGIAT-----SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGgnIVFNASknavapGPN----- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 159 fNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWP-GIVQT-----ELLKEHMAKEEGLQDPVFKQlRSVFSSAETTEMS 232
Cdd:cd08943  147 -AAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPdAVFRGskiweGVWRAARAKAYGLLEEEYRT-RNLLKREVLPEDV 224
                        250
                 ....*....|.
gi 296214664 233 GKCVVALATDP 243
Cdd:cd08943  225 AEAVVAMASED 235
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
5-211 2.51e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 107.28  E-value: 2.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQG 84
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVE-TFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTILNTRskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ-YMFNVPY 163
Cdd:PRK12429  81 GVDILVNN--AGIQHVAPIE-----DFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVgSAGKAAY 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHM---AKEEGL 211
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIpdlAKERGI 204
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
5-194 9.34e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 105.80  E-value: 9.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEET-LERFG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGvqtilntrskafW-----ETPASMWDDINNVGLRGHYLCS-VYGARLMVPAGRGLIVVISSPGGLQ-- 156
Cdd:PRK08213  89 HVDILVNNAGAT------------WgapaeDHPVEAWDKVMNLNVRGLFLLSqAVAKRSMIPRGYGRIINVASVAGLGgn 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 157 ---YMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPG 194
Cdd:PRK08213 157 ppeVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPG 197
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
11-244 1.07e-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: 105.39  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRvAAQEAQSLGGQCVPVvcDSSQESEVRSLFEQVdREQQGRLDVLV 90
Cdd:cd05374    4 LITGCSSGIGLALALALAAQGYRVIATARNPDKLE-SLGELLNDNLEVLEL--DVTDEESIKAAVKEV-IERFGRIDVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYAGVqtilntrSKAFWETPAsmwDDINNVglrghYLCSVYG--------ARLMVPAGRGLIVVISSPGGLQYM-FNV 161
Cdd:cd05374   80 NNAGYGL-------FGPLEETSI---EEVREL-----FEVNVFGplrvtrafLPLMRKQGSGRIVNVSSVAGLVPTpFLG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAK-----EEGLQDPVFKQLRSVFSSAETTEMS---- 232
Cdd:cd05374  145 PYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSaledpEISPYAPERKEIKENAAGVGSNPGDpekv 224
                        250
                 ....*....|..
gi 296214664 233 GKCVVALATDPN 244
Cdd:cd05374  225 ADVIVKALTSES 236
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
6-203 3.35e-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: 103.89  E-value: 3.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRhmDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 82
Cdd:cd05362    2 AGKVALVTGASRGIGRAIAKRLARDGASVvvnYASSK--AAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAE-KA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRglIVVISSPGGLQYM-FNV 161
Cdd:cd05362   79 FGGVDILVNN--AGV-----MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR--IINISSSLTAAYTpNYG 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:cd05362  150 AYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYA 191
PRK06172 PRK06172
SDR family oxidoreductase;
1-202 5.82e-26

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 103.29  E-value: 5.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK06172   1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQT-I 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVQtILNTRSKafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN 160
Cdd:PRK06172  80 AAYGRLDYAFNN--AGIE-IEQGRLA---EGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 161 VP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK06172 154 MSiYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR 196
PRK06181 PRK06181
SDR family oxidoreductase;
7-202 6.91e-26

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 103.52  E-value: 6.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAA-VARFGGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVqtilnTRSKAFWETPA-SMWDDINNVglrgHYLCSVYGARLMVP---AGRGLIVVISSPGGLQymfNVP 162
Cdd:PRK06181  80 DILVNN--AGI-----TMWSRFDELTDlSVFERVMRV----NYLGAVYCTHAALPhlkASRGQIVVVSSLAGLT---GVP 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 163 YGVGKAA--------CDKLAAdcahELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK06181 146 TRSGYAAskhalhgfFDSLRI----ELADDGVAVTVVCPGFVATDIRK 189
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
7-211 1.61e-25

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: 102.35  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKA-GDAFGRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGvqtilntRSKAFWETPASMWDDinnvGLRGHYLCSVYGARLMVPA----GRGLIVVISSPGGLQYMFN-V 161
Cdd:cd05344   80 DILVNNAGGP-------PPGPFAELTDEDWLE----AFDLKLLSVIRIVRAVLPGmkerGWGRIVNISSLTVKEPEPNlV 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK---EHMAKEEGL 211
Cdd:cd05344  149 LSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRrllEARAEKEGI 201
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-213 1.67e-25

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 101.69  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK07666   1 MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQL-K 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVQTILNtrskaFWETPASMWDDINNVGLRGHYlcsvYGARLMVPA----GRGLIVVISSPGGLQ 156
Cdd:PRK07666  80 NELGSIDILINN--AGISKFGK-----FLELDPAEWEKIIQVNLMGVY----YATRAVLPSmierQSGDIINISSTAGQK 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296214664 157 YMFNV-PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEllkehMAKEEGLQD 213
Cdd:PRK07666 149 GAAVTsAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATD-----MAVDLGLTD 201
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-200 5.61e-25

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 100.81  E-value: 5.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQI-AEDFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGV----QTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGLQYMF 159
Cdd:PRK08217  82 QLNGLINN--AGIlrdgLLVKAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSIARAGNMG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 160 NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK08217 160 QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM 200
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-243 6.61e-25

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 100.74  E-value: 6.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKV-A 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVQTILNTRSKAFwetpaSMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVV--------ISSP 152
Cdd:PRK13394  80 ERFGSVDILVSN--AGIQIVNPIENYSF-----ADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIymgsvhshEASP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 153 GGLQYMfnvpygVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHM---AKEEGL-QDPVFKQLRS------V 222
Cdd:PRK13394 153 LKSAYV------TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIpeqAKELGIsEEEVVKKVMLgktvdgV 226
                        250       260
                 ....*....|....*....|.
gi 296214664 223 FSsaeTTEMSGKCVVALATDP 243
Cdd:PRK13394 227 FT---TVEDVAQTVLFLSSFP 244
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
5-242 1.57e-24

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: 99.45  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrhmDTLRVAAQE-AQSLGGQCVPVV-CDSSQESEVRSLF-EQVDRe 81
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIA----DIDDDAGQAvAAELGDPDISFVhCDVTVEADVRAAVdTAVAR- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 qQGRLDVLVNNAyaGVqtiLNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNV 161
Cdd:cd05326   77 -FGRLDIMFNNA--GV---LGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 162 -PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLRSVFSSAETTEMSGKCVVALA 240
Cdd:cd05326  151 hAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYLA 230

                 ..
gi 296214664 241 TD 242
Cdd:cd05326  231 SD 232
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
11-199 2.53e-24

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: 98.35  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRhmDTLRVaAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLV 90
Cdd:cd08929    4 LVTGASRGIGEATARLLHAEGYRVGICAR--DEARL-AAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEA-FGGLDALV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYAGVQTILNTRSKAFWetpasmWDDINNVgLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQymfnvPYGVGKAAC 170
Cdd:cd08929   80 NNAGVGVMKPVEELTPEEW------RLVLDTN-LTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKN-----AFKGGAAYN 147
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 296214664 171 DK------LAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:cd08929  148 ASkfgllgLSEAAMLDLREANIRVVNVMPGSVDTG 182
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
5-242 3.13e-24

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: 98.61  E-value: 3.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAE---LGDAARFFHLDVTDEDGWTAVVDTA-REAFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTILNTRskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-Y 163
Cdd:cd05341   79 RLDVLVNN--AGILTGGTVE-----TTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAaY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELR--RYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPvfkQLRSVFSSAETTEMSGkCVVALAT 241
Cdd:cd05341  152 NASKGAVRGLTKSAALECAtqGYGIRVNSVHPGYIYTPMTDELLIAQGEMGNY---PNTPMGRAGEPDEIAY-AVVYLAS 227

                 .
gi 296214664 242 D 242
Cdd:cd05341  228 D 228
PRK07326 PRK07326
SDR family oxidoreductase;
5-199 4.01e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 98.16  E-value: 4.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN-KGNVLGLAADVRDEADVQRAVDAIVAA-FG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNA----YAGVQtilntrskafwETPASMWDDINNVGLRGHYlcsvYGARLMVPA---GRGLIVVISSPGGLQY 157
Cdd:PRK07326  82 GLDVLIANAgvghFAPVE-----------ELTPEEWRLVIDTNLTGAF----YTIKAAVPAlkrGGGYIINISSLAGTNF 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 158 MFN-VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK07326 147 FAGgAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-186 4.16e-24

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 102.62  E-value: 4.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   2 AAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQ--CVPVVCDSSQESEVRSLFEQVD 79
Cdd:PRK08324 417 PKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAE---LGGPdrALGVACDVTDEAAVQAAFEEAA 493
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  80 REQQGrLDVLVNNayAGVQTilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISS-----PG 153
Cdd:PRK08324 494 LAFGG-VDIVVSN--AGIAI-----SGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASknavnPG 565
                        170       180       190
                 ....*....|....*....|....*....|...
gi 296214664 154 GLqymfNVPYGVGKAACDKLAADCAHELRRYGV 186
Cdd:PRK08324 566 PN----FGAYGAAKAAELHLVRQLALELGPDGI 594
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
5-193 7.25e-24

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: 97.52  E-value: 7.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMD-------TLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 77
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  78 VdREQQGRLDVLVNNAYAGVQTilNTRskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQY 157
Cdd:cd09762   81 A-VEKFGGIDILVNNASAISLT--GTL-----DTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNP 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296214664 158 MF---NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWP 193
Cdd:cd09762  153 KWfknHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
5-181 7.59e-24

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: 97.55  E-value: 7.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLgGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAY-GECIAIPADLSSEEGIEALVARV-AERSD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAgvqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR----GLIVVISSPGGL--QYM 158
Cdd:cd08942   82 RLDVLVNNAGA-------TWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIvvSGL 154
                        170       180
                 ....*....|....*....|...
gi 296214664 159 FNVPYGVGKAACDKLAADCAHEL 181
Cdd:cd08942  155 ENYSYGASKAAVHQLTRKLAKEL 177
PRK08278 PRK08278
SDR family oxidoreductase;
3-193 7.72e-24

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 98.05  E-value: 7.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR----HMD---TLRVAAQEAQSLGGQCVPVVCDSSQESEVRslf 75
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaepHPKlpgTIHTAAEEIEAAGGQALPLVGDVRDEDQVA--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  76 EQVDR--EQQGRLDVLVNNAYA----GVQtilntrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVI 149
Cdd:PRK08278  79 AAVAKavERFGGIDICVNNASAinltGTE-----------DTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTL 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 150 SSPGGL-QYMF--NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWP 193
Cdd:PRK08278 148 SPPLNLdPKWFapHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
5-209 2.55e-23

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: 96.36  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 84
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilNTRSKAFWETPASmWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYM-FNVPY 163
Cdd:cd05329   84 KLNILVNN--AGT----NIRKEAKDYTEED-YSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVpSGAPY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEE 209
Cdd:cd05329  157 GATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKE 202
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-199 2.91e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 96.28  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhmDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK12829   5 LLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDV--SEAALAATAARLPGAKVTATVADVADPAQVERVFDTA-V 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNA-----YAGVQTIlntrskafweTPASmWDDINNVGLRGHYlcsvYGARLMVPAGR-----GLIVVIS 150
Cdd:PRK12829  82 ERFGGLDVLVNNAgiagpTGGIDEI----------TPEQ-WEQTLAVNLNGQF----YFARAAVPLLKasghgGVIIALS 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296214664 151 SPGG-LQYMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK12829 147 SVAGrLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
5-208 4.05e-23

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: 95.68  E-value: 4.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERT-VEALG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTILNTRSKAFWETPAsmwdDINNVGLrghylcsVYGAR----LMVPAGRGLIVVISSPGGLQYMFN 160
Cdd:cd08934   80 RLDILVNNAGIMLLGPVEDADTTDWTRMI----DTNLLGL-------MYTTHaalpHHLLRNKGTIVNISSVAGRVAVRN 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296214664 161 -VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTElLKEHMAKE 208
Cdd:cd08934  149 sAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTE-LRDHITHT 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
7-200 8.26e-23

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: 95.14  E-value: 8.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMD-TLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQA-VEKFGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGLQYMFNVP-Y 163
Cdd:cd05366   81 FDVMVNN--AGIAPI-----TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNLGaY 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05366  154 SASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
7-200 8.27e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 94.78  E-value: 8.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAqslggQCVPVVCDSSQESEVRSLFeqvdrEQQGRL 86
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGET-----GCEPLRLDVGDDAAIRAAL-----AAAGAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGLQ-YMFNVPYG 164
Cdd:PRK07060  79 DGLVNC--AGI-----ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVgLPDHLAYC 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 165 VGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK07060 152 ASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
5-234 2.90e-22

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 93.54  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYitgrhMDTLRVAAQEAQSLggqcVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVV-----NADIHGGDGQHENY----QFVPTDVSSAEEVNHTVAEI-IEKFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTIL----NTRSKafWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGL----- 155
Cdd:PRK06171  77 RIDGLVNNAGINIPRLLvdekDPAGK--YELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLegseg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 156 QYMfnvpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhMAKEEGL---QDPVFKQLRSVFSSAETTEM- 231
Cdd:PRK06171 155 QSC----YAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRT-PEYEEALaytRGITVEQLRAGYTKTSTIPLg 229

                 ....
gi 296214664 232 -SGK 234
Cdd:PRK06171 230 rSGK 233
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
5-200 6.32e-22

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: 92.65  E-value: 6.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVV-CDSSQESEVRSLFEQVdREQQ 83
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVpLDMSDLEDAEQVVEEA-LKLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAyagvqtILNTRSKaFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLqymFNVPY 163
Cdd:cd05332   80 GGLDILINNA------GISMRSL-FHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGK---IGVPF 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 164 GVGKAAcDKLA----ADC-AHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05332  150 RTAYAA-SKHAlqgfFDSlRAELSEPNISVTVVCPGLIDTNI 190
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
9-251 6.44e-22

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: 91.92  E-value: 6.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:cd05324    2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFV-EEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNayAGVQTILNTRSKAFWETpASMWDDINnvglrghylcsVYGARLM----------VPAGRglIVVISSPGGLQy 157
Cdd:cd05324   81 ILVNN--AGIAFKGFDDSTPTREQ-ARETMKTN-----------FFGTVDVtqallpllkkSPAGR--IVNVSSGLGSL- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 mfNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEllkehMAKEEGLQDPvfkqlrsvfssaettEMSGKCVV 237
Cdd:cd05324  144 --TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTD-----MGGGKAPKTP---------------EEGAETPV 201
                        250
                 ....*....|....
gi 296214664 238 ALATDPNILSLSGK 251
Cdd:cd05324  202 YLALLPPDGEPTGK 215
PRK12937 PRK12937
short chain dehydrogenase; Provisional
3-200 1.26e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 91.34  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdRE 81
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAA-ET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNayAGVQTILNTRskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRglIVVIS-SPGGLQYMFN 160
Cdd:PRK12937  80 AFGRIDVLVNN--AGVMPLGTIA-----DFDLEDFDRTIATNLRGAFVVLREAARHLGQGGR--IINLStSVIALPLPGY 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK12937 151 GPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK12743 PRK12743
SDR family oxidoreductase;
8-198 2.66e-21

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 90.86  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRH-MDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSdEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKL-IQRLGRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVqtilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISS-------PGGlqym 158
Cdd:PRK12743  82 DVLVNNAGAMT-------KAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSvhehtplPGA---- 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 296214664 159 fnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK12743 151 --SAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIAT 188
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
7-251 2.68e-21

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: 91.13  E-value: 2.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMD-TLRVAAQEAQSLGGQCVPVV-CD-SSQESeVRSLFEQVdREQQ 83
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEkGEEAAAEIKKETGNAKVEVIqLDlSSLAS-VRQFAEEF-LARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVQTIlntrskAFWETPasmwDDIN-----NvglrghYLCSVYGARLMVPAGR----GLIVVISSpgG 154
Cdd:cd05327   79 PRLDILINN--AGIMAP------PRRLTK----DGFElqfavN------YLGHFLLTNLLLPVLKasapSRIVNVSS--I 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 155 LQYM-----------FNVPYGVGKAACD-KLAA-----DCAHELRRYGVSYVSLWPGIVQTELLKEHmakeeglqdPVFK 217
Cdd:cd05327  139 AHRAgpidfndldleNNKEYSPYKAYGQsKLANilftrELARRLEGTGVTVNALHPGVVRTELLRRN---------GSFF 209
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 296214664 218 QLRSVFS--SAETTEMSGKCVVALATDPNILSLSGK 251
Cdd:cd05327  210 LLYKLLRpfLKKSPEQGAQTALYAATSPELEGVSGK 245
PRK06841 PRK06841
short chain dehydrogenase; Provisional
4-210 3.93e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 90.49  E-value: 3.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQL---LGGNAKGLVCDVSDSQSVEAAVAAV-ISAF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVQTIlntrSKAFwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VP 162
Cdd:PRK06841  88 GRIDILVNS--AGVALL----APAE-DVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERhVA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:PRK06841 161 YCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKG 208
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
9-257 6.82e-21

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: 89.28  E-value: 6.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 88
Cdd:cd05323    2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKA-IEKFGRVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNAyagvqTILNTRSKAFWETPASMWDDINNVGLRGhylcSVYGARLMVPAGR-------GLIVVISSPGGLQYMFNV 161
Cdd:cd05323   81 LINNA-----GILDEKSYLFAGKLPPPWEKTIDVNLTG----VINTTYLALHYMDknkggkgGVIVNIGSVAGLYPAPQF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 162 P-YGVGKAACDKLAADCAHEL-RRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQlrsvfssaeTTEMSGKCVVAL 239
Cdd:cd05323  152 PvYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQ---------SPEVVAKAIVYL 222
                        250
                 ....*....|....*...
gi 296214664 240 ATDPnilSLSGKVLPSCD 257
Cdd:cd05323  223 IEDD---EKNGAIWIVDG 237
PRK08589 PRK08589
SDR family oxidoreductase;
5-242 7.66e-21

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 89.84  E-value: 7.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEI-KEQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAyaGVqtilNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGrGLIVVISSPGGLQY-MFNVPY 163
Cdd:PRK08589  82 RVDVLFNNA--GV----DNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAAdLYRSGY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLR---SVFSSAETTEMSGKCVVALA 240
Cdd:PRK08589 155 NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFRENQkwmTPLGRLGKPEEVAKLVVFLA 234

                 ..
gi 296214664 241 TD 242
Cdd:PRK08589 235 SD 236
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-186 9.91e-21

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 90.23  E-value: 9.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHMDTLRVA--AQEAQSLGGQCVPVVCDSSQESEVRSLFEQV 78
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATV-VVNDVASALDASdvLDEIRAAGAKAVAVAGDISQRATADELVATA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  79 DreQQGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYL-----CSVYGARLMVPAGR--GLIVVISS 151
Cdd:PRK07792  85 V--GLGGLDIVVNN--AGI-----TRDRMLFNMSDEEWDAVIAVHLRGHFLltrnaAAYWRAKAKAAGGPvyGRIVNTSS 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 152 PGGLQYMFNVP-YGVGKAACDKLAADCAHELRRYGV 186
Cdd:PRK07792 156 EAGLVGPVGQAnYGAAKAGITALTLSAARALGRYGV 191
PRK07774 PRK07774
SDR family oxidoreductase;
6-199 1.04e-20

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 89.03  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADAT-VSAFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNA--YAGVQ-TILNTrskafweTPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqYMFNVP 162
Cdd:PRK07774  84 IDYLVNNAaiYGGMKlDLLIT-------VPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAA--WLYSNF 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK07774 155 YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE 191
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
11-234 1.30e-20

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: 88.51  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAG-ATVYITGRHMDtlrvAAQEAQSLGGQCVPVVC---DSSqeSEVRSLFEQV-DREQQGR 85
Cdd:cd05325    2 LITGASRGIGLELVRQLLARGnNTVIATCRDPS----AATELAALGASHSRLHIlelDVT--DEIAESAEAVaERLGDAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNayAGVQTILNTRSkafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGG----LQYMFNV 161
Cdd:cd05325   76 LDVLINN--AGILHSYGPAS----EVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigdNTSGGWY 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhMAKEEGLQDPVF--KQLRSVFSSAeTTEMSGK 234
Cdd:cd05325  150 SYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGP-FAKNKGPITPEEsvAGLLKVIDNL-NEEDSGK 222
PRK09242 PRK09242
SDR family oxidoreductase;
5-233 1.78e-20

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 88.65  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 82
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDElaEEFPEREVHGLAADVSDDEDRRAILDWVE-DH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilNTRSKAFWETPASmWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-V 161
Cdd:PRK09242  86 WDGLHILVNN--AGG----NIRKAAIDYTEDE-WRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSgA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQdPVFKQ--LRSVfssAETTEMSG 233
Cdd:PRK09242 159 PYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE-QVIERtpMRRV---GEPEEVAA 228
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
9-211 2.13e-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: 88.29  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINdLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQA-WEDFGRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNayAGVQTilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMV-----PAG--RGLIVVISSPGGLQYMFN 160
Cdd:cd05337   82 CLVNN--AGIAV---RPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpdrFDGphRSIIFVTSINAYLVSPNR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGL 211
Cdd:cd05337  157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDEL 207
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
9-205 2.21e-20

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: 87.42  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRvaaqeAQSLGGQCV-PVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:cd08932    2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLA-----ALSASGGDVeAVPYDARDPEDARALVDAL-RDRFGRID 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNAYAGVQTILNTRSKAFWEtpaSMWdDINnvglrghylcsVYGARLMV--------PAGRGLIVVISS-PGGLQYM 158
Cdd:cd08932   76 VLVHNAGIGRPTTLREGSDAELE---AHF-SIN-----------VIAPAELTrallpalrEAGSGRVVFLNSlSGKRVLA 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 159 FNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHM 205
Cdd:cd08932  141 GNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLT 187
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
6-245 2.48e-20

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: 87.95  E-value: 2.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCV-PVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd05343    5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAI-RTQHQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGvqtilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLM--VPAGRGLIVVISSPGG----LQYM 158
Cdd:cd05343   84 GVDVCINNAGLA-------RPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININSMSGhrvpPVSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 159 FNVpYGVGKAACDKLAADCAHELR--RYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLRSVfssaETTEMSGKCV 236
Cdd:cd05343  157 FHF-YAATKHAVTALTEGLRQELReaKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCL----KPEDVANAVL 231

                 ....*....
gi 296214664 237 VALATDPNI 245
Cdd:cd05343  232 YVLSTPPHV 240
PRK07814 PRK07814
SDR family oxidoreductase;
7-253 3.79e-20

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 87.91  E-value: 3.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQA-VEAFGRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNN-AYAGVQTILNTrskafweTPASMWDDIN-NVGlRGHYLcSVYGARLMV-PAGRGLIVVISSPGG-LQYMFNVP 162
Cdd:PRK07814  89 DIVVNNvGGTMPNPLLST-------STKDLADAFTfNVA-TAHAL-TVAAVPLMLeHSGGGSVINISSTMGrLAGRGFAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 163 YGVGKAACD---KLAA-DCAHELRRYGVSyvslwPGIVQTELLKEHMAKEEgLQDPVFKQ--LRSVFSSAETtemsGKCV 236
Cdd:PRK07814 160 YGTAKAALAhytRLAAlDLCPRIRVNAIA-----PGSILTSALEVVAANDE-LRAPMEKAtpLRRLGDPEDI----AAAA 229
                        250
                 ....*....|....*..
gi 296214664 237 VALATdPNILSLSGKVL 253
Cdd:PRK07814 230 VYLAS-PAGSYLTGKTL 245
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
9-202 3.93e-20

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: 87.24  E-value: 3.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 88
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKAT-VSQFGGITI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNAYAG------VQTILNTRSKAFWETPASMWddinnvglRGHYLCsvygARLMVPAGRGLIVVISSPGGLQYMFNV- 161
Cdd:cd05365   80 LVNNAGGGgpkpfdMPMTEEDFEWAFKLNLFSAF--------RLSQLC----APHMQKAGGGAILNISSMSSENKNVRIa 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:cd05365  148 AYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALA 188
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
7-230 4.45e-20

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: 86.92  E-value: 4.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE----AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 82
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeANASGQKVSYISADLSDYEEVEQAFAQAV-EK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-V 161
Cdd:cd08939   80 GGPPDLVVNC--AGI-----SIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGyS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhmakEEGLQDPVFKQLrSVFSSAETTE 230
Cdd:cd08939  153 AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEE----ENKTKPEETKAI-EGSSGPITPE 216
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
6-205 5.19e-20

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 87.40  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQ 83
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEinAEYGEGMAYGFGADATSEQSVLALSRGVD-EIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAyaGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAG-RGLIVVISSPGG-LQYMFNV 161
Cdd:PRK12384  80 GRVDLLVYNA--GI-----AKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGkVGSKHNS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGivqtELLKEHM 205
Cdd:PRK12384 153 GYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG----NLLKSPM 192
PRK06124 PRK06124
SDR family oxidoreductase;
7-215 6.32e-20

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 87.08  E-value: 6.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 86
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAE-HGRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAgvqtiLNTRSKAfwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGV 165
Cdd:PRK06124  90 DILVNNVGA-----RDRRPLA--ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGdAVYPA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296214664 166 GKAACDKLAADCAHELRRYGVSYVSLWPGIVQTElLKEHMAKEEGLQDPV 215
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE-TNAAMAADPAVGPWL 211
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
5-202 6.99e-20

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 86.82  E-value: 6.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFeQVDREQQG 84
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALA-DFALSKLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGvqtilntRSKAFwETPAS--MWDDINNVGLRGHyLCSVyGARLMVPAGRGLIVVISSPGGLQYMFNV- 161
Cdd:PRK06113  88 KVDILVNNAGGG-------GPKPF-DMPMAdfRRAYELNVFSFFH-LSQL-VAPEMEKNGGGVILTITSMAAENKNINMt 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK06113 158 SYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALK 198
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
5-202 7.04e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 86.73  E-value: 7.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKD-IG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQtilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSpggLQYMFN---- 160
Cdd:PRK08085  86 PIDVLINN--AGIQ-----RRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICS---MQSELGrdti 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK08085 156 TPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
PRK06138 PRK06138
SDR family oxidoreductase;
5-207 8.41e-20

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 86.74  E-value: 8.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQEAQSL--GGQCVPVVCDSSQESEVRSLFEQVDREq 82
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEA---AERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAAR- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNAYAGVQTILNTrskafweTPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYM-FNV 161
Cdd:PRK06138  79 WGRLDVLVNNAGFGCGGTVVT-------TDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGrGRA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAK 207
Cdd:PRK06138 152 AYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFAR 197
PRK06484 PRK06484
short chain dehydrogenase; Validated
6-214 1.08e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.14  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRvaaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGR 85
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERAR---ERADSLGPDHHALAMDVSDEAQIREGFEQLHR-EFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAyagvqTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGL-IVVISSPGGLQYMFN-VPY 163
Cdd:PRK06484  80 IDVLVNNA-----GVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKrTAY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhmAKEEGLQDP 214
Cdd:PRK06484 155 SASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAE--LERAGKLDP 203
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
6-242 1.25e-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: 86.35  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHmDTLRVAAQEAQSLGGQCVPVV---CDSSQESEVRSLFEQVDReQ 82
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFG-DAAEIEAVRAGLAAKHGVKVLyhgADLSKPAAIEDMVAYAQR-Q 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGhylcSVYGARLMVPA----GRGLIVVISSPGGL-QY 157
Cdd:cd08940   79 FGGVDILVNN--AGIQHV-----APIEDFPTEKWDAIIALNLSA----VFHTTRLALPHmkkqGWGRIINIASVHGLvAS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK---EHMAKEEGlqDPVFKQLRSVFSSAE------T 228
Cdd:cd08940  148 ANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEkqiSALAQKNG--VPQEQAARELLLEKQpskqfvT 225
                        250
                 ....*....|....
gi 296214664 229 TEMSGKCVVALATD 242
Cdd:cd08940  226 PEQLGDTAVFLASD 239
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
5-98 1.44e-19

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: 85.98  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGqcvpVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLHT----IVLDVADPASIAALAEQV-TAEFP 77
                         90
                 ....*....|....
gi 296214664  85 RLDVLVNNayAGVQ 98
Cdd:COG3967   78 DLNVLINN--AGIM 89
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
5-206 1.65e-19

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: 86.05  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd08945    1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAA-VARYG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAyagvqtilnTRS--KAFWETPASMWDDINNVGLRGHYLCS--VYGARLMVPAGRGLIVVISSPGGLQ-YMF 159
Cdd:cd08945   80 PIDVLVNNA---------GRSggGATAELADELWLDVVETNLTGVFRVTkeVLKAGGMLERGTGRIINIASTGGKQgVVH 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296214664 160 NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL---LKEHMA 206
Cdd:cd08945  151 AAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMaasVREHYA 200
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
7-258 1.69e-19

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: 86.37  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQg 84
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEirRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTILNTRSKAFWETPASmwddINNVglrGHYLCSVYGARLMVPAGRGLIVVISS----PGGLQY--- 157
Cdd:cd09807   80 RLDVLINN--AGVMRCPYSKTEDGFEMQFG----VNHL---GHFLLTNLLLDLLKKSAPSRIVNVSSlahkAGKINFddl 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFNVPYGVGKAAC-DKLA-----ADCAHELRRYGVSYVSLWPGIVQTELLKeHMAKEEGLQDPVFKQLRSVFssAETTEM 231
Cdd:cd09807  151 NSEKSYNTGFAYCqSKLAnvlftRELARRLQGTGVTVNALHPGVVRTELGR-HTGIHHLFLSTLLNPLFWPF--VKTPRE 227
                        250       260
                 ....*....|....*....|....*..
gi 296214664 232 SGKCVVALATDPNILSLSGKVLPSCDL 258
Cdd:cd09807  228 GAQTSIYLALAEELEGVSGKYFSDCKL 254
PRK06057 PRK06057
short chain dehydrogenase; Provisional
1-242 1.82e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 85.94  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVvcDSSQESEVRSLFEQVDr 80
Cdd:PRK06057   1 LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE---VGGLFVPT--DVTDEDAVNALFDTAA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVQ-----TILNTRSKAfwetpasmWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSpggl 155
Cdd:PRK06057  75 ETYGSVDIAFNN--AGISppeddSILNTGLDA--------WQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTAS---- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 156 qymF---------NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKeeglqDPVFKQLRSVF--- 223
Cdd:PRK06057 141 ---FvavmgsatsQISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAK-----DPERAARRLVHvpm 212
                        250       260
                 ....*....|....*....|
gi 296214664 224 -SSAETTEMSGkCVVALATD 242
Cdd:PRK06057 213 gRFAEPEEIAA-AVAFLASD 231
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
9-253 2.66e-19

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: 85.03  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGAT--VYITGRHMDTLRvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQ-ELKEELRPGLRVTTVKADLSDAAGVEQLLEAI-RKLDGER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVqtiLNTRSKAFwetPASMwDDINNvglrgHYLCSVYGARLMV----PAGR-----GLIVVISSPGGLQY 157
Cdd:cd05367   79 DLLINN--AGS---LGPVSKIE---FIDL-DELQK-----YFDLNLTSPVCLTstllRAFKkrglkKTVVNVSSGAAVNP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFN-VPYGVGKAACDKLAADCAHELrrYGVSYVSLWPGIVQTELLKEhmAKEEGLQDPVFKQLRSVFSSAE--TTEMSGK 234
Cdd:cd05367  145 FKGwGLYCSSKAARDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQRE--IRETSADPETRSRFRSLKEKGEllDPEQSAE 220
                        250
                 ....*....|....*....
gi 296214664 235 CVVALAtdPNILSLSGKVL 253
Cdd:cd05367  221 KLANLL--EKDKFESGAHV 237
PRK06198 PRK06198
short chain dehydrogenase; Provisional
3-199 2.85e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 85.44  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrE 81
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAAD-E 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAYagvqtiLNTRSkAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAG-RGLIVVI---SSPGGLQY 157
Cdd:PRK06198  81 AFGRLDALVNAAG------LTDRG-TILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIgsmSAHGGQPF 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 158 MfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK06198 154 L--AAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK12746 PRK12746
SDR family oxidoreductase;
5-241 3.43e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 85.09  E-value: 3.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 83
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GR-----LDVLVNNAYAGVQ-TILNTRSKAFwetpasmwDDINNVGLRGHYLCSVYGARLMVPAGRgLIVVISSPGGLQY 157
Cdd:PRK12746  84 IRvgtseIDILVNNAGIGTQgTIENTTEEIF--------DEIMAVNIKAPFFLIQQTLPLLRAEGR-VINISSAEVRLGF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELlkehmaKEEGLQDPVFKQL---RSVFSSAETTEMSGK 234
Cdd:PRK12746 155 TGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI------NAKLLDDPEIRNFatnSSVFGRIGQVEDIAD 228

                 ....*..
gi 296214664 235 CVVALAT 241
Cdd:PRK12746 229 AVAFLAS 235
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
9-181 4.59e-19

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: 84.36  E-value: 4.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLR-VAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLD 87
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEaLLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEE-IGPLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNAYAGVQ-TILntrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGV 165
Cdd:cd05373   80 VLVYNAGANVWfPIL--------ETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGfAAFAG 151
                        170
                 ....*....|....*.
gi 296214664 166 GKAACDKLAADCAHEL 181
Cdd:cd05373  152 AKFALRALAQSMAREL 167
PRK12827 PRK12827
short chain dehydrogenase; Provisional
3-215 6.22e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 84.39  E-value: 6.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSL----GGQCVPVVCDSSQESEVRSLFEqV 78
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGieaaGGKALGLAFDVRDFAATRAALD-A 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  79 DREQQGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHY-LCSVYGARLMVPAGRGLIVVISSPGGLqy 157
Cdd:PRK12827  81 GVEEFGRLDILVNN--AGI-----ATDAAFAELSIEEWDDVIDVNLDGFFnVTQAALPPMIRARRGGRIVNIASVAGV-- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296214664 158 MFN---VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLkEHMAKEEGLQDPV 215
Cdd:PRK12827 152 RGNrgqVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMA-DNAAPTEHLLNPV 211
PRK07825 PRK07825
short chain dehydrogenase; Provisional
4-200 6.23e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 84.61  E-value: 6.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAqslgGQCVPVVCDSSQESEVRSLFEQVDReQQ 83
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEA-DL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGhylcSVYGARL----MVPAGRGLIVVISSPGGlqyMF 159
Cdd:PRK07825  77 GPIDVLVNN--AGVMPV-----GPFLDEPDAVTRRILDVNVYG----VILGSKLaaprMVPRGRGHVVNVASLAG---KI 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 160 NVP----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK07825 143 PVPgmatYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTEL 187
PRK07074 PRK07074
SDR family oxidoreductase;
8-220 6.66e-19

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 84.44  E-value: 6.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLG-GQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADA---LGdARFVPVACDLTDAASLAAALANA-AAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVQTILNTRSKAFWETPasmwddiNNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVPYGVG 166
Cdd:PRK07074  79 DVLVANAGAARAASLHDTTPASWRAD-------NALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKeeglqDP-VFKQLR 220
Cdd:PRK07074 152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAA-----NPqVFEELK 201
PRK12828 PRK12828
short chain dehydrogenase; Provisional
1-205 7.25e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 83.69  E-value: 7.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDR 80
Cdd:PRK12828   1 MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAP--LSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 eQQGRLDVLVNNAYAGV-QTIlntrskafWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQY-M 158
Cdd:PRK12828  79 -QFGRLDALVNIAGAFVwGTI--------ADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAgP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 159 FNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHM 205
Cdd:PRK12828 150 GMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADM 196
PRK07454 PRK07454
SDR family oxidoreductase;
12-200 8.25e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 83.86  E-value: 8.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLVN 91
Cdd:PRK07454  11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAEL-LEQFGCPDVLIN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 NAYAGVQTILNtrskafwETPASMWDDINNVGLRGHYLCsvygARLMVPAGR----GLIVVISSPGGlqymFNV-----P 162
Cdd:PRK07454  90 NAGMAYTGPLL-------EMPLSDWQWVIQLNLTSVFQC----CSAVLPGMRarggGLIINVSSIAA----RNAfpqwgA 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
6-186 1.33e-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: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYI---------TGRHMDTLRVAAQEAQSLGGQCVPvvcDSSQESEVRSLFE 76
Cdd:cd05353    4 DGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVA---NYDSVEDGEKIVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  77 QVdREQQGRLDVLVNNAyagvqTILntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQ 156
Cdd:cd05353   81 TA-IDAFGRVDILVNNA-----GIL--RDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 296214664 157 YMF-NVPYGVGKAACDKLAADCAHELRRYGV 186
Cdd:cd05353  153 GNFgQANYSAAKLGLLGLSNTLAIEGAKYNI 183
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-200 1.41e-18

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: 83.15  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLVN 91
Cdd:cd05350    3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAE-LGGLDLVII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 NayAGVQTILNTRSKAFWETPASMwdDINNVGlrghylcSVYGARLMVPA----GRGLIVVISSPGGLQYMFNVP-YGVG 166
Cdd:cd05350   82 N--AGVGKGTSLGDLSFKAFRETI--DTNLLG-------AAAILEAALPQfrakGRGHLVLISSVAALRGLPGAAaYSAS 150
                        170       180       190
                 ....*....|....*....|....*....|....
gi 296214664 167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05350  151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
8-216 1.63e-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: 82.82  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLfEQVDREQQGRLD 87
Cdd:cd05360    1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERA-ADTAVERFGRID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHylcsVYGARLMVP----AGRGLIVVISSPGGLQYM-FNVP 162
Cdd:cd05360   80 TWVNN--AGVAVF-----GRFEDVTPEEFRRVFDVNYLGH----VYGTLAALPhlrrRGGGALINVGSLLGYRSApLQAA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296214664 163 YGVGKAAC----DKLAADCAHELRryGVSYVSLWPGIVQT---ELLKEHMAKEEGLQDPVF 216
Cdd:cd05360  149 YSASKHAVrgftESLRAELAHDGA--PISVTLVQPTAMNTpffGHARSYMGKKPKPPPPIY 207
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-194 2.79e-18

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 82.69  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHmDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK12823   2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAA-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNAyAGvqTIlntRSKAFWE-TPASMWDDINNVGLRGHYLCSvygARL--MVPAGRGLIVVISS--PGGL 155
Cdd:PRK12823  80 EAFGRIDVLINNV-GG--TI---WAKPFEEyEEEQIEAEIRRSLFPTLWCCR---AVLphMLAQGGGAIVNVSSiaTRGI 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296214664 156 QymfNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPG 194
Cdd:PRK12823 151 N---RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-242 2.89e-18

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 82.52  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdR 80
Cdd:PRK06463   1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKGVFTIK--CDVGNRDQVKKSKEVV-E 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVQTILntrskAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGL----- 155
Cdd:PRK06463  75 KEFGRVDVLVNN--AGIMYLM-----PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaae 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 156 QYMFnvpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEglqdpvFKQLRSVFSSAETTEMSGK- 234
Cdd:PRK06463 148 GTTF---YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEE------AEKLRELFRNKTVLKTTGKp 218
                        250
                 ....*....|...
gi 296214664 235 -----CVVALATD 242
Cdd:PRK06463 219 edianIVLFLASD 231
PRK06123 PRK06123
SDR family oxidoreductase;
8-200 3.63e-18

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 82.13  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHmdtlRVAAQEA-----QSLGGQCVPVVCDSSQESEVRSLFEQVDREq 82
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYLR----NRDAAEAvvqaiRRQGGEALAVAADVADEADVLRLFEAVDRE- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNAyagvqTILNTRSKaFWETPASMWDDINNVGLRGHYLCSVYGARLMVP--AGR-GLIVVISS-------P 152
Cdd:PRK06123  78 LGRLDALVNNA-----GILEAQMR-LEQMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRgGAIVNVSSmaarlgsP 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 153 GglQYmfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK06123 152 G--EY---IDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
6-244 3.91e-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: 82.20  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLG-GQCVPVVCDSSQESEVRSLFEqVDREQQG 84
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLIS-VTVERFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNA--YAGVQTILNTRSKAFwetpasmwDDINNVGLRGHYLCSVYgARLMVPAGRGLIVVISS-PGGLQYMFNV 161
Cdd:cd08933   87 RIDCLVNNAgwHPPHQTTDETSAQEF--------RDLLNLNLISYFLASKY-ALPHLRKSQGNIINLSSlVGSIGQKQAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhMAKEEGLQDPVFK--QLRSVFSSAETTEMSGKCVVAL 239
Cdd:cd08933  158 PYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEE-LAAQTPDTLATIKegELAQLLGRMGTEAESGLAALFL 236

                 ....*
gi 296214664 240 ATDPN 244
Cdd:cd08933  237 AAEAT 241
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
6-194 4.65e-18

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: 81.61  E-value: 4.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGG-QCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYL-EKFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTilntRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGL--------- 155
Cdd:cd08930   80 RIDILINNAYPSPKV----WGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriye 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 156 --QYMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPG 194
Cdd:cd08930  156 ntQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-151 6.38e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 82.66  E-value: 6.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDR 80
Cdd:PRK07109   2 MLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EqQGRLDVLVNNAYAGV-----QTILNTRSKAFwetpasmwdDINnvglrghYLCSVYGA----RLMVPAGRGLIVVISS 151
Cdd:PRK07109  82 E-LGPIDTWVNNAMVTVfgpfeDVTPEEFRRVT---------EVT-------YLGVVHGTlaalRHMRPRDRGAIIQVGS 144
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-212 1.10e-17

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 80.58  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRhmdTLRVAAQEAQSLGG----QCVPVVCDSSQESEVRSLFEQVDrEQQ 83
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEEYGftedQVRLKELDVTDTEECAEALAEIE-EEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGlrghyLCSVYG-ARLMVPA----GRGLIVVISSPGGLQYM 158
Cdd:PRK12824  79 GPVDILVNN--AGI-----TRDSVFKRMSHQEWNDVINTN-----LNSVFNvTQPLFAAmceqGYGRIINISSVNGLKGQ 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 159 FNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhmAKEEGLQ 212
Cdd:PRK12824 147 FGQTnYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQ--MGPEVLQ 199
PRK07832 PRK07832
SDR family oxidoreductase;
10-238 1.13e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.24  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  10 CVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQcVP--VVCDSSQESEVRSLFEQVDREqQGRLD 87
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGT-VPehRALDISDYDAVAAFAADIHAA-HGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNayAGVqtilntrskAFWETPASM----WDDINNVGLRGhylcSVYGARLMVP----AGR-GLIVVISSPGGLQYM 158
Cdd:PRK07832  81 VVMNI--AGI---------SAWGTVDRLtheqWRRMVDVNLMG----PIHVIETFVPpmvaAGRgGHLVNVSSAAGLVAL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 159 -FNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDPVFKQLRSVFSS-AETTEMSGKCV 236
Cdd:PRK07832 146 pWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGVDREDPRVQKWVDRFRGhAVTPEKAAEKI 225

                 ..
gi 296214664 237 VA 238
Cdd:PRK07832 226 LA 227
PRK09730 PRK09730
SDR family oxidoreductase;
9-200 1.17e-17

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 80.66  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRH-MDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRLD 87
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQnLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNAyagvqTILNTRSKAFWETPASmwddINNV---GLRGHYLCSVYGARLMV--PAGR-GLIVVISS-------PGg 154
Cdd:PRK09730  82 ALVNNA-----GILFTQCTVENLTAER----INRVlstNVTGYFLCCREAVKRMAlkHGGSgGAIVNVSSaasrlgaPG- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 296214664 155 lQYmfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK09730 152 -EY---VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK05855 PRK05855
SDR family oxidoreductase;
4-198 1.59e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.72  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWV-RAEH 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGVqtilntrSKAFWETPASMWDDINNVGLRGhylcSVYGARL----MVPAGR-GLIVVISSPGGLQYM 158
Cdd:PRK05855 391 GVPDIVVNNAGIGM-------AGGFLDTSAEDWDRVLDVNLWG----VIHGCRLfgrqMVERGTgGHIVNVASAAAYAPS 459
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 159 FNVP-YGVGKAACDKLaADCAH-ELRRYGVSYVSLWPGIVQT 198
Cdd:PRK05855 460 RSLPaYATSKAAVLML-SECLRaELAAAGIGVTAICPGFVDT 500
PRK07201 PRK07201
SDR family oxidoreductase;
4-93 1.72e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 82.69  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 83
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAE-H 446
                         90
                 ....*....|
gi 296214664  84 GRLDVLVNNA 93
Cdd:PRK07201 447 GHVDYLVNNA 456
PRK07063 PRK07063
SDR family oxidoreductase;
1-200 1.89e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 80.09  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQV 78
Cdd:PRK07063   1 MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAiaRDVAGARVLAVPADVTDAASVAAAVAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  79 DREqQGRLDVLVNNAYAGVqtilntrskafWETPASM----WDDINNVGLRGHYlcsvYGARL----MVPAGRGLIVVIS 150
Cdd:PRK07063  81 EEA-FGPLDVLVNNAGINV-----------FADPLAMtdedWRRCFAVDLDGAW----NGCRAvlpgMVERGRGSIVNIA 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296214664 151 S-------PGGLqymfnvPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK07063 145 SthafkiiPGCF------PYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQL 195
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
7-202 2.85e-17

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: 79.18  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE-AQSLGGQCVPVVCDSSQESEVrslFEQVDREQQGr 85
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEiEEKYGVETKTIAADFSAGDDI---YERIEKELEG- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDV--LVNNayAGvqtILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqyMFNVP- 162
Cdd:cd05356   77 LDIgiLVNN--VG---ISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAG---LIPTPl 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 163 ---YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:cd05356  149 latYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
PRK06949 PRK06949
SDR family oxidoreductase;
5-210 2.85e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 79.81  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETE-AG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilNTRSKAFWETPASmWDDINNVGLRGHYLCSVYGARLMVPAGRGL--------IVVISSPGGLQ 156
Cdd:PRK06949  86 TIDILVNN--SGV----STTQKLVDVTPAD-FDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 157 YMFNV-PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:PRK06949 159 VLPQIgLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQG 213
PRK07856 PRK07856
SDR family oxidoreductase;
6-211 2.92e-17

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 79.59  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHmdtlrvAAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR------APETVDGRPAEFHA--ADVRDPDQVAALVDAI-VERHGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGVQTILNTRSKAFWETpasmwddINNVGLRGHYLCSVYGARLMVP-AGRGLIVVISS-------PGglqy 157
Cdd:PRK07856  76 LDVLVNNAGGSPYALAAEASPRFHEK-------IVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSvsgrrpsPG---- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296214664 158 mfNVPYGVGKAACDKLAADCAHElrrYG--VSYVSLWPGIVQTELLKEHMAKEEGL 211
Cdd:PRK07856 145 --TAAYGAAKAGLLNLTRSLAVE---WApkVRVNAVVVGLVRTEQSELHYGDAEGI 195
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-214 6.47e-17

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 78.69  E-value: 6.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVaAQEAQSLGGQCVPVVCDSSQESEVRSLFEqVDREQQG 84
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKL-ADELCGRGHRCTAVVADVRDPASVAAAIK-RAKEKEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYlcSVYGARL--MVPAGRGLIVVISS--------PGg 154
Cdd:PRK08226  82 RIDILVNN--AGV-----CRLGSFLDMSDEDRDFHIDINIKGVW--NVTKAVLpeMIARKDGRIVMMSSvtgdmvadPG- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 155 lqymfNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLkEHMAKEEGLQDP 214
Cdd:PRK08226 152 -----ETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMA-ESIARQSNPEDP 205
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-199 6.54e-17

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 78.62  E-value: 6.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIIT-THGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEA-LEEFG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAyagvQTIlnTRSKAFwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISS----PGGlqyMFN 160
Cdd:PRK06935  91 KIDILVNNA----GTI--RRAPLL-EYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASmlsfQGG---KFV 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK06935 161 PAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-253 7.80e-17

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 78.61  E-value: 7.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-----MDTLRvaaqEAQSLGGQCVPVVCDSSQESEVRSLFeQVD 79
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKraeemNETLK----MVKENGGEGIGVLADVSTREGCETLA-KAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  80 REQQGRLDVLVNNAYAGVQTIlntrskaFWETPASMWDDINNVGLRGHYLCSVYGARLMvPAGrGLIVVISSPGGLQYMF 159
Cdd:PRK06077  79 IDRYGVADILVNNAGLGLFSP-------FLNVDDKLIDKHISTDFKSVIYCSQELAKEM-REG-GAIVNIASVAGIRPAY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 160 NVP-YGVGKAACDKLAADCAHELR-RYGVSYVSlwPGIVQTElLKEHMAKEEGLQDPVFKQLRSVFSSAETTEMSGKCVV 237
Cdd:PRK06077 150 GLSiYGAMKAAVINLTKYLALELApKIRVNAIA--PGFVKTK-LGESLFKVLGMSEKEFAEKFTLMGKILDPEEVAEFVA 226
                        250
                 ....*....|....*.
gi 296214664 238 ALATDPNIlslSGKVL 253
Cdd:PRK06077 227 AILKIESI---TGQVF 239
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
5-210 8.12e-17

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: 77.73  E-value: 8.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLrvaaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQg 84
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERL----AEAKKELPNIHTIVLDVGDAESVEALAEALLSEYP- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTILNTRSKAfwETPASMWDDInNVGLRGhylcSVYGARLMVP----AGRGLIVVISSPGGLQYMFN 160
Cdd:cd05370   78 NLDILINN--AGIQRPIDLRDPA--SDLDKADTEI-DTNLIG----PIRLIKAFLPhlkkQPEATIVNVSSGLAFVPMAA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 161 VP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:cd05370  149 NPvYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGG 199
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-200 8.90e-17

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 78.46  E-value: 8.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITG-RHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAA-QAAWGRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVQTIlnTRSKAFWETPASmWDDINNVGLRGHYLCSVYGARLMVpAGRGL-------IVVISSPGGLQYMF 159
Cdd:PRK12745  82 DCLVNN--AGVGVK--VRGDLLDLTPES-FDRVLAINLRGPFFLTQAVAKRML-AQPEPeelphrsIVFVSSVNAIMVSP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 160 N-VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK12745 156 NrGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
4-218 9.80e-17

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: 78.34  E-value: 9.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAqEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLA-EILAAGDAAHVHTADLETYAGAQGVVRAA-VERF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGV----------QTILNTRSKAFWETpasMWddinnvglrghylCSVYGARLMVPAGRGLIVVISS-- 151
Cdd:cd08937   79 GRVDVLINNVGGTIwakpyehyeeEQIEAEIRRSLFPT---LW-------------CCRAVLPHMLERQQGVIVNVSSia 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 152 -PGGLQymfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK-EHMAKEEGLQDPVFKQ 218
Cdd:cd08937  143 tRGIYR----IPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKiPRNAAPMSEQEKVWYQ 207
PRK06179 PRK06179
short chain dehydrogenase; Provisional
5-244 9.87e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 78.41  E-value: 9.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHmdtlrvaAQEAQSLGGqcVP-VVCDSSQESEVRSLFEQVdREQQ 83
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRN-------PARAAPIPG--VElLELDVTDDASVQAAVDEV-IARA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGVQTILNTRSKAfwetPASMWDDINNVGLrghylcsVYGARLMVP----AGRGLIVVISSPGGL---Q 156
Cdd:PRK06179  72 GRIDVLVNNAGVGLAGAAEESSIA----QAQALFDTNVFGI-------LRMTRAVLPhmraQGSGRIINISSVLGFlpaP 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 157 YMfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL----------LKEHMAKEEGLQdpvfKQLRSVFSSA 226
Cdd:PRK06179 141 YM--ALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFdanapepdspLAEYDRERAVVS----KAVAKAVKKA 214
                        250
                 ....*....|....*...
gi 296214664 227 ETTEMSGKCVVALATDPN 244
Cdd:PRK06179 215 DAPEVVADTVVKAALGPW 232
PRK07791 PRK07791
short chain dehydrogenase; Provisional
5-213 1.01e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 78.56  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT--GRHMDTLRVAAQEAQSL-------GGQCVPVVCDSSQESEVRSLF 75
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdiGVGLDGSASGGSAAQAVvdeivaaGGEAVANGDDIADWDGAANLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  76 EQVdREQQGRLDVLVNNAyagvqTILntRSKAFWETPASMWDDINNVGLRGHYLCSVYGA---RLMVPAGRGL---IVVI 149
Cdd:PRK07791  84 DAA-VETFGGLDVLVNNA-----GIL--RDRMIANMSEEEWDAVIAVHLKGHFATLRHAAaywRAESKAGRAVdarIINT 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296214664 150 SSPGGLQYmfNV---PYGVGKAACDKLAADCAHELRRYGVSYVSLWPgIVQTEL----LKEHMAK-EEGLQD 213
Cdd:PRK07791 156 SSGAGLQG--SVgqgNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRMtetvFAEMMAKpEEGEFD 224
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
6-242 1.10e-16

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: 77.89  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQeaqslGGQCVPVVCDSSQESEVRSLFEQVDreqqgR 85
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER-----GPGITTRVLDVTDKEQVAALAKEEG-----R 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNA-YAGVQTILNTRSKAfwetpasmWDDINNVGLRGHYLcsVYGARL--MVPAGRGLIVVISSPGGlqYMFNVP 162
Cdd:cd05368   71 IDVLFNCAgFVHHGSILDCEDDD--------WDFAMNLNVRSMYL--MIKAVLpkMLARKDGSIINMSSVAS--SIKGVP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 163 ----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAK----EEGLQDPVFKQLRSVFSSAEttEMSGK 234
Cdd:cd05368  139 nrfvYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAqpdpEEALKAFAARQPLGRLATPE--EVAAL 216

                 ....*...
gi 296214664 235 CVVaLATD 242
Cdd:cd05368  217 AVY-LASD 223
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-203 1.51e-16

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 77.84  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQV-VDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGVQTILNTRskafweTPaSMWDDINNVGLRGhylcSVYGARLMVPAGR-----GLIVVISSPGGLQYMFN 160
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETI------TE-EQFDKVYNINVGG----VIWGIQAAQEAFKklghgGKIINATSQAGVVGNPE 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296214664 161 VP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:PRK08643 149 LAvYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFD 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
7-198 1.84e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 79.51  E-value: 1.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEG---AKKLAEALGDEHLSVQADITDEAAVESAFAQI-QARWGRL 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVQTILNTRskafwETPASMwDDINNVGLRGHYLCSVYGARLMvpAGRGLIVVISSPGGLQYMF-NVPYGV 165
Cdd:PRK06484 345 DVLVNNAGIAEVFKPSLE-----QSAEDF-TRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPpRNAYCA 416
                        170       180       190
                 ....*....|....*....|....*....|...
gi 296214664 166 GKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK06484 417 SKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
9-200 2.12e-16

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: 76.90  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 88
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKI-KKEVGDVTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYlcSVYGARL--MVPAGRGLIVVISSPGGLQY-MFNVPYGV 165
Cdd:cd05339   80 LINN--AGVVSG-----KKLLELPDEEIEKTFEVNTLAHF--WTTKAFLpdMLERNHGHIVTIASVAGLISpAGLADYCA 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 166 GKAACDKLAADCAHELRRY---GVSYVSLWPGIVQTEL 200
Cdd:cd05339  151 SKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTGM 188
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
11-199 2.16e-16

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: 76.94  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTL-RVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQgRLDVL 89
Cdd:cd05346    4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLqELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR-DIDIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  90 VNNayAGVQTILNTRSKAF---WETpasMWdDINNVGLrghylcsVYGARLMVPA----GRGLIVVISS-------PGGl 155
Cdd:cd05346   83 VNN--AGLALGLDPAQEADledWET---MI-DTNVKGL-------LNVTRLILPImiarNQGHIINLGSiagrypyAGG- 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296214664 156 qymfNVpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:cd05346  149 ----NV-YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK07890 PRK07890
short chain dehydrogenase; Provisional
5-210 2.42e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 77.31  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALA-LERFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAgVQTIlntrsKAFWETPASMWDDINNVglrghylcSVYGA----RLMVPA---GRGLIVVISS----PG 153
Cdd:PRK07890  82 RVDALVNNAFR-VPSM-----KPLADADFAHWRAVIEL--------NVLGTlrltQAFTPAlaeSGGSIVMINSmvlrHS 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 154 GLQYmfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK---EHMAKEEG 210
Cdd:PRK07890 148 QPKY---GAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfRHQAGKYG 204
PRK05650 PRK05650
SDR family oxidoreductase;
11-201 2.50e-16

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 77.39  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSlFEQVDREQQGRLDVLV 90
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTA-LAQACEEKWGGIDVIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNayAGVQTilntrSKAFWETPASMWD---DINNVGLrghylcsVYGARLMVPA----GRGLIVVISSPGGLQ---YMFN 160
Cdd:PRK05650  83 NN--AGVAS-----GGFFEELSLEDWDwqiAINLMGV-------VKGCKAFLPLfkrqKSGRIVNIASMAGLMqgpAMSS 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 161 vpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELL 201
Cdd:PRK05650 149 --YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLL 187
PRK06114 PRK06114
SDR family oxidoreductase;
5-242 2.60e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 77.13  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDT-LRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 83
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAE-L 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAyagvqTILNtrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGL---QYMFN 160
Cdd:PRK06114  85 GALTLAVNAA-----GIAN--ANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIivnRGLLQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL-LKEHMAKeeglQDPVFKQLRSVFSSAETTEMSGKCVVaL 239
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMnTRPEMVH----QTKLFEEQTPMQRMAKVDEMVGPAVF-L 232

                 ...
gi 296214664 240 ATD 242
Cdd:PRK06114 233 LSD 235
PRK06947 PRK06947
SDR family oxidoreductase;
8-200 2.74e-16

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 76.77  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 86
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSA-FGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVQtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPA--GR-GLIVVISSPGGL-----QYm 158
Cdd:PRK06947  82 DALVNN--AGIV----APSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrgGRgGAIVNVSSIASRlgspnEY- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 159 fnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK06947 155 --VDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
6-199 2.94e-16

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 77.25  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI-LEDFGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNA--------YAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQY 157
Cdd:PRK08277  88 CDILINGAggnhpkatTDNEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTP 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 158 MFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK08277 168 LTKVPaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
5-200 3.13e-16

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: 76.29  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHMDTLRVAAQEAQSlggQCVPVVCDSSQESEVRSLFEQVDreqq 83
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGD---KVVPLRLDVTDPESIKAAAAQAK---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 gRLDVLVNNayAGVQTILNTRSKAFWET-PASMwdDINNVGLRGhyLCSVYgARLMVPAGRGLIVVISSPGGLQymfNVP 162
Cdd:cd05354   74 -DVDVVINN--AGVLKPATLLEEGALEAlKQEM--DVNVFGLLR--LAQAF-APVLKANGGGAIVNLNSVASLK---NFP 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 296214664 163 ----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05354  143 amgtYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRM 184
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
7-185 6.80e-16

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 78.04  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 84
Cdd:COG3347  425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAElgGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGvqtilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRG-LIVVISSPGGLQYmfnvPY 163
Cdd:COG3347  505 SDIGVANAGIAS--------SSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGgSSVFAVSKNAAAA----AY 572
                        170       180
                 ....*....|....*....|..
gi 296214664 164 GVGKAACDKLAAdcAHELRRYG 185
Cdd:COG3347  573 GAAAAATAKAAA--QHLLRALA 592
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
5-210 7.46e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 75.87  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKE-VG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSpgglqyMFNV--- 161
Cdd:PRK07097  87 VIDILVNN--AGI-----IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICS------MMSElgr 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296214664 162 ----PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIV---QTELLKEHMAKEEG 210
Cdd:PRK07097 154 etvsAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIatpQTAPLRELQADGSR 209
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
5-254 9.17e-16

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: 75.63  E-value: 9.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLG--GQCVPVVCDSSQESEVRSlFEQVDREQ 82
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEA-YVDATVEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVQTILNTrSKAFwetPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-V 161
Cdd:cd05330   80 FGRIDGFFNN--AGIEGKQNL-TEDF---GADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNqS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMaKEEGLQDPvfKQLRSVFSSAETTEMSGK-----CV 236
Cdd:cd05330  154 GYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSL-KQLGPENP--EEAGEEFVSVNPMKRFGEpeevaAV 230
                        250
                 ....*....|....*....
gi 296214664 237 VA-LATDPNILsLSGKVLP 254
Cdd:cd05330  231 VAfLLSDDAGY-VNAAVVP 248
PRK05875 PRK05875
short chain dehydrogenase; Provisional
11-201 9.49e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 75.61  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 88
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEieALKGAGAVRYEPADVTDEDQVARAVDAA-TAWHGRLHG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNAyAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISS--PGGLQYMFNvPYGVG 166
Cdd:PRK05875  90 VVHCA-GGSETI-----GPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSiaASNTHRWFG-AYGVT 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 296214664 167 KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELL 201
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLV 197
PRK09072 PRK09072
SDR family oxidoreductase;
6-93 1.33e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 74.98  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaQSLGGQCVPVVCDSSQESEVRSLFEQVdrEQQGR 85
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAAR-LPYPGRHRWVVADLTSEAGREAVLARA--REMGG 80

                 ....*...
gi 296214664  86 LDVLVNNA 93
Cdd:PRK09072  81 INVLINNA 88
PRK07677 PRK07677
short chain dehydrogenase; Provisional
7-96 1.61e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 74.71  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQGRL 86
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQID-EKFGRI 79
                         90
                 ....*....|
gi 296214664  87 DVLVNNAyAG 96
Cdd:PRK07677  80 DALINNA-AG 88
PRK06182 PRK06182
short chain dehydrogenase; Validated
5-199 1.96e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 75.00  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLrvaaQEAQSLGGQCVPVvcDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKM----EDLASLGVHPLSL--DVTDEASIKAAVDTI-IAEEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVqtilntrskafwetpasmWDDINNVGL---RGHYLCSVYG-ARL-------MVPAGRGLIVVISSPG 153
Cdd:PRK06182  74 RIDVLVNNAGYGS------------------YGAIEDVPIdeaRRQFEVNLFGaARLtqlvlphMRAQRSGRIINISSMG 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 154 GLQY-MFNVPYGVGKAACDKLaADCAH-ELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK06182 136 GKIYtPLGAWYHATKFALEGF-SDALRlEVAPFGIDVVVIEPGGIKTE 182
PRK12747 PRK12747
short chain dehydrogenase; Provisional
5-225 3.02e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 73.96  E-value: 3.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 83
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GR-----LDVLVNNAYAGVQTILNtrskafwETPASMWDDINNVGLRGHYlcsvYGARLMVPAGR--GLIVVISSPGGLQ 156
Cdd:PRK12747  82 NRtgstkFDILINNAGIGPGAFIE-------ETTEQFFDRMVSVNAKAPF----FIIQQALSRLRdnSRIINISSAATRI 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 157 YMFN-VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELlkehmaKEEGLQDPVFKQLRSVFSS 225
Cdd:PRK12747 151 SLPDfIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM------NAELLSDPMMKQYATTISA 214
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
5-212 3.32e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 73.76  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyiTGrhmdtlrVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKV--IG-------FDQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAE-TG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqymfNVP-- 162
Cdd:PRK08220  76 PLDVLVNA--AGI-----LRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAA-----HVPri 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296214664 163 ----YGVGKAACDKLAADCAHELRRYGV--SYVSlwPGIVQTELLKEHMAKEEGLQ 212
Cdd:PRK08220 144 gmaaYGASKAALTSLAKCVGLELAPYGVrcNVVS--PGSTDTDMQRTLWVDEDGEQ 197
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
5-210 3.80e-15

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: 74.03  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIV-AQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVN-------NAYAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQY 157
Cdd:cd08935   82 TVDILINgaggnhpDATTDPEHYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296214664 158 MFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:cd08935  162 LTKVPaYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPDG 215
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
5-198 4.81e-15

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: 72.99  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGG---QCVPVVCDSSQESEVRSLFEQVDRE 81
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGrqpQWFILDLLTCTSENCQQLAQRIAVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 qQGRLDVLVNNAyagvqTILNTRSKAFWETPAsMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNV 161
Cdd:cd05340   82 -YPRLDGVLHNA-----GLLGDVCPLSEQNPQ-VWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 162 -PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:cd05340  155 gAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
1-151 5.81e-15

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 73.22  E-value: 5.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVD 79
Cdd:PRK08936   1 MYSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296214664  80 REqQGRLDVLVNNayAGVQTILNTRskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAG-RGLIVVISS 151
Cdd:PRK08936  81 KE-FGTLDVMINN--AGIENAVPSH-----EMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSS 145
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
8-242 6.68e-15

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: 72.88  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVyITGRHMDTLRvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 87
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARV-VVNYYRSTES-AEAVAAEAGERAIAIQADVRDRDQVQAMIEEA-KNHFGPVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 VLVNNAYAGVQTILNTRSKAFWETpasmWDDINN---VGLRGHYLCSVYGARLMVPAGRGLIVVISSpgGLQYMFNVPYG 164
Cdd:cd05349   78 TIVNNALIDFPFDPDQRKTFDTID----WEDYQQqleGAVKGALNLLQAVLPDFKERGSGRVINIGT--NLFQNPVVPYH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 165 ---VGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEllkehmAKEEGLQDPVFK------QLRSVFSSAETTEMsgkc 235
Cdd:cd05349  152 dytTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT------DASAATPKEVFDaiaqttPLGKVTTPQDIADA---- 221

                 ....*..
gi 296214664 236 VVALATD 242
Cdd:cd05349  222 VLFFASP 228
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
7-203 6.71e-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: 6.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITgrHMDTLRvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA--DIDEER-GADFAEAEGPNLFFVHGDVADETLVKFVVYAM-LEKLGRI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVQTILNTRskafwetPASMWDDINNVGLRGHYLCSVYGARLMVpAGRGLIVVISSPGGLQYMFNV-PYGV 165
Cdd:cd09761   77 DVLVNNAARGSKGILSSL-------LLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSeAYAA 148
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 166 GKAACDKLAADCAHELRRYgVSYVSLWPGIVQTELLKE 203
Cdd:cd09761  149 SKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQE 185
PLN02253 PLN02253
xanthoxin dehydrogenase
7-213 1.00e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 72.93  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYItgrhMDTLRVAAQE-AQSLGGQ--CVPVVCDSSQESEVRslfEQVD--RE 81
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCI----VDLQDDLGQNvCDSLGGEpnVCFFHCDVTVEDDVS---RAVDftVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAYAGVQTILNTRSKAFwetpaSMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqymfnV 161
Cdd:PLN02253  91 KFGTLDIMVNNAGLTGPPCPDIRNVEL-----SEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVAS------A 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 162 PYGVG-------KAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQD 213
Cdd:PLN02253 160 IGGLGphaytgsKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTED 218
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
5-242 1.08e-14

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 72.34  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYItgrHMDTLRVAAQ----EAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAEnlvnELGKEGHDVYAVQADVSKVEDANRLVEEA-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 EQQGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMF- 159
Cdd:PRK12935  80 NHFGKVDILVNN--AGI-----TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFg 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 160 NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEhmAKEEGLQDPVFKQLRSVFSSAETTemsGKCVVAL 239
Cdd:PRK12935 153 QTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAE--VPEEVRQKIVAKIPKKRFGQADEI---AKGVVYL 227

                 ...
gi 296214664 240 ATD 242
Cdd:PRK12935 228 CRD 230
PRK05872 PRK05872
short chain dehydrogenase; Provisional
4-241 1.17e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 73.08  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQC--VPVVCDSSQESEVRSLFEQVdRE 81
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAE---LGGDDrvLTVVADVTDLAAMQAAAEEA-VE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNayAGVQTilntrSKAFWETPASMWD---DINNVGlrghylcSVYGARLMVPA---GRGLIVVISS---- 151
Cdd:PRK05872  82 RFGGIDVVVAN--AGIAS-----GGSVAQVDPDAFRrviDVNLLG-------VFHTVRATLPAlieRRGYVLQVSSlaaf 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 152 ---PGGlqymfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAkeeglQDPVFKQLRSVFS-SAE 227
Cdd:PRK05872 148 aaaPGM------AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADA-----DLPAFRELRARLPwPLR 216
                        250
                 ....*....|....
gi 296214664 228 TTEMSGKCVVALAT 241
Cdd:PRK05872 217 RTTSVEKCAAAFVD 230
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
5-200 1.21e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 72.49  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSlfeQVDR--EQ 82
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRA---AIDAfeAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVQtilnTRSkAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISS-------PGgl 155
Cdd:PRK07523  85 IGPIDILVNN--AGMQ----FRT-PLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASvqsalarPG-- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 156 qymfNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK07523 156 ----IAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196
PRK06398 PRK06398
aldose dehydrogenase; Validated
5-214 1.43e-14

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 72.17  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQeaqslggqcvpVVCDSSQESEVRSLFEQVDReQQG 84
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY-----------FKVDVSNKEQVIKGIDYVIS-KYG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNV-PY 163
Cdd:PRK06398  72 RIDILVNN--AGIESY-----GAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAaAY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 164 GVGKAA----CDKLAADCAHELRrygvsYVSLWPGIVQTELLKEHMAKEEGlQDP 214
Cdd:PRK06398 145 VTSKHAvlglTRSIAVDYAPTIR-----CVAVCPGSIRTPLLEWAAELEVG-KDP 193
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
6-205 3.78e-14

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: 70.96  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDT-LRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENaEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVD-EIFK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAG-RGLIVVISSPGG-LQYMFNVP 162
Cdd:cd05322   80 RVDLLVYS--AGI-----AKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGkVGSKHNSG 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGivqtELLKEHM 205
Cdd:cd05322  153 YSAAKFGGVGLTQSLALDLAEHGITVNSLMLG----NLLKSPM 191
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-199 3.91e-14

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 70.70  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGrHMDTLRVAAQeAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVG-VAEAPETQAQ-VEALGRKFHFITADLIQQKDIDSIVSQA-VEVMG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGLQYMFNVP- 162
Cdd:PRK12481  83 HIDILINN--AGI-----IRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPs 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:PRK12481 156 YTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
7-203 4.00e-14

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: 70.81  E-value: 4.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    7 GQVCVVTGASRGIGRGIALQLCKAGATVYIT---------GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavGYPLATRAELDAVAAACPDQVLPVIADVRDPAALAAAVAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   78 VdREQQGRLDVLVnnAYAGVqtILNTRskAFWETPASMWDDINNVGLRGhylcsVYG-ARLMVPA-------GRGLIVVI 149
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGV--IAGGR--PLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 296214664  150 SSPGGLQYMFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
6-202 6.51e-14

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: 70.01  E-value: 6.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALA-KAKFGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGV-QTILNtrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVP------AGRGLIVVISSPGGLQ-Y 157
Cdd:cd05371   76 LDIVVNCAGIAVaAKTYN--KKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKnepdqgGERGVIINTASVAAFEgQ 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 158 MFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:cd05371  154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLA 198
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
7-200 1.04e-13

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: 69.42  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLggqcVPVVCDSSQESEVRSLFEQVdreqqGRL 86
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGI----EPVCVDLSDWDATEEALGSV-----GPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAG-RGLIVVISSPGGLQYMFN-VPYG 164
Cdd:cd05351   78 DLLVNN--AAVAIL-----QPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNhTVYC 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 165 VGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd05351  151 STKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK07831 PRK07831
SDR family oxidoreductase;
5-148 1.36e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 69.29  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGAS-RGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE-AQSLGGQCVP-VVCDSSQESEVRSLFEQVDrE 81
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADElAAELGLGRVEaVVCDVTSEAQVDALIDAAV-E 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296214664  82 QQGRLDVLVNNAYAGVQTILntrskafwetpASM----WDDINNVGLRGHYLCSVYGARLMVPAGRGLIVV 148
Cdd:PRK07831  94 RLGRLDVLVNNAGLGGQTPV-----------VDMtddeWSRVLDVTLTGTFRATRAALRYMRARGHGGVIV 153
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-210 2.72e-13

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: 68.26  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVyiTGrhmdtLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLVN 91
Cdd:cd05331    3 VTGAAQGIGRAVARHLLQAGATV--IA-----LDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAE-HGPIDALVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 naYAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqymfNVP------YGV 165
Cdd:cd05331   75 --CAGV-----LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAA-----HVPrismaaYGA 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 166 GKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:cd05331  143 SKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDG 187
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-187 2.96e-13

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 68.19  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR- 85
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSED---AAEAlADELGDRAIALQADVTDREQVQAMFATA-TEHFGKp 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGVQTILNTRSKAfwetPASMWDDINNvGLRGhylcSVYGARL--------MVPAGRGLIVVISSPgglqy 157
Cdd:PRK08642  82 ITTVVNNALADFSFDGDARKKA----DDITWEDFQQ-QLEG----SVKGALNtiqaalpgMREQGFGRIINIGTN----- 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 158 MFNVP------YGVGKAACDKLAADCAHELRRYGVS 187
Cdd:PRK08642 148 LFQNPvvpyhdYTTAKAALLGLTRNLAAELGPYGIT 183
PRK08264 PRK08264
SDR family oxidoreductase;
5-200 6.26e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 67.22  E-value: 6.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHMDTlrvaaqeAQSLGGQCVPVVCDSSQESEVRSLFEQVdreqq 83
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPES-------VTDLGPRVVPLQLDVTDPASVAAAAEAA----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNayAGVQTilntrskafweTPASMWDDiNNVGLRGHYLCSVYG----ARLMVPA----GRGLIVVISSPGGL 155
Cdd:PRK08264  72 SDVTILVNN--AGIFR-----------TGSLLLEG-DEDALRAEMETNYFGplamARAFAPVlaanGGGAIVNVLSVLSW 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296214664 156 qymFNVP----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK08264 138 ---VNFPnlgtYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM 183
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-212 7.58e-13

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 67.36  E-value: 7.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALE---IGPAAIAVSLDVTRQDSIDRIVAAAV-ERFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYA-GVQTILntrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRG-LIVVISSPGGLQYMFNVP 162
Cdd:PRK07067  80 GIDILFNNAALfDMAPIL--------DISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296214664 163 -YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL---LKEHMAKEEGLQ 212
Cdd:PRK07067 152 hYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMwdqVDALFARYENRP 205
PRK09291 PRK09291
SDR family oxidoreductase;
12-198 1.01e-12

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 66.95  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAG----ATVYITGRhMDTLRVAAQEaqslggqcvpvvCDSSQESEVRSLFEQVDREQQGRL- 86
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGhnviAGVQIAPQ-VTALRAEAAR------------RGLALRVEKLDLTDAIDRAQAAEWd 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 -DVLVNNAYAGvqtilntRSKAFWETPASMwddinnvgLRGHYLCSVYG--------ARLMVPAGRGLIVVISSPGGLqy 157
Cdd:PRK09291  74 vDVLLNNAGIG-------EAGAVVDIPVEL--------VRELFETNVFGpleltqgfVRKMVARGKGKVVFTSSMAGL-- 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 158 mFNVP----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK09291 137 -ITGPftgaYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
12-200 1.73e-12

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: 65.24  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGgqcvpVVCDSSQESEVRSLFEQVdreqqGRLDVLVn 91
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA-----RPADVAAELEVWALAQEL-----GPLDLLV- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 naYAgVQTILntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVvisspGGLQYMFNVP----YGVGK 167
Cdd:cd11730   72 --YA-AGAIL---GKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL-----GAYPELVMLPglsaYAAAK 140
                        170       180       190
                 ....*....|....*....|....*....|...
gi 296214664 168 AACDKLAADCAHELRryGVSYVSLWPGIVQTEL 200
Cdd:cd11730  141 AALEAYVEVARKEVR--GLRLTLVRPPAVDTGL 171
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-205 2.75e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 65.58  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEV 71
Cdd:PRK12859   4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTywtaydkempwGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  72 RSLFEQVdREQQGRLDVLVNNAYAGVqtilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISS 151
Cdd:PRK12859  84 KELLNKV-TEQLGYPHILVNNAAYST-------NNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 152 PGGLQYM-FNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT----ELLKEHM 205
Cdd:PRK12859 156 GQFQGPMvGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTgwmtEEIKQGL 214
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
5-93 2.91e-12

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: 65.78  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT--GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 82
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEV-VKE 102
                         90
                 ....*....|.
gi 296214664  83 QGRLDVLVNNA 93
Cdd:cd05355  103 FGKLDILVNNA 113
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
4-211 3.07e-12

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: 65.26  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQeSEVRSLFEQVDREQQ 83
Cdd:cd08936    7 PLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGK-AEDRERLVATAVNLH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYAGvqtilntrskAFW----ETPASMWDDINNVGLRGHYLCSvygaRLMVPA----GRGLIVVISSPGGL 155
Cdd:cd08936   86 GGVDILVSNAAVN----------PFFgnilDSTEEVWDKILDVNVKATALMT----KAVVPEmekrGGGSVVIVSSVAAF 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 156 QYMFNV-PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT---ELLKEHMAKEEGL 211
Cdd:cd08936  152 HPFPGLgPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTsfsSALWMDKAVEESM 211
PRK07062 PRK07062
SDR family oxidoreductase;
1-198 4.21e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 65.06  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhmDTLRVAAQEAQSL----GGQCVPVVCDSSQESEVRSLFE 76
Cdd:PRK07062   2 MQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGR--DEERLASAEARLRekfpGARLLAARCDVLDEADVAAFAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  77 QVDReQQGRLDVLVNNAYAGvqtilntRSKAFWETPASMWDDinnvGLRGHYLCSVYGARLMVPAGR----GLIVVISSP 152
Cdd:PRK07062  80 AVEA-RFGGVDMLVNNAGQG-------RVSTFADTTDDAWRD----ELELKYFSVINPTRAFLPLLRasaaASIVCVNSL 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296214664 153 GGLQ---YMfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK07062 148 LALQpepHM--VATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
PRK08265 PRK08265
short chain dehydrogenase; Provisional
3-93 4.59e-12

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 65.03  E-value: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 82
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN---GAAVAASLGERARFIATDITDDAAIERAVATV-VAR 77
                         90
                 ....*....|.
gi 296214664  83 QGRLDVLVNNA 93
Cdd:PRK08265  78 FGRVDILVNLA 88
PRK08628 PRK08628
SDR family oxidoreductase;
5-186 5.41e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 64.59  E-value: 5.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVaAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 84
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEF-AEELRALQPRAEFVQVDLTDDAQCRDAVEQTV-AKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTILNTRSKAFwetPASMwdDINNVglrgHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-Y 163
Cdd:PRK08628  83 RIDGLVNNAGVNDGVGLEAGREAF---VASL--ERNLI----HYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSgY 153
                        170       180
                 ....*....|....*....|...
gi 296214664 164 GVGKAACDKLAADCAHELRRYGV 186
Cdd:PRK08628 154 AAAKGAQLALTREWAVALAKDGV 176
PRK06194 PRK06194
hypothetical protein; Provisional
6-238 5.57e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 65.04  E-value: 5.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK06194   5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAA-LERFGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGVQTILntrskafWETPASMWDDINNVGLRGhylcSVYGARLMVP----------AGRGLIVVISSPGGL 155
Cdd:PRK06194  84 VHLLFNNAGVGAGGLV-------WENSLADWEWVLGVNLWG----VIHGVRAFTPlmlaaaekdpAYEGHIVNTASMAGL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 156 qymFNVP----YGVGKAACDKLAADCAHELR----RYGVSYvsLWPGIVQTELLKEHMAKEEGLQDPvfKQLRSVFSSAE 227
Cdd:PRK06194 153 ---LAPPamgiYNVSKHAVVSLTETLYQDLSlvtdQVGASV--LCPYFVPTGIWQSERNRPADLANT--APPTRSQLIAQ 225
                        250
                 ....*....|.
gi 296214664 228 ttEMSGKCVVA 238
Cdd:PRK06194 226 --AMSQKAVGS 234
PRK06139 PRK06139
SDR family oxidoreductase;
1-154 9.09e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 64.74  E-value: 9.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 80
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQA-A 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296214664  81 EQQGRLDVLVNNayAGVQTILNtrskaFWETPASMWDDINNVGLRGHylcsVYGARLMVP----AGRGLIVVISSPGG 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) ...
5-206 9.91e-12

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: 63.95  E-value: 9.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADG---AERVAADIGEAAIAIQADVTKRADVEAMVEAA-LSKFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilNTRSKAFWETPASMWDDINNVGLRGHYLcsvyGARLMVP----AGRGLIVVISSPGGLQYMFN 160
Cdd:cd05345   79 RLDILVNN--AGI----THRNKPMLEVDEEEFDRVFAVNVKSIYL----SAQALVPhmeeQGGGVIINIASTAGLRPRPG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 161 -VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMA 206
Cdd:cd05345  149 lTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMG 195
PRK09134 PRK09134
SDR family oxidoreductase;
1-93 1.13e-11

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 63.79  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMkgqVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVd 79
Cdd:PRK09134   6 MAAPR---AALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARA- 81
                         90
                 ....*....|....
gi 296214664  80 REQQGRLDVLVNNA 93
Cdd:PRK09134  82 SAALGPITLLVNNA 95
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-209 1.17e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 63.74  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATvyITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 84
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCD--IVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE-FG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGR-GLIVVISSPGGLQYMFNVP- 162
Cdd:PRK08993  85 HIDILVNN--AGL-----IRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVPs 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEE 209
Cdd:PRK08993 158 YTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQ 204
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
5-199 1.51e-11

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: 63.41  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEV-RSLFEQVDReqQ 83
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE---IGPAACAISLDVTDQASIdRCVAALVDR--W 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  84 GRLDVLVNNAYA-GVQTILNTRskafWETpasmWDDINNVGLRGHYLCSVYGARLMVPAGRG--LIVVISSPGGLQYMFN 160
Cdd:cd05363   76 GSIDILVNNAALfDLAPIVDIT----RES----YDRLFAINVSGTLFMMQAVARAMIAQGRGgkIINMASQAGRRGEALV 147
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:cd05363  148 GVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
9-214 1.65e-11

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: 63.25  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGAT---VYITGRHM---DTLRVAAQEAQslgGQCVPV----VCDSsqesevRSLFEQV 78
Cdd:cd09806    2 VVLITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLkkkGRLWEAAGALA---GGTLETlqldVCDS------KSVAAAV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  79 DREQQGRLDVLVNNAYAGVQTILNTRSKAfwETPASMwdDINNVGLrghylcsvygARL-------MVPAGRGLIVVISS 151
Cdd:cd09806   73 ERVTERHVDVLVCNAGVGLLGPLEALSED--AMASVF--DVNVFGT----------VRMlqaflpdMKRRGSGRILVTSS 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296214664 152 PGGLQ-YMFNVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGLQDP 214
Cdd:cd09806  139 VGGLQgLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDR 202
PRK07069 PRK07069
short chain dehydrogenase; Validated
12-212 1.82e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 63.19  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITgrHMDTLRVAAQEAQSLGGQCVPVVC-----DSSQESEVRSLFEQVDrEQQGRL 86
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLT--DINDAAGLDAFAAEINAAHGEGVAfaavqDVTDEAQWQALLAQAA-DAMGGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNayAGVQTILNTRSKAFWEtpasmWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFNVP-YGV 165
Cdd:PRK07069  81 SVLVNN--AGVGSFGAIEQIELDE-----WRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTaYNA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296214664 166 GKAACDKL----AADCAHelRRYGVSYVSLWPGIVQT---ELLKEHMAKEEGLQ 212
Cdd:PRK07069 154 SKAAVASLtksiALDCAR--RGLDVRCNSIHPTFIRTgivDPIFQRLGEEEATR 205
PRK06196 PRK06196
oxidoreductase; Provisional
5-260 1.94e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 63.55  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQslggQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID----GVEVVMLDLADLESVRAFAERF-LDSGR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTILNTRSKAFWETPASmwddINNVglrGHYLCSVYGARLMVPAGRGLIVVISSPG----GLQY--- 157
Cdd:PRK06196  99 RIDILINN--AGVMACPETRVGDGWEAQFA----TNHL---GHFALVNLLWPALAAGAGARVVALSSAGhrrsPIRWddp 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFNVP------YGVGKAA-------CDKLAADcahelrrYGVSYVSLWPGIVQTElLKEHMAKEE----GLQDPVFKQLR 220
Cdd:PRK06196 170 HFTRGydkwlaYGQSKTAnalfavhLDKLGKD-------QGVRAFSVHPGGILTP-LQRHLPREEqvalGWVDEHGNPID 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 296214664 221 SVFssaETTEMSGKCVVALATDPNILSLSGKVLPSCDLAR 260
Cdd:PRK06196 242 PGF---KTPAQGAATQVWAATSPQLAGMGGLYCEDCDIAE 278
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-206 2.24e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 62.78  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESE 70
Cdd:PRK12748   2 PLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmpwGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  71 VRSLFEQVdREQQGRLDVLVNNAYAGVQTILNtrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVIS 150
Cdd:PRK12748  82 PNRVFYAV-SERLGDPSILINNAAYSTHTRLE-------ELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLT 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296214664 151 SPGGLQYMFN-VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT----ELLKEHMA 206
Cdd:PRK12748 154 SGQSLGPMPDeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTgwitEELKHHLV 214
PRK08219 PRK08219
SDR family oxidoreductase;
9-214 2.59e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 62.26  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAgATVYITGRHMDTLRVAAQEAQSLggqcVPVVCDSSQESEVRSLFEQVDreqqgRLDV 88
Cdd:PRK08219   5 TALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGA----TPFPVDLTDPEAIAAAVEQLG-----RLDV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNayAGVqtilnTRSKAFWETPASMWddinnvglRGHYLCSVYGA----RLMVP---AGRGLIVVISSPGGLQ-YMFN 160
Cdd:PRK08219  75 LVHN--AGV-----ADLGPVAESTVDEW--------RATLEVNVVAPaeltRLLLPalrAAHGHVVFINSGAGLRaNPGW 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296214664 161 VPYGVGK----AACDKLAADCAHELRrygVSyvSLWPGIVQTELLKEHMAKEEGLQDP 214
Cdd:PRK08219 140 GSYAASKfalrALADALREEEPGNVR---VT--SVHPGRTDTDMQRGLVAQEGGEYDP 192
PRK05693 PRK05693
SDR family oxidoreductase;
9-211 3.03e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 62.89  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqslGGQCVPVvcDSSQESEVRSLFEQVDrEQQGRLDV 88
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA----GFTAVQL--DVNDGAALARLAEELE-AEHGGLDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNA-YAGVQTILntrskafwetpasmwdDINNVGLRGHYLCSVYG----ARLMVPA---GRGLIVVISSPGG-LQYMF 159
Cdd:PRK05693  76 LINNAgYGAMGPLL----------------DGGVEAMRRQFETNVFAvvgvTRALFPLlrrSRGLVVNIGSVSGvLVTPF 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 296214664 160 NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGL 211
Cdd:PRK05693 140 AGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASREAEQL 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
5-211 5.15e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 61.87  E-value: 5.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALA-VERFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVqtilNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGlqYMFNVP-- 162
Cdd:PRK07478  83 GLDIAFNN--AGT----LGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVG--HTAGFPgm 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296214664 163 --YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEEGL 211
Cdd:PRK07478 155 aaYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEAL 205
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
6-250 1.01e-10

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (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. 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: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 61.38  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVcVVTGASRGIGRGIALQLCKAGA-TVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd09810    1 KGTV-VITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNF-RRTGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTILNTRSKA--FWETPAS-----------MWDDINN----------VGLRGHYLCSVYGarlMVPA 141
Cdd:cd09810   79 PLDALVCNAAVYLPTAKEPRFTAdgFELTVGVnhlghflltnlLLEDLQRsenaspriviVGSITHNPNTLAG---NVPP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 142 GRGLIVVISSPGGLQyMFNVPYGVGKAACDKLAAD---C----AHEL-RRY----GVSYVSLWPG-IVQTELLKEHMAke 208
Cdd:cd09810  156 RATLGDLEGLAGGLK-GFNSMIDGGEFEGAKAYKDskvCnmltTYELhRRLheetGITFNSLYPGcIAETGLFREHYP-- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 296214664 209 egLQDPVFKQLRS-VFSSAETTEMSGKCVVALATDPNiLSLSG 250
Cdd:cd09810  233 --LFRTLFPPFQKyITKGYVSEEEAGERLAAVIADPS-LGVSG 272
PRK06500 PRK06500
SDR family oxidoreductase;
5-201 1.03e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 60.74  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAE---LGESALVIRADAGDVAAQKALAQAL-AEAFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNayAGVQTIlntrsKAFWETPASMWDDINNVGLRGHY-----------------LCSVYGARLMVPAgrgliv 147
Cdd:PRK06500  80 RLDAVFIN--AGVAKF-----APLEDWDEAMFDRSFNTNVKGPYfliqallpllanpasivLNGSINAHIGMPN------ 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296214664 148 viSSpgglqymfnvPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELL 201
Cdd:PRK06500 147 --SS----------VYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLY 188
PRK12742 PRK12742
SDR family oxidoreductase;
3-200 1.09e-10

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 60.54  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHMDTLRVAAQEAQSLGGQCVPVvcDSSQESEVRSLFeqvdrEQ 82
Cdd:PRK12742   2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFT--YAGSKDAAERLAQETGATAVQT--DSADRDAVIDVV-----RK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNA---YAGVQTILNTrskafwetpasmwDDIN---NVGLRGHYLCSVYGARLMVPAGRglIVVISSPGGLQ 156
Cdd:PRK12742  73 SGALDILVVNAgiaVFGDALELDA-------------DDIDrlfKINIHAPYHASVEAARQMPEGGR--IIIIGSVNGDR 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 296214664 157 YMFN--VPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK12742 138 MPVAgmAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-155 1.14e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 61.78  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   2 AAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhmdtLRV-AAQE-----AQSLGGqcVPVVCDSSQESEVRSLF 75
Cdd:PRK08261 205 DRPLAGKVALVTGAARGIGAAIAEVLARDGAHVVC-------LDVpAAGEalaavANRVGG--TALALDITAPDAPARIA 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  76 EQVdREQQGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRG-----HYLcsvYGARLMVPAGRglIVVIS 150
Cdd:PRK08261 276 EHL-AERHGGLDIVVHN--AGI-----TRDKTLANMDEARWDSVLAVNLLAplritEAL---LAAGALGDGGR--IVGVS 342

                 ....*
gi 296214664 151 SPGGL 155
Cdd:PRK08261 343 SISGI 347
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
5-122 1.15e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.66  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGG-QCVPVVCD--SSQESEVRSLFEQVDrE 81
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGpQPAIIPLDllTATPQNYQQLADTIE-E 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 296214664  82 QQGRLDVLVNNAyagvqTILNTRSkAFWETPASMWDDINNV 122
Cdd:PRK08945  89 QFGRLDGVLHNA-----GLLGELG-PMEQQDPEVWQDVMQV 123
PRK08703 PRK08703
SDR family oxidoreductase;
4-93 1.34e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 60.33  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQ---CVPVVCDSSQESEVRSLFEQVDR 80
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPepfAIRFDLMSAEEKEFEQFAATIAE 82
                         90
                 ....*....|...
gi 296214664  81 EQQGRLDVLVNNA 93
Cdd:PRK08703  83 ATQGKLDGIVHCA 95
PRK08416 PRK08416
enoyl-ACP reductase;
1-209 1.67e-10

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 60.56  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHMDTLRVAAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQV 78
Cdd:PRK08416   2 MSNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDlEQKYGIKAKAYPLNILEPETYKELFKKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  79 DrEQQGRLDVLVNNAyagvqtILNTRSKAFWETPAsmwddinnVGLRGHYLCSVY-------------GARLMVPAGRGL 145
Cdd:PRK08416  82 D-EDFDRVDFFISNA------IISGRAVVGGYTKF--------MRLKPKGLNNIYtatvnafvvgaqeAAKRMEKVGGGS 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296214664 146 IVVISSPGGLQYMFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLKEHMAKEE 209
Cdd:PRK08416 147 IISLSSTGNLVYIENYAgHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEE 211
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
12-202 1.97e-10

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: 59.77  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLrvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQGRLDVLVN 91
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGL--AALAAELGAENVVAGALDVTDRAAWAAALADFAAATGGRLDALFN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 NAYAGvqtilntRSKAFWETPASMWDDINNVGLRGhylcSVYGARLMVPAGR----GLIVVISSPGGLqymFNVP----Y 163
Cdd:cd08931   83 NAGVG-------RGGPFEDVPLAAHDRMVDINVKG----VLNGAYAALPYLKatpgARVINTASSSAI---YGQPdlavY 148
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296214664 164 GVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:cd08931  149 SATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILT 187
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-202 2.20e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 60.03  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHMDTLRVAA--QEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREq 82
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKV-VAGCGPNSPRRVKwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAE- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  83 QGRLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMF-NV 161
Cdd:PRK12938  79 VGEIDVLVNN--AGI-----TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFgQT 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 296214664 162 PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK12938 152 NYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
PRK06701 PRK06701
short chain dehydrogenase; Provisional
5-93 2.52e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 60.05  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHMDTLRVAAQEAQSL---GGQCVPVVCDSSQESEVRSLFEQVDRE 81
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIV--YLDEHEDANETKQRVekeGVKCLLIPGDVSDEAFCKDAVEETVRE 121
                         90
                 ....*....|..
gi 296214664  82 qQGRLDVLVNNA 93
Cdd:PRK06701 122 -LGRLDILVNNA 132
PRK07806 PRK07806
SDR family oxidoreductase;
7-99 2.85e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 59.73  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTA-REEFGG 84
                         90
                 ....*....|....
gi 296214664  86 LDVLVNNAYAGVQT 99
Cdd:PRK07806  85 LDALVLNASGGMES 98
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
11-209 3.95e-10

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: 58.83  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYItgrHMDTLRVAAQEAQ----SLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRL 86
Cdd:cd05357    4 LVTGAAKRIGRAIAEALAAEGYRVVV---HYNRSEAEAQRLKdelnALRNSAVLVQADLSDFAACADLVAAAFR-AFGRC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVQTILNtrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYMFN-VPYGV 165
Cdd:cd05357   80 DVLVNNASAFYPTPLG-------QGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGyFAYCM 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296214664 166 GKAACDKL----AADCAHELRRYGVSyvslwPGIVqteLLKEHMAKEE 209
Cdd:cd05357  153 SKAALEGLtrsaALELAPNIRVNGIA-----PGLI---LLPEDMDAEY 192
PRK06180 PRK06180
short chain dehydrogenase; Provisional
5-194 4.79e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 59.16  E-value: 4.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhmDTLRVAAQEAQSlGGQCVPVVCDSSQesevrslFEQVDR---- 80
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVR--SEAARADFEALH-PDRALARLLDVTD-------FDAIDAvvad 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 --EQQGRLDVLVNNAYAGVQTILNtrskafwETPASmwddinnvGLRGHYLCSVYGARLMVPA--------GRGLIVVIS 150
Cdd:PRK06180  72 aeATFGPIDVLVNNAGYGHEGAIE-------ESPLA--------EMRRQFEVNVFGAVAMTKAvlpgmrarRRGHIVNIT 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 151 SPGGLQYMFNVPYGVG-KAACDKLAADCAHELRRYGVSYVSLWPG 194
Cdd:PRK06180 137 SMGGLITMPGIGYYCGsKFALEGISESLAKEVAPFGIHVTAVEPG 181
PRK05866 PRK05866
SDR family oxidoreductase;
2-198 5.32e-10

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 59.37  E-value: 5.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   2 AAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrE 81
Cdd:PRK05866  35 PVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVE-K 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAYAGVQTILntrskafwETPASMWDDINNVGLRGHY--LCSVYG-ARLMVPAGRGLIVVISS---PGGL 155
Cdd:PRK05866 114 RIGGVDILINNAGRSIRRPL--------AESLDRWHDVERTMVLNYYapLRLIRGlAPGMLERGDGHIINVATwgvLSEA 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 156 QYMFNVpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK05866 186 SPLFSV-YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK08263 PRK08263
short chain dehydrogenase; Provisional
5-200 5.58e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 58.90  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLrvaAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATL---ADLAEKYGDRLLPLALDVTDRAAVFAAVETA-VEHFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVqtilntrskafwetpASMWDDINNVGLRGHYLCSVYGARLMVPA--------GRGLIVVISSPGGLQ 156
Cdd:PRK08263  77 RLDIVVNNAGYGL---------------FGMIEEVTESEARAQIDTNFFGALWVTQAvlpylreqRSGHIIQISSIGGIS 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296214664 157 YMFNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK08263 142 AFPMSGiYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDW 186
PRK09135 PRK09135
pteridine reductase; Provisional
4-193 1.42e-09

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 57.63  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-MDTLRVAAQEAQSLGGQCVPVVC-DSSQESEVRSLFEQVDRe 81
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQaDLLDPDALPELVAACVA- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAyagvqtilntrsKAFWETP-----ASMWDDINNVGLRGHYLCSVYGARLMVPAgRGLIVVISSPGGLQ 156
Cdd:PRK09135  82 AFGRLDALVNNA------------SSFYPTPlgsitEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHAER 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 157 YMFNVP-YGVGKAACDKLAADCAHEL----RRYGVSY-VSLWP 193
Cdd:PRK09135 149 PLKGYPvYCAAKAALEMLTRSLALELapevRVNAVAPgAILWP 191
PRK06914 PRK06914
SDR family oxidoreductase;
5-198 1.74e-09

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 57.73  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMD---TLRVAAQEAqslggqcvpvvcDSSQESEVRSL----FEQ 77
Cdd:PRK06914   1 MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEkqeNLLSQATQL------------NLQQNIKVQQLdvtdQNS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  78 VDREQQ-----GRLDVLVNNA---YAGvqtilntrskafwetpasMWDDINNVGLRGHYLCSVYGA----RLMVP----A 141
Cdd:PRK06914  69 IHNFQLvlkeiGRIDLLVNNAgyaNGG------------------FVEEIPVEEYRKQFETNVFGAisvtQAVLPymrkQ 130
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 142 GRGLIVVISSPGGlQYMFNV--PYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK06914 131 KSGKIINISSISG-RVGFPGlsPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK06125 PRK06125
short chain dehydrogenase; Provisional
1-210 3.00e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 56.59  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPV-VCDSSQESEVRSLFEQVd 79
Cdd:PRK06125   1 MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVhALDLSSPEAREQLAAEA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  80 reqqGRLDVLVNNAYAgvqtilntrskafweTPASMWDDINNVGLRGHYLCSVYG----ARLMVPA----GRGLIVVISS 151
Cdd:PRK06125  80 ----GDIDILVNNAGA---------------IPGGGLDDVDDAAWRAGWELKVFGyidlTRLAYPRmkarGSGVIVNVIG 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296214664 152 PGGLQYMFNvpYGVGKAACDKLAA-DCA--HELRRYGVSYVSLWPGIVQTE----LLKEHMAKEEG 210
Cdd:PRK06125 141 AAGENPDAD--YICGSAGNAALMAfTRAlgGKSLDDGVRVVGVNPGPVATDrmltLLKGRARAELG 204
PRK06523 PRK06523
short chain dehydrogenase; Provisional
6-219 4.37e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 56.07  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAqslggqcvpVVCDSSQESEVRSLFEQVdREQQGR 85
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEF---------VAADLTTAEGCAAVARAV-LERLGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAgvqtilntrSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPA----GRGLIVVISSPGGL--QYMF 159
Cdd:PRK06523  78 VDILVHVLGG---------SSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGmiarGSGVIIHVTSIQRRlpLPES 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296214664 160 NVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE---LLKEHMAKEEGLQDPVFKQL 219
Cdd:PRK06523 149 TTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavALAERLAEAAGTDYEGAKQI 211
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
7-90 4.93e-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: 56.05  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGAS--RGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEV-KKDWG 79

                 ....*.
gi 296214664  85 RLDVLV 90
Cdd:cd05372   80 KLDGLV 85
PRK08267 PRK08267
SDR family oxidoreductase;
12-202 6.08e-09

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 55.71  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLG-GQCVPVVCDSSQESEVRSLFEQVDREQQGRLDVLV 90
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAE---LGaGNAWTGALDVTDRAAWDAALADFAAATGGRLDVLF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAyaGVqtilnTRSKAFWETPASMWD---DINNVGLrghylcsVYGARLMVPAGR----GLIVVISSPGGLqymFNVP- 162
Cdd:PRK08267  83 NNA--GI-----LRGGPFEDIPLEAHDrviDINVKGV-------LNGAHAALPYLKatpgARVINTSSASAI---YGQPg 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 163 ---YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELLK 202
Cdd:PRK08267 146 lavYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLD 188
PRK07576 PRK07576
short chain dehydrogenase; Provisional
7-96 7.06e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 55.73  E-value: 7.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 86
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI-ADEFGPI 87
                         90
                 ....*....|
gi 296214664  87 DVLVNNAyAG 96
Cdd:PRK07576  88 DVLVSGA-AG 96
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-203 8.38e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 55.46  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVY-ITGRHMDTLRVAAQEAqslGGQCVPVVCDSSQESEVRSLFEQVDREQQGRLD-- 87
Cdd:PRK06924   5 IITGTSQGLGEAIANQLLEKGTHVIsISRTENKELTKLAEQY---NSNLTFHSLDLQDVHELETNFNEILSSIQEDNVss 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  88 -VLVNNAyagvqTILntrskafweTPASMWDDINNVGLRGHY---------LCSVYGARLMVPAGRGLIVVISSPGGLQY 157
Cdd:PRK06924  82 iHLINNA-----GMV---------APIKPIEKAESEELITNVhlnllapmiLTSTFMKHTKDWKVDKRVINISSGAAKNP 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296214664 158 MFN-VPYGVGKAACDkLAADCAH---ELRRYGVSYVSLWPGIVQTELLKE 203
Cdd:PRK06924 148 YFGwSAYCSSKAGLD-MFTQTVAteqEEEEYPVKIVAFSPGVMDTNMQAQ 196
PRK08862 PRK08862
SDR family oxidoreductase;
5-92 1.05e-08

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 54.73  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPV-VCDSSQESeVRSLFEQVDREQQ 83
Cdd:PRK08862   3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFqLKDFSQES-IRHLFDAIEQQFN 81

                 ....*....
gi 296214664  84 GRLDVLVNN 92
Cdd:PRK08862  82 RAPDVLVNN 90
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
5-200 1.10e-08

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 54.92  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 84
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAE---LGERVKIFPANLSDRDEVKALGQKAEADLEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 rLDVLVNNayAGVqtilnTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISS-------PGGLQY 157
Cdd:PRK12936  81 -VDILVNN--AGI-----TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSvvgvtgnPGQANY 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 158 MfnvpygVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK12936 153 C------ASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAM 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
7-201 2.45e-08

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 54.19  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRL 86
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFR-LLGHV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAYAGVQTILN--TRSKAFWETPASMWDDINNVglrghylcSVYGARLMVPAGRGLIVVISSPGGLqymfnVP-- 162
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVemTHDDWRWVIDVDLWGSIHTV--------EAFLPRLLEQGTGGHVVFTASFAGL-----VPna 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 163 ----YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELL 201
Cdd:PRK05876 152 glgaYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLV 194
PRK05717 PRK05717
SDR family oxidoreductase;
2-151 2.90e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 53.74  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   2 AAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHMDTLRvAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDRe 81
Cdd:PRK05717   5 NPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLA--DLDRER-GSKVAKALGENAWFIAMDVADEAQVAAGVAEVLG- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  82 QQGRLDVLVNNAyagvqTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMvPAGRGLIVVISS 151
Cdd:PRK05717  81 QFGRLDALVCNA-----AIADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYL-RAHNGAIVNLAS 144
PRK06720 PRK06720
hypothetical protein; Provisional
1-93 9.96e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 51.13  E-value: 9.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   1 MAAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEqVDR 80
Cdd:PRK06720  10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVIS-ITL 88
                         90
                 ....*....|...
gi 296214664  81 EQQGRLDVLVNNA 93
Cdd:PRK06720  89 NAFSRIDMLFQNA 101
PRK07041 PRK07041
SDR family oxidoreductase;
11-93 1.03e-07

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 51.96  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVdreqqGRLDVLV 90
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGG-GAPVRTAALDITDEAAVDAFFAEA-----GPFDHVV 74

                 ...
gi 296214664  91 NNA 93
Cdd:PRK07041  75 ITA 77
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
5-90 1.43e-07

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: 51.56  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGA--SRGIGRGIALQLCKAGATVYITGRHmDTLRVAAQE-AQSLGgqCVPVV-CDSSQESEVRSLFEQVdR 80
Cdd:COG0623    3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQG-EALKKRVEPlAEELG--SALVLpCDVTDDEQIDALFDEI-K 78
                         90
                 ....*....|
gi 296214664  81 EQQGRLDVLV 90
Cdd:COG0623   79 EKWGKLDFLV 88
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
5-200 1.55e-07

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 51.49  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAqslgGQCVPVVcdssqESEVRSLFEQ---VDR- 80
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF----GDHVLVV-----EGDVTSYADNqraVDQt 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  81 -EQQGRLDVLVNNayAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLcsvyGARLMVPA---GRGLIVVISS----- 151
Cdd:PRK06200  75 vDAFGKLDCFVGN--AGIWDYNTSLVDIPAETLDTAFDEIFNVNVKGYLL----GAKAALPAlkaSGGSMIFTLSnssfy 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 296214664 152 PGGlqymFNVPYGVGKAACDKLAADCAHEL----RRYGVSyvslwPGIVQTEL 200
Cdd:PRK06200 149 PGG----GGPLYTASKHAVVGLVRQLAYELapkiRVNGVA-----PGGTVTDL 192
PRK07024 PRK07024
SDR family oxidoreductase;
11-198 1.63e-07

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 51.47  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGG-QCVPV-VCDSSQESEVRSLFEQvdreQQGRLDV 88
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARvSVYAAdVRDADALAAAAADFIA----AHGLPDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  89 LVNNAYAGVQTILNTRS--KAFWETpasMwdDINNVGLRGHYLCSVYGarlMVPAGRGLIVVISSPGGLQYMfnvP---- 162
Cdd:PRK07024  82 VIANAGISVGTLTEEREdlAVFREV---M--DTNYFGMVATFQPFIAP---MRAARRGTLVGIASVAGVRGL---Pgaga 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK07024 151 YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
12-166 1.65e-07

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 51.30  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDREQQgRLDVLVN 91
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDE---LGDNLYIAQLDVRNRAAIEEMLASLPAEWR-NIDVLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 NayAGVQTILNTRSKAF---WETPAsmwdDINNVGLrghylcsVYGARL----MVPAGRGLIVVISSPGGlqymfNVPYG 164
Cdd:PRK10538  81 N--AGLALGLEPAHKASvedWETMI----DTNNKGL-------VYMTRAvlpgMVERNHGHIINIGSTAG-----SWPYA 142

                 ..
gi 296214664 165 VG 166
Cdd:PRK10538 143 GG 144
PRK07102 PRK07102
SDR family oxidoreductase;
12-198 2.16e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 51.08  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPV-VCDSSQESEVRSLFEQVdreqQGRLD-VL 89
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSThELDILDTASHAAFLDSL----PALPDiVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  90 VNNAYAGVQtilnTRSKAFWETpASMWDDINNVG---LRGHYlcsvygARLMVPAGRGLIVVISSPGG-----LQYMfnv 161
Cdd:PRK07102  82 IAVGTLGDQ----AACEADPAL-ALREFRTNFEGpiaLLTLL------ANRFEARGSGTIVGISSVAGdrgraSNYV--- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 296214664 162 pYGVGKAAcdkLAADCA---HELRRYGVSYVSLWPGIVQT 198
Cdd:PRK07102 148 -YGSAKAA---LTAFLSglrNRLFKSGVHVLTVKPGFVRT 183
PRK08340 PRK08340
SDR family oxidoreductase;
11-93 2.17e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 50.96  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGqCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 90
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEA-WELLGGIDALV 81

                 ...
gi 296214664  91 NNA 93
Cdd:PRK08340  82 WNA 84
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-194 4.25e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 50.14  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVpVVCDSSQESEVRSLFEQVDREQQG 84
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHY-VVGDVSSTESARNVIEKAAKVLNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYAGVQTIlntrskafwETPASMWDDINNvGLRGHYLCSVYGARLMVPAGRglIVVISSPGGL--QYMFNVP 162
Cdd:PRK05786  82 IDGLVVTVGGYVEDTV---------EEFSGLEEMLTN-HIKIPLYAVNASLRFLKEGSS--IVLVSSMSGIykASPDQLS 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 296214664 163 YGVGKAACDKLAADCAHELRRYGVSYVSLWPG 194
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPT 181
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-155 7.10e-07

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 49.19  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYitgrhmdtlRVAAQEAQSLGGQCVPVVCDSSQESEvrSLFEQVdreqqGR 85
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVY---------GVDKQDKPDLSGNFHFLQLDLSDDLE--PLFDWV-----PS 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296214664  86 LDVLVNNayAGV----QTILntrskafwETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGL 155
Cdd:PRK06550  68 VDILCNT--AGIlddyKPLL--------DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASF 131
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
6-93 1.05e-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: 49.67  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCK-AGATVYITGRH-----MDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVd 79
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARrYGARLVLLGRSplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKV- 282
                         90
                 ....*....|....
gi 296214664  80 REQQGRLDVLVNNA 93
Cdd:cd08953  283 RERYGAIDGVIHAA 296
PRK07775 PRK07775
SDR family oxidoreductase;
11-198 3.51e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 47.44  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQGRLDVLV 90
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAE-EALGEIEVLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 nnAYAGvqtilNTRSKAFWETPASMWDDINNVGLRGHYlcSVYGARL--MVPAGRGLIVVISSPGGL-QYMFNVPYGVGK 167
Cdd:PRK07775  93 --SGAG-----DTYFGKLHEISTEQFESQVQIHLVGAN--RLATAVLpgMIERRRGDLIFVGSDVALrQRPHMGAYGAAK 163
                        170       180       190
                 ....*....|....*....|....*....|.
gi 296214664 168 AACDKLAADCAHELRRYGVSYVSLWPGIVQT 198
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
5-181 5.21e-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: 46.96  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhmdtLRVAAQEAQSL----GGQCVPVVCDssqeseVRSLFEQ--- 77
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAV-------LDRSAEKVAELradfGDAVVGVEGD------VRSLADNera 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  78 VDR--EQQGRLDVLVNNayAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLcsvyGARLMVPA---GRGLIVVISS- 151
Cdd:cd05348   69 VARcvERFGKLDCFIGN--AGIWDYSTSLVDIPEEKLDEAFDELFHINVKGYIL----GAKAALPAlyaTEGSVIFTVSn 142
                        170       180       190
                 ....*....|....*....|....*....|....
gi 296214664 152 ----PGGlqymFNVPYGVGKAACDKLAADCAHEL 181
Cdd:cd05348  143 agfyPGG----GGPLYTASKHAVVGLVKQLAYEL 172
PRK09186 PRK09186
flagellin modification protein A; Provisional
5-151 6.46e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 46.52  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGGQ---CVpVVCDSSQESEVRSLFEQVdRE 81
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklSL-VELDITDQESLEEFLSKS-AE 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296214664  82 QQGRLDVLVNNAYAgvqtilntRSKA----FWEtpASMwDDIN---NVGLRGHYLCSVYGARLMVPAGRGLIVVISS 151
Cdd:PRK09186  80 KYGKIDGAVNCAYP--------RNKDygkkFFD--VSL-DDFNenlSLHLGSSFLFSQQFAKYFKKQGGGNLVNISS 145
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
12-200 6.48e-06

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: 46.89  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITgrhmdTLRVAAQEAQSLGGQCVP----VVCDSSQESEVRSLFEQVDREQQGR-L 86
Cdd:cd09805    5 ITGCDSGFGNLLAKKLDSLGFTVLAG-----CLTKNGPGAKELRRVCSDrlrtLQLDVTKPEQIKRAAQWVKEHVGEKgL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNAyaGVQTILntrSKAFWeTPASMWDDINNVGLRGhyLCSVYGARL-MVPAGRGLIVVISSPGG-LQYMFNVPYG 164
Cdd:cd09805   80 WGLVNNA--GILGFG---GDEEL-LPMDDYRKCMEVNLFG--TVEVTKAFLpLLRRAKGRVVNVSSMGGrVPFPAGGAYC 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 296214664 165 VGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:cd09805  152 ASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187
PRK06128 PRK06128
SDR family oxidoreductase;
5-99 6.99e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 46.78  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRHMDTLRVaAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdRE 81
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIalnYLPEEEQDAAEV-VQLIQAEGRKAVALPGDLKDEAFCRQLVERA-VK 130
                         90
                 ....*....|....*...
gi 296214664  82 QQGRLDVLVNNayAGVQT 99
Cdd:PRK06128 131 ELGGLDILVNI--AGKQT 146
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
7-198 1.11e-05

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: 45.78  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGrhmdtlRVAAQEAqslgGQCVPVVCDSSQESEVRSLFEQVDReQQGRL 86
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASID------LAENEEA----DASIIVLDSDSFTEQAKQVVASVAR-LSGKV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  87 DVLVNNA--YAGVqtilNTRSKAFWETPASMWDdinnVGLRGHYLCSVYGARLMVPAgrGLIVVISSPGGLQ-YMFNVPY 163
Cdd:cd05334   70 DALICVAggWAGG----SAKSKSFVKNWDLMWK----QNLWTSFIASHLATKHLLSG--GLLVLTGAKAALEpTPGMIGY 139
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 164 GVGKAACDKLAADCAHELR--RYGVSYVSLWPGIVQT 198
Cdd:cd05334  140 GAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDT 176
PRK07985 PRK07985
SDR family oxidoreductase;
5-235 1.22e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 46.14  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRHMDTLRVAA--QEAqslGGQCVPVVCDSSQESEVRSLFEQVd 79
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVaisYLPVEEEDAQDVKKiiEEC---GRKAVLLPGDLSDEKFARSLVHEA- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  80 REQQGRLDV--LVNNAYAGVQTILNTRSKAFWETPAsmwddINNVGLrgHYLCSvyGARLMVPAGRGLIVVIS------S 151
Cdd:PRK07985 123 HKALGGLDImaLVAGKQVAIPDIADLTSEQFQKTFA-----INVFAL--FWLTQ--EAIPLLPKGASIITTSSiqayqpS 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 152 PGGLQymfnvpYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL-----LKEHMAKEEGLQDP------------ 214
Cdd:PRK07985 194 PHLLD------YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisggQTQDKIPQFGQQTPmkragqpaelap 267
                        250       260
                 ....*....|....*....|.
gi 296214664 215 VFKQLRSVFSSAETTEMSGKC 235
Cdd:PRK07985 268 VYVYLASQESSYVTAEVHGVC 288
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
7-93 1.26e-05

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: 45.66  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrvaAQEAQS-----LGGQCVPV-VCDSSQESEVRSLFEQVDR 80
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTR----AEEARKeieteSGNQNIFLhIVDMSDPKQVWEFVEEFKE 76
                         90
                 ....*....|...
gi 296214664  81 EQQgRLDVLVNNA 93
Cdd:cd09808   77 EGK-KLHVLINNA 88
PRK05854 PRK05854
SDR family oxidoreductase;
7-99 1.93e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 45.44  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHmdtlRVAAQEAQSLGGQCVPVV------CDSSQESEVRSLFEQVDR 80
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRN----RAKGEAAVAAIRTAVPDAklslraLDLSSLASVAALGEQLRA 89
                         90       100
                 ....*....|....*....|
gi 296214664  81 EqqGR-LDVLVNNayAGVQT 99
Cdd:PRK05854  90 E--GRpIHLLINN--AGVMT 105
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-196 2.18e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 45.35  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAqslggQCVPVVCDSSQESEVRSLFEQVdreqqgrlDVLV 90
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALP-----GVEFVRGDLRDPEALAAALAGV--------DAVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNayAGVQTILNTRSKAFWET----PASMWDDINNVGLRgHYL----CSVYGarlmvpAGRGLIVVISSPGGLQymfnvP 162
Cdd:COG0451   70 HL--AAPAGVGEEDPDETLEVnvegTLNLLEAARAAGVK-RFVyassSSVYG------DGEGPIDEDTPLRPVS-----P 135
                        170       180       190
                 ....*....|....*....|....*....|....
gi 296214664 163 YGVGKAACDKLAADCAhelRRYGVSYVSLWPGIV 196
Cdd:COG0451  136 YGASKLAAELLARAYA---RRYGLPVTILRPGNV 166
PRK06197 PRK06197
short chain dehydrogenase; Provisional
6-97 2.27e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.40  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 83
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARitAATPGADVTLQELDLTSLASVRAAADAL-RAAY 93
                         90
                 ....*....|....
gi 296214664  84 GRLDVLVNNayAGV 97
Cdd:PRK06197  94 PRIDLLINN--AGV 105
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
9-123 2.91e-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: 44.92  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHM--DTLRVAAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDR---EQQ 83
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSaaAASTLAAELNARRPNSAVTCQADLSNSATLFSRCEAIIDacfRAF 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 296214664   84 GRLDVLVNNAyagvqtilntrsKAFWETPASMWDDINNVG 123
Cdd:TIGR02685  83 GRCDVLVNNA------------SAFYPTPLLRGDAGEGVG 110
PRK05993 PRK05993
SDR family oxidoreductase;
11-199 3.57e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 44.63  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTlrVAAQEAQSLggQCVPVvcDSSQESEVRSLFEQVDREQQGRLDVLV 90
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEED--VAALEAEGL--EAFQL--DYAEPESIAALVAQVLELSGGRLDALF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NN-AYAgvqtilntrskafwetPASMWDDINNVGLRGHYLCSVYG----ARLMVPA----GRGLIVVISSPGGL-QYMFN 160
Cdd:PRK05993  82 NNgAYG----------------QPGAVEDLPTEALRAQFEANFFGwhdlTRRVIPVmrkqGQGRIVQCSSILGLvPMKYR 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 296214664 161 VPYGVGKAACDKLAADCAHELRRYGVsYVSLW-PGIVQTE 199
Cdd:PRK05993 146 GAYNASKFAIEGLSLTLRMELQGSGI-HVSLIePGPIETR 184
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
12-93 5.71e-05

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: 44.02  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRhmDTLRVAAQEAQSLGGQCVpVVCDSSQESEVRSLFEQVDreQQGRLDVLVN 91
Cdd:cd08951   12 ITGSSDGLGLAAARTLLHQGHEVVLHAR--SQKRAADAKAACPGAAGV-LIGDLSSLAETRKLADQVN--AIGRFDAVIH 86

                 ..
gi 296214664  92 NA 93
Cdd:cd08951   87 NA 88
PRK08339 PRK08339
short chain dehydrogenase; Provisional
5-210 9.53e-05

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 43.31  E-value: 9.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSlggqcvpvvcdssqESEVRSLFEQVDREQQG 84
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKS--------------ESNVDVSYIVADLTKRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  85 RLDVLVNNAYA-GVQTIL-----NTRSKAFWETPASMWDDinnvGLRGHYLCSVYGARLMVPA----GRGLIVVISSPGG 154
Cdd:PRK08339  72 DLERTVKELKNiGEPDIFffstgGPKPGYFMEMSMEDWEG----AVKLLLYPAVYLTRALVPAmerkGFGRIIYSTSVAI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664 155 LQYMFNVPYG-VGKAACDKLAADCAHELRRYGVSYVSLWPGIVQT---ELLKEHMAKEEG 210
Cdd:PRK08339 148 KEPIPNIALSnVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTdrvIQLAQDRAKREG 207
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
10-82 1.21e-04

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: 43.14  E-value: 1.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296214664  10 CVVTGASRGIGRGIALQLCKAGAT-VYITGRHMDTLRVAAQEAQSLGGQCVPVV--CDSSQESEVRSLFEQVDREQ 82
Cdd:cd05274  153 YLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLRAGGARVSVvrCDVTDPAALAALLAELAAGG 228
PRK06482 PRK06482
SDR family oxidoreductase;
12-154 1.27e-04

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 42.80  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDTLR-VAAQEAQSLGgqcvPVVCDSSQESEVRSLFEQVDREqQGRLDVLV 90
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDdLKARYGDRLW----VLQLDVTDSAAVRAVVDRAFAA-LGRIDVVV 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296214664  91 NNAYAGVQTILNTRSKAFWETPAsmwdDINNVGlrghylcSVYGARLMVP----AGRGLIVVISSPGG 154
Cdd:PRK06482  82 SNAGYGLFGAAEELSDAQIRRQI----DTNLIG-------SIQVIRAALPhlrrQGGGRIVQVSSEGG 138
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
11-210 1.52e-04

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: 42.48  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVyitgrhmdtLRVAAQEAQslggqcvpVVCDSSQESEVRSLFEQVDREQQGRLDVLV 90
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTV---------IGIDLREAD--------VIADLSTPEGRAAAIADVLARCSGVLDGLV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYAGVQTILNTRSKafwetpasmwddINNVGLRgHYLCSVygARLMVPAGRGLIVVISSPGGLQYMFNVP-------- 162
Cdd:cd05328   66 NCAGVGGTTVAGLVLK------------VNYFGLR-ALMEAL--LPRLRKGHGPAAVVVSSIAGAGWAQDKLelakalaa 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296214664 163 --------------------YGVGKAACDKLAADCAHE-LRRYGVSYVSLWPGIVQTELLKEHMAKEEG 210
Cdd:cd05328  131 gtearavalaehagqpgylaYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRG 199
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
11-199 2.14e-04

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: 41.79  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYItgrHMDTLRVAAqEAQSLGGQCVPVVCDSSQESevRSLFEQVdREQQGRLDVLV 90
Cdd:cd05361    5 LVTHARHFAGPASAEALTEDGYTVVC---HDASFADAA-ERQAFESENPGTKALSEQKP--EELVDAV-LQAGGAIDVLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYagvqtilntrskafWETPASMWDDINNVGLRGHYLCSVYGARLMVPA--------GRGLIVVISSPGGLQYMFNVP 162
Cdd:cd05361   78 SNDY--------------IPRPMNPIDGTSEADIRQAFEALSIFPFALLQAaiaqmkkaGGGSIIFITSAVPKKPLAYNS 143
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296214664 163 -YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTE 199
Cdd:cd05361  144 lYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSP 181
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
11-93 3.27e-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: 41.03  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVaaqeaqslggqcvpvvcDSSQESEVRSLFEQVdreqqGRLDVLV 90
Cdd:cd11731    2 IVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQV-----------------DITDEASIKALFEKV-----GHFDAIV 59

                 ...
gi 296214664  91 NNA 93
Cdd:cd11731   60 STA 62
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-81 3.99e-04

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: 40.62  E-value: 3.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296214664   11 VVTGASRGIGRGIALQLCKAGA-TVYITGRHMDTLRVAAQ---EAQSLGGQCVPVVCDSSQESEVRSLFEQVDRE 81
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQAliaELEARGVEVVVVACDVSDPDAVAALLAEIKAE 78
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
9-220 4.47e-04

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: 41.05  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664    9 VCVVTGASRGIGRGIALQLCKA----GATVYITGRHMDTLRV--AAQEAQSLGGQCVPVVCDSSQESEV----RSLFEQV 78
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQlkAEIGAERSGLRVVRVSLDLGAEAGLeqllKALRELP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   79 DREQQGRLdVLVNNayAGVQTILNTRSKAFWETPASMWDDINNVGLRGHYLCSVYGARLMVPAGRGLIVVISSPGGLQYM 158
Cdd:TIGR01500  82 RPKGLQRL-LLINN--AGTLGDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVVNISSLCAIQPF 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296214664  159 FNVP-YGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTELlkEHMAKEEGLQDPVFKQLR 220
Cdd:TIGR01500 159 KGWAlYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM--QQQVREESVDPDMRKGLQ 219
PRK05884 PRK05884
SDR family oxidoreductase;
11-91 6.89e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 40.18  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGgqcvpVVCDSSQES---EVRSLFEQvdreqqgRLD 87
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDA-----IVCDNTDPAsleEARGLFPH-------HLD 71

                 ....
gi 296214664  88 VLVN 91
Cdd:PRK05884  72 TIVN 75
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
7-96 8.22e-04

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 40.47  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGAS--RGIGRGIALQLCKAGATVYIT------GRHMDTLR-VAAQEAQSLggqCVPvvCDSSQESEVRSLFEQ 77
Cdd:PRK07370   6 GKKALVTGIAnnRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVReLTEPLNPSL---FLP--CDVQDDAQIEETFET 80
                         90       100
                 ....*....|....*....|
gi 296214664  78 VdREQQGRLDVLVNN-AYAG 96
Cdd:PRK07370  81 I-KQKWGKLDILVHClAFAG 99
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
9-93 1.26e-03

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: 39.00  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664     9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRHMDTLRVAA---QEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 84
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAallAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80

                   ....*....
gi 296214664    85 RLDVLVNNA 93
Cdd:smart00822  81 PLTGVIHAA 89
PRK06953 PRK06953
SDR family oxidoreductase;
12-200 2.59e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 38.51  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  12 VTGASRGIGRGIALQLCKAGATVYITGRHMDtlrvAAQEAQSLGGQCVPVvcDSSQESEVRSLFEQVDREqqgRLDVLVN 91
Cdd:PRK06953   6 IVGASRGIGREFVRQYRADGWRVIATARDAA----ALAALQALGAEALAL--DVADPASVAGLAWKLDGE---ALDAAVY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  92 NayAGVqtiLNTRSKAFWETPASMWDDINNVGLRGhYLCSVYGARLMVPAGRGLIVVISSP----GGLQYMFNVPYGVGK 167
Cdd:PRK06953  77 V--AGV---YGPRTEGVEPITREDFDAVMHTNVLG-PMQLLPILLPLVEAAGGVLAVLSSRmgsiGDATGTTGWLYRASK 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 296214664 168 AACDKLAADCAHELRRygVSYVSLWPGIVQTEL 200
Cdd:PRK06953 151 AALNDALRAASLQARH--ATCIALHPGWVRTDM 181
PRK08017 PRK08017
SDR family oxidoreductase;
11-198 2.67e-03

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 38.53  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  11 VVTGASRGIGRGIALQLCKAGATVYITGRHMDTLrvaaQEAQSLGGQCVPVVCDSSQEseVRSLFEQVDREQQGRLDVLV 90
Cdd:PRK08017   6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDV----ARMNSLGFTGILLDLDDPES--VERAADEVIALTDNRLYGLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  91 NNAYAGVQTILNTRSKAFWETPASMwddiNNVGLrgHYLCSvygaRL---MVPAGRGLIVVISSPGGLqymFNVPyGVGK 167
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFST----NFFGT--HQLTM----LLlpaMLPHGEGRIVMTSSVMGL---ISTP-GRGA 145
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296214664 168 AACDKLAADC-----AHELRRYGVSyVSLW-PGIVQT 198
Cdd:PRK08017 146 YAASKYALEAwsdalRMELRHSGIK-VSLIePGPIRT 181
PLN02780 PLN02780
ketoreductase/ oxidoreductase
7-93 2.68e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 39.08  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQEAQSLGG--QCVPVVCDSSQESE--VRSLFEQVDREQ 82
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSktQIKTVVVDFSGDIDegVKRIKETIEGLD 132
                         90
                 ....*....|.
gi 296214664  83 QGrldVLVNNA 93
Cdd:PLN02780 133 VG---VLINNV 140
PRK08251 PRK08251
SDR family oxidoreductase;
8-200 2.95e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 38.38  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHMDTLRVAAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGR 85
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAEllARYPGIKVAVAALDVNDHDQVFEVFAEFRDE-LGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296214664  86 LDVLVNNAYAGVQTILNTRSkaFWETPASMwdDINNVGLrghyLCSVYGA-RLMVPAGRGLIVVISS-------PGGLqy 157
Cdd:PRK08251  82 LDRVIVNAGIGKGARLGTGK--FWANKATA--ETNFVAA----LAQCEAAmEIFREQGSGHLVLISSvsavrglPGVK-- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296214664 158 mfnVPYGVGKAACDKLAADCAHELRRYGVSYVSLWPGIVQTEL 200
Cdd:PRK08251 152 ---AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH