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Conserved domains on  [gi|1269612287|ref|NP_001344203|]
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short-chain dehydrogenase/reductase 3 isoform 2 [Mus musculus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143197)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to human 17-beta-hydroxysteroid dehydrogenase type XI that preferentially converts 5 alpha-androstane-3 alpha,17 beta-diol (3-alpha-diol) to androsterone; 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 27-255 1.07e-112

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: 324.58  E-value: 1.07e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:cd05339    14 LLALEFAKRGA-KVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL--DCP 184
Cdd:cd05339    93 LELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLELKayGKP 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAA 255
Cdd:cd05339   173 GIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTNQQMLYLPFYAYFLPILKRTLPTPV 243
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 27-255 1.07e-112

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: 324.58  E-value: 1.07e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:cd05339    14 LLALEFAKRGA-KVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL--DCP 184
Cdd:cd05339    93 LELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLELKayGKP 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAA 255
Cdd:cd05339   173 GIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTNQQMLYLPFYAYFLPILKRTLPTPV 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
28-254 1.34e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.98  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:COG0300    21 LARALAARGAR-VVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:COG0300   100 ELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAP-TGVR 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 188 ATTVLPFHTSTEMFQGMRVRFPNlfPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQA 254
Cdd:COG0300   179 VTAVCPGPVDTPFTARAGAPAGR--PLLSPEEVARAILRALERGRAEVYVGWDARLLARLLRLLPRL 243
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 28-202 3.40e-31

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 114.63  E-value: 3.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:pfam00106  16 IAKRLAKEGAKVVLV-DRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:pfam00106  95 ELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAP-HGIR 173

                         170
                  ....*....|....*
gi 1269612287 188 ATTVLPFHTSTEMFQ 202
Cdd:pfam00106 174 VNAVAPGGVDTDMTK 188
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 29-229 2.64e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 107.70  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-VHGKsLM 107
Cdd:PRK07109   25 ARAFARRGAK-VVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMVtVFGP-FE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL-DCPGV 186
Cdd:PRK07109  103 DVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCELLhDGSPV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRFPN---LFPPL-KPETVARRTVDAVQ 229
Cdd:PRK07109  183 SVTMVQPPAVNTPQFDWARSRLPVepqPVPPIyQPEVVADAILYAAE 229
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 21-176 8.25e-09

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: 54.03  E-value: 8.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   21 GRGIGRHLAREFAERGARKIVLWGRT---EKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNN 97
Cdd:smart00822   9 LGGLGRALARWLAERGARRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVIHA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   98 AAVVHGKSLMDSDDDALlksQHVntlgqfWTTK---------AFLPRMLElqngHIVCLNSVLALSAIPGAIDYctskAS 168
Cdd:smart00822  89 AGVLDDGVLASLTPERF---AAV------LAPKaagawnlheLTADLPLD----FFVLFSSIAGVLGSPGQANY----AA 151


                   ....*...
gi 1269612287  169 AFAFMESL 176
Cdd:smart00822 152 ANAFLDAL 159
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 30-178 2.34e-08

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: 53.76  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  30 REFAERGARKI-------VLWGRTEKCLKETTEEIRQM--GTECHYFICDVGNREEVYQMAKAVREKVG----DITILVN 96
Cdd:TIGR01500  14 RTIAQELAKCLkspgsvlVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKALRELPRpkglQRLLLIN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  97 NAAVVH--GKSLMD-SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ--NGHIVCLNSVLALSAIPGAIDYCTSKASAFA 171
Cdd:TIGR01500  94 NAGTLGdvSKGFVDlSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPglNRTVVNISSLCAIQPFKGWALYCAGKAARDM 173


                  ....*..
gi 1269612287 172 FMESLTL 178
Cdd:TIGR01500 174 LFQVLAL 180
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 27-255 1.07e-112

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: 324.58  E-value: 1.07e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:cd05339    14 LLALEFAKRGA-KVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL--DCP 184
Cdd:cd05339    93 LELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLELKayGKP 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAA 255
Cdd:cd05339   173 GIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTNQQMLYLPFYAYFLPILKRTLPTPV 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
28-254 1.34e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.98  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:COG0300    21 LARALAARGAR-VVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:COG0300   100 ELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAP-TGVR 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 188 ATTVLPFHTSTEMFQGMRVRFPNlfPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQA 254
Cdd:COG0300   179 VTAVCPGPVDTPFTARAGAPAGR--PLLSPEEVARAILRALERGRAEVYVGWDARLLARLLRLLPRL 243
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 28-222 7.75e-44

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: 148.59  E-value: 7.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETtEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd05233    14 IARRLAREGAK-VVLADRNEEALAEL-AAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:cd05233    92 ELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAP-YGIR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1269612287 188 ATTVLPFHTSTEMFQGMRVRFPN--------LFPPLKPETVAR 222
Cdd:cd05233   171 VNAVAPGLVDTPMLAKLGPEEAEkelaaaipLGRLGTPEEVAE 213
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 29-205 1.46e-43

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: 148.40  E-value: 1.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:COG1028    23 ARALAAEGAR-VVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLTLGL---LDCPG 185
Cdd:COG1028   102 LTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA----VVGLTRSLaleLAPRG 177

                         170       180
                  ....*....|....*....|
gi 1269612287 186 VSATTVLPFHTSTEMFQGMR 205
Cdd:COG1028   178 IRVNAVAPGPIDTPMTRALL 197
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-230 1.68e-41

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: 142.63  E-value: 1.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:COG4221    21 TARALAAAGAR-VVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCpGVS 187
Cdd:COG4221    97 ELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPT-GIR 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1269612287 188 ATTVLPFHTSTEMFQGMRVRFPN-------LFPPLKPETVARRTVDAVQQ 230
Cdd:COG4221   176 VTVIEPGAVDTEFLDSVFDGDAEaaaavyeGLEPLTPEDVAEAVLFALTQ 225
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-253 7.40e-32

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: 118.07  E-value: 7.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARkIVLWGRTEKCLKETTEEIRQMG-TECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAvVHGKS 105
Cdd:cd05332    18 ELAYHLARLGAR-LVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFGGLDILINNAG-ISMRS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 106 LMDSDD-DALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGlLDCP 184
Cdd:cd05332    96 LFHDTSiDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAE-LSEP 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 185 GVSATTVLP--------FHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILII-LKSILPQ 253
Cdd:cd05332   175 NISVTVVCPglidtniaMNALSGDGSMSAKMDDTTANGMSPEECALEILKAIALRKREVFYARQVPLLAVyLRQLFPG 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 28-202 3.40e-31

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 114.63  E-value: 3.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:pfam00106  16 IAKRLAKEGAKVVLV-DRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:pfam00106  95 ELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAP-HGIR 173

                         170
                  ....*....|....*
gi 1269612287 188 ATTVLPFHTSTEMFQ 202
Cdd:pfam00106 174 VNAVAPGGVDTDMTK 188
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 29-229 3.89e-31

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: 115.56  E-value: 3.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-VHGKsLM 107
Cdd:cd05360    17 ALAFAERGA-KVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVaVFGR-FE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL-LDCPGV 186
Cdd:cd05360    95 DVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELaHDGAPI 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRF---PNLFPPL-KPETVARRTVDAVQ 229
Cdd:cd05360   175 SVTLVQPTAMNTPFFGHARSYMgkkPKPPPPIyQPERVAEAIVRAAE 221
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 28-227 4.86e-31

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: 115.43  E-value: 4.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIR----QMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHG 103
Cdd:cd08939    17 LAKELVKEGA-NVIIVARSESKLEEAVEEIEaeanASGQKVSYISADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 104 KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLdC 183
Cdd:cd08939    96 GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELK-P 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 184 PGVSATTVLPFHTSTEMFQGMRVRFPNLF-------PPLKPETVARRTVDA 227
Cdd:cd08939   175 YNIRVSVVYPPDTDTPGFEEENKTKPEETkaiegssGPITPEEAARIIVKG 225
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 29-200 1.44e-28

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: 109.17  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM- 107
Cdd:cd05333    17 ALRLAAEGA-KVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAGITRDNLLMr 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 --DSDDDALLKsqhVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPG 185
Cdd:cd05333    96 msEEDWDAVIN---VNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELAS-RG 171

                         170
                  ....*....|....*
gi 1269612287 186 VSATTVLPFHTSTEM 200
Cdd:cd05333   172 ITVNAVAPGFIDTDM 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 29-229 2.64e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 107.70  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-VHGKsLM 107
Cdd:PRK07109   25 ARAFARRGAK-VVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMVtVFGP-FE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL-DCPGV 186
Cdd:PRK07109  103 DVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCELLhDGSPV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRFPN---LFPPL-KPETVARRTVDAVQ 229
Cdd:PRK07109  183 SVTMVQPPAVNTPQFDWARSRLPVepqPVPPIyQPEVVADAILYAAE 229
PRK05855 PRK05855
SDR family oxidoreductase;
29-233 7.28e-27

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 109.30  E-value: 7.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK05855  332 ALAFAREGAE-VVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIGMAGGFLD 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLA------LSAipgaidYCTSKASAFAFMESLTLGLL 181
Cdd:PRK05855  411 TSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAyapsrsLPA------YATSKAAVLMLSECLRAELA 484

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 182 D--------CPGV-----SATTVLPfHTSTEMFQGMRVRFPNLFP--PLKPETVARRTVDAVQQNQA 233
Cdd:PRK05855  485 AagigvtaiCPGFvdtniVATTRFA-GADAEDEARRRGRADKLYQrrGYGPEKVAKAIVDAVKRNKA 550
PRK12826 PRK12826
SDR family oxidoreductase;
29-221 1.58e-26

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 103.84  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK12826   23 AVRLAADGAEVIVV-DICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLAL-SAIPGAIDYCTSKASAFAFMESLTLgLLDCPGVS 187
Cdd:PRK12826  102 MDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPrVGYPGLAHYAASKAGLVGFTRALAL-ELAARNIT 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 188 ATTVLPFHTSTEMFQ--GMRVRFPNL--FPPLK----PETVA 221
Cdd:PRK12826  181 VNSVHPGGVDTPMAGnlGDAQWAEAIaaAIPLGrlgePEDIA 222
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 27-177 3.24e-26

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: 102.51  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTEchYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV--HGK 104
Cdd:pfam13561  11 AIARALAEEGAE-VVLTDLNEALAKRVEELAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApkLKG 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLT 177
Cdd:pfam13561  88 PFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE--GGSIVNLSSIGAERVVPNYNAYGAAKAA----LEALT 154
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-251 5.55e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 103.51  E-value: 5.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARkIVLWGRTEKCLKETTEEirqMGTEC--HYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK 104
Cdd:PRK05872   24 ELARRLHARGAK-LALVDLEEAELAALAAE---LGGDDrvLTVVADVTDLAAMQAAAEEAVERFGGIDVVVANAGIASGG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcP 184
Cdd:PRK05872  100 SVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIE-RRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAH-H 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 185 GVSATTVLPFHTSTEM----------FQGMRVRFPnlfPPLK----PETVARRTVDAVQQNQALLLLPWTMNILIILKSI 250
Cdd:PRK05872  178 GVTVGSAYLSWIDTDLvrdadadlpaFRELRARLP---WPLRrttsVEKCAAAFVDGIERRARRVYAPRWVRLMQWLRPV 254


                  .
gi 1269612287 251 L 251
Cdd:PRK05872  255 L 255
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 29-265 2.21e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 101.56  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQmgteCHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK07825   22 ARALAALGAR-VAIGDLDEALAKETAAELGL----VVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSA 188
Cdd:PRK07825   97 EPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDAARLELRG-TGVHV 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 189 TTVLPFHTSTEMFQGmrVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGT 265
Cdd:PRK07825  176 SVVLPSFVNTELIAG--TGGAKGFKNVEPEDVAAAIVGTVAKPRPEVRVPRALGPLAQAQRLLPRRVREALNRLLGG 250
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
29-176 7.95e-25

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 99.08  E-value: 7.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA-----AVVHG 103
Cdd:PRK05653   22 ALRLAADGAK-VVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAgitrdALLPR 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 104 kslMDSDD-DALLksqHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK05653  101 ---MSEEDwDRVI---DVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKAL 168
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-242 2.37e-24

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 97.84  E-value: 2.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK07666   23 VAIALAKEGVN-VGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:PRK07666  102 ELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRK-HNIR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 188 ATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLL---LPWTMN 242
Cdd:PRK07666  181 VTALTPSTVATDMAVDLGLTDGNPDKVMQPEDLAEFIVAQLKLNKRTFIksaGLWSTN 238
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 22-201 7.84e-24

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 96.80  E-value: 7.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRTEKCLKET-TEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:PRK05557   15 RGIGRAIAERLAAQGA-NVVINYASSEAGAEAlVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNAGI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLTLGL 180
Cdd:PRK05557   94 TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG----VIGFTKSL 169

                         170       180
                  ....*....|....*....|....
gi 1269612287 181 ---LDCPGVSATTVLPFHTSTEMF 201
Cdd:PRK05557  170 areLASRGITVNAVAPGFIETDMT 193
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
28-228 8.42e-24

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 96.79  E-value: 8.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKcLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK08226   22 IARVFARHGA-NLILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLA-LSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGV 186
Cdd:PRK08226  100 DMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAAIVGLTKSLAVEYAQ-SGI 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRfpnlFPPLKPETVARRTVDAV 228
Cdd:PRK08226  179 RVNAICPGYVRTPMAESIARQ----SNPEDPESVLTEMAKAI 216
PRK06181 PRK06181
SDR family oxidoreductase;
28-252 2.13e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 95.82  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK06181   17 LAVRLARAGAQ-LVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDILVNNAGITMWSRFD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALL-KSQHVNTLGQFWTTKAFLPRMLELQnGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGV 186
Cdd:PRK06181   96 ELTDLSVFeRVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLRIELAD-DGV 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 187 SATTVLPFHTSTEM------FQGMrvrfPNLFPPLK------PETVARRTVDAVQQNQALLLLPWTMNILIILKSILP 252
Cdd:PRK06181  174 AVTVVCPGFVATDIrkraldGDGK----PLGKSPMQeskimsAEECAEAILPAIARRKRLLVMSLRGRLGRWLKLIAP 247
PRK08264 PRK08264
SDR family oxidoreductase;
27-236 3.11e-23

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 94.96  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRTekclketTEEIRQMGTECHYFICDVGNREEVYQMAkavrEKVGDITILVNNAAVVHGKSL 106
Cdd:PRK08264   21 AFVEQLLARGAAKVYAAARD-------PESVTDLGPRVVPLQLDVTDPASVAAAA----EAASDVTILVNNAGIFRTGSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQ-HVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFafmeSLTLGL---LD 182
Cdd:PRK08264   90 LLEGDEDALRAEmETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAW----SLTQALraeLA 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 183 CPGVSATTVLPFHTSTEMFQGMRVrfpnlfPPLKPETVARRTVDAVQQNQALLL 236
Cdd:PRK08264  166 PQGTRVLGVHPGPIDTDMAAGLDA------PKASPADVARQILDALEAGDEEVL 213
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-176 9.54e-23

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 93.78  E-value: 9.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKV 88
Cdd:PRK12825    3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKAS 168
Cdd:PRK12825   83 GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAG 162


                  ....*...
gi 1269612287 169 AFAFMESL 176
Cdd:PRK12825  163 LVGLTKAL 170
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-199 2.93e-22

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: 92.72  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd05344    18 ARALAREGAR-VAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFAE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSA 188
Cdd:cd05344    97 LTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAP-DGVTV 175

                         170
                  ....*....|.
gi 1269612287 189 TTVLPFHTSTE 199
Cdd:cd05344   176 NSVLPGYIDTE 186
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 22-238 5.79e-22

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: 91.64  E-value: 5.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:cd05359     8 RGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVSNAAAG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLl 181
Cdd:cd05359    88 AFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVRYLAVEL- 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 182 dCP-GVSATTVLPFHTSTEMFQgmrvRFPNLFPPLKPE---TVARR--TVDAVQQNQALLLLP 238
Cdd:cd05359   167 -GPrGIRVNAVSPGVIDTDALA----HFPNREDLLEAAaanTPAGRvgTPQDVADAVGFLCSD 224
PRK07024 PRK07024
SDR family oxidoreductase;
28-254 7.57e-22

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 91.53  E-value: 7.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEiRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK07024   18 LAREYARQGAT-LGLVARRTDALQAFAAR-LPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIANAGISVGTLTE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDD-DALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGV 186
Cdd:PRK07024   96 EREDlAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRP-AGV 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRFPNLFPplkPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQA 254
Cdd:PRK07024  175 RVVTIAPGYIRTPMTAHNPYPMPFLMD---ADRFAARAARAIARGRRFRVIPWQMGVVAKLLRVLPRW 239
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 27-222 9.54e-22

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: 90.50  E-value: 9.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARkIVLWGRTEKCLKETTEEirqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:cd08932    15 EIARALARDGYR-VSLGLRNPEDLAALSAS----GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIGRPTTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGV 186
Cdd:cd08932    90 REGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWD-HGV 168

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1269612287 187 SATTVLPFHTSTEMFQGMRVRfpNLFPPL---KPETVAR 222
Cdd:cd08932   169 RVSAVCPGFVDTPMAQGLTLV--GAFPPEemiQPKDIAN 205
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 28-253 1.04e-21

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: 90.85  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd05350    14 LAREFAKAGYN-VALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVIINAGVGKGTSLG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTlGLLDCPGVS 187
Cdd:cd05350    93 DLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESLR-YDVKKRGIR 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 188 ATTVLPFHTSTEMFQGMrvrFPnLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQ 253
Cdd:cd05350   172 VTVINPGFIDTPLTANM---FT-MPFLMSVEQAAKRIYKAIKKGAAEPTFPWRLAVPLRLLKLLPE 233
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 27-201 1.58e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 90.42  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRTEKcLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK12939   22 AFAEALAEAGATVAFNDGLAAE-ARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLTLGL---LDC 183
Cdd:PRK12939  101 TELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGA----VIGMTRSLareLGG 176

                         170
                  ....*....|....*...
gi 1269612287 184 PGVSATTVLPFHTSTEMF 201
Cdd:PRK12939  177 RGITVNAIAPGLTATEAT 194
PRK06194 PRK06194
hypothetical protein; Provisional
 30-232 1.17e-20

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 88.92  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  30 REFAERGAR---KIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK06194   20 LAFARIGAAlgmKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHLLFNNAGVGAGGLV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDddalLKSQH----VNTLGQFWTTKAFLPRMLE------LQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK06194  100 WENS----LADWEwvlgVNLWGVIHGVRAFTPLMLAaaekdpAYEGHIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 177 --TLGLLDCPgVSATTVLPFHTSTEMFQGMRVR---FPNLFPPLKP-------------------ETVARRTVDAVQQNQ 232
Cdd:PRK06194  176 yqDLSLVTDQ-VGASVLCPYFVPTGIWQSERNRpadLANTAPPTRSqliaqamsqkavgsgkvtaEEVAQLVFDAIRAGR 254
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 28-222 1.45e-20

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: 87.83  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKC------------LKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILV 95
Cdd:cd05338    19 IALRLAKAGA-TVVVAAKTASEgdngsakslpgtIEETAEEIEAAGGQALPIVVDVRDEDQVRALVEATVDQFGRLDILV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  96 NNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMES 175
Cdd:cd05338    98 NNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVAYAAGKAG----MSR 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 176 LTLGL---LDCPGVSATTVLPfHTSTEMFQGMRVrFPNLFPPL--KPETVAR 222
Cdd:cd05338   174 LTLGLaaeLRRHGIAVNSLWP-STAIETPAATEL-SGGSDPARarSPEILSD 223
PRK05650 PRK05650
SDR family oxidoreductase;
28-261 2.82e-20

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 87.40  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK05650   16 IALRWAREGWR-LALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAGVASGGFFE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 D---SDDDALLKsqhVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcP 184
Cdd:PRK05650   95 ElslEDWDWQIA---INLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVELAD-D 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFPN-------LF--PPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAA 255
Cdd:PRK05650  171 EIGVHVVCPSFFQTNLLDSFRGPNPAmkaqvgkLLekSPITAADIADYIYQQVAKGEFLILPHEQGRRAWQLKRQAPQAL 250


                  ....*.
gi 1269612287 256 LEEIHR 261
Cdd:PRK05650  251 YDEMTL 256
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 30-232 3.35e-20

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: 86.69  E-value: 3.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  30 REFAERGARKIVLWGRTEKCLKETTEEirqMGTECHYFICDVGNREEVyqmaKAVREKVGDITILVNNAAVVHGKSLMDS 109
Cdd:cd05354    21 ESLLAHGAKKVYAAVRDPGSAAHLVAK---YGDKVVPLRLDVTDPESI----KAAAAQAKDVDVVINNAGVLKPATLLEE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 110 DDDALLKSQ-HVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSA 188
Cdd:cd05354    94 GALEALKQEmDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQGLRAELAA-QGTLV 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1269612287 189 TTVLPFHTSTEMFQGMRvrfpnlFPPLKPETVARRTVDAVQQNQ 232
Cdd:cd05354   173 LSVHPGPIDTRMAAGAG------GPKESPETVAEAVLKALKAGE 210
FabG-like PRK07231
SDR family oxidoreductase;
22-192 4.45e-20

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 86.42  E-value: 4.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTeCHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK07231   15 SGIGEGIARRFAAEGAR-VVVTDRNEEAAERVAAEILAGGR-AIAVAADVSDEADVEAAVAAALERFGSVDILVNNAGTT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HG-KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK07231   93 HRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAEL 172

                         170       180
                  ....*....|....*....|
gi 1269612287 181 LD--------CPGVSATTVL 192
Cdd:PRK07231  173 GPdkirvnavAPVVVETGLL 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 28-228 1.39e-19

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: 85.36  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKEtteEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd05374    16 LALALAAQGYR-VIATARNPDKLES---LGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKasaFAfMESLTLGL---LDCP 184
Cdd:cd05374    92 ETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASK---AA-LEALSESLrleLAPF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFP---------------------NLFPPLKPETVARRTVDAV 228
Cdd:cd05374   168 GIKVTIIEPGPVRTGFADNAAGSALedpeispyaperkeikenaagVGSNPGDPEKVADVIVKAL 232
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 29-221 1.85e-19

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: 85.02  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQ-MGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGkslM 107
Cdd:cd05346    17 ARRFAKAGA-KLILTGRRAERLQELADELGAkFPVKVLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAGLALG---L 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DS-DDDALLKSQHV---NTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLD- 182
Cdd:cd05346    93 DPaQEADLEDWETMidtNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGt 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1269612287 183 -------CPGVSATTvlpFhtSTEMFQGMRVRFPNLFP---PLKPETVA 221
Cdd:cd05346   173 girvtniEPGLVETE---F--SLVRFHGDKEKADKVYEgvePLTPEDIA 216
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 28-176 1.32e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 82.69  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK08213   28 IAEALGEAGAR-VVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDILVNNAGATWGAPAE 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPR-MLELQNGHIVCLNSVLAL----SAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK08213  107 DHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLggnpPEVMDTIAYNTSKGAVINFTRAL 180
PRK07814 PRK07814
SDR family oxidoreductase;
28-237 4.96e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 81.36  E-value: 4.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK07814   26 IALAFAEAGA-DVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDIVVNNVGGTMPNPLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCTSKAsAFAFMESLTlgLLD-CPG 185
Cdd:PRK07814  105 STSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKA-ALAHYTRLA--ALDlCPR 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 186 VSATTVLPFHTSTEMFQGMRVRfPNLFPPLKPETVARRTVDAVQQNQALLLL 237
Cdd:PRK07814  182 IRVNAIAPGSILTSALEVVAAN-DELRAPMEKATPLRRLGDPEDIAAAAVYL 232
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 28-193 5.99e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 80.77  E-value: 5.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHG-KSL 106
Cdd:PRK07890   21 LAVRAARAGA-DVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAFRVPSmKPL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLT--LGlldcP 184
Cdd:PRK07890  100 ADADFAHWRAVIELNVLGTLRLTQAFTPALAE-SGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLAteLG----P 174

                         170
                  ....*....|
gi 1269612287 185 -GVSATTVLP 193
Cdd:PRK07890  175 qGIRVNSVAP 184
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-176 7.76e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 80.27  E-value: 7.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK05565   15 GGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNAGIS 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLAL-SAIPGAIdYCTSKASAFAFMESL 176
Cdd:PRK05565   95 NFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLiGASCEVL-YSASKGAVNAFTKAL 169
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-200 1.14e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 80.21  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKclkeTTEEIRQMGTEChyFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK06463   23 IAEAFLREGAKVAVLYNSAEN----EAKELREKGVFT--IKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLAL-SAIPGAIDYCTSKASAFAFMESLTLGLLDCpGV 186
Cdd:PRK06463   97 EFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKAGIIILTRRLAFELGKY-GI 175

                         170
                  ....*....|....
gi 1269612287 187 SATTVLPFHTSTEM 200
Cdd:PRK06463  176 RVNAVAPGWVETDM 189
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 29-192 2.80e-17

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: 78.67  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLwgrtekCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKavreKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd05368    19 ALAFAREGANVIAT------DINEEKLKELERGPGITTRVLDVTDKEQVAALAK----EEGRIDVLFNCAGFVHHGSILD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLA-LSAIPGAIDYCTSKASAFAFMESLTLGLLD----- 182
Cdd:cd05368    89 CEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKSVAADFAQqgirc 168

                         170
                  ....*....|...
gi 1269612287 183 ---CPGVSATTVL 192
Cdd:cd05368   169 naiCPGTVDTPSL 181
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 28-167 6.19e-17

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: 77.78  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd05347    21 IASGLAEAGA-NIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAE 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKA 167
Cdd:cd05347   100 EFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKG 159
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 29-178 6.53e-17

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: 78.01  E-value: 6.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGT-ECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAvvhGKSLM 107
Cdd:cd05369    20 AKAFAELGAS-VAIAGRKPEVLEAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFGKIDILINNAA---GNFLA 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 108 DSDD------DALLKsqhVNTLGQFWTTKAFLPRMLELQN-GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTL 178
Cdd:cd05369    96 PAESlspngfKTVID---IDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAV 170
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-166 7.44e-17

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 78.00  E-value: 7.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK12429   19 EIALALAKEGA-KVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILVNNAGIQHVAPI 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 107 MD---SDDDALLKsqhVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK12429   98 EDfptEKWKKMIA---IMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
22-177 7.82e-17

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 77.84  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK08063   14 RGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVFVNNAASG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDsdddalLKSQHVNtlgqfWT----TKAFL-------PRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASaf 170
Cdd:PRK08063   94 VLRPAME------LEESHWD-----WTmninAKALLfcaqeaaKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAA-- 160


                  ....*..
gi 1269612287 171 afMESLT 177
Cdd:PRK08063  161 --LEALT 165
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 29-230 1.35e-16

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: 76.81  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd08934    20 ARALAAEGA-AVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVED 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL----TLGLLDC- 183
Cdd:cd08934    99 ADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLrqevTERGVRVv 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1269612287 184 ---PGVSATTvLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQ 230
Cdd:cd08934   179 viePGTVDTE-LRDHITHTITKEAYEERISTIRKLQAEDIAAAVRYAVTA 227
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 9-232 2.32e-16

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: 75.81  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARKIVLwGRTEKCLKETTEEIRQMgtecHYFICDVGNREEVYQMAKAVREKV 88
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIIT-GRREERLAEAKKELPNI----HTIVLDVGDAESVEALAEALLSEY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMD--SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:cd05370    77 PNLDILINNAGIQRPIDLRDpaSDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 167 ASAFAFMESLTLGLLDCpGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQ 232
Cdd:cd05370   157 AALHSYTLALRHQLKDT-GVEVVEIVPPAVDTELHEERRNPDGGTPRKMPLDEFVDEVVAGLERGR 221
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 29-229 3.80e-16

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: 75.24  E-value: 3.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKclkETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd08929    17 ARLLHAEGYR-VGICARDEA---RLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 -SDDDALLKSQHVNTLGQFWTTKAfLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCpGVS 187
Cdd:cd08929    93 lTPEEWRLVLDTNLTGAFYCIHKA-APALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREA-NIR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 188 ATTVLPFHTSTEmFQGmrvRFPNLFPPLKPETVARRTVDAVQ 229
Cdd:cd08929   171 VVNVMPGSVDTG-FAG---SPEGQAWKLAPEDVAQAVLFALE 208
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 22-201 3.80e-16

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: 75.77  E-value: 3.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:cd05362    13 RGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILVNNAGVM 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL 181
Cdd:cd05362    93 LKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRD--GGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELG 170

                         170       180
                  ....*....|....*....|
gi 1269612287 182 DcPGVSATTVLPFHTSTEMF 201
Cdd:cd05362   171 G-RGITVNAVAPGPVDTDMF 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 29-238 3.82e-16

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 76.15  E-value: 3.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK05876   23 GTEFARRGAR-VVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSNAGIVVGGPIVE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLE-LQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:PRK05876  102 MTHDDWRWVIDVDLWGSIHTVEAFLPRLLEqGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETLAREVTA-DGIG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 188 ATTVLPFHTSTEMFQGM-RVR---------------FPNLFPPLKPETVARRTVDAVQQNQaLLLLP 238
Cdd:PRK05876  181 VSVLCPMVVETNLVANSeRIRgaacaqssttgspgpLPLQDDNLGVDDIAQLTADAILANR-LYVLP 246
PRK07062 PRK07062
SDR family oxidoreductase;
29-169 5.79e-16

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 75.46  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFI--CDVGNREEVYQMAKAVREKVGDITILVNNAavvhGKSL 106
Cdd:PRK07062   25 VELLLEAGA-SVAICGRDEERLASAEARLREKFPGARLLAarCDVLDEADVAAFAAAVEARFGGVDMLVNNA----GQGR 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 107 M----DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIdyCTSKASA 169
Cdd:PRK07062  100 VstfaDTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMV--ATSAARA 164
PRK07201 PRK07201
SDR family oxidoreductase;
29-227 1.28e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 76.53  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK07201  388 AIKVAEAGA-TVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNNAGRSIRRSVEN 466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDA--LLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFME---SLTLGLldc 183
Cdd:PRK07201  467 STDRFhdYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKAALDAFSDvaaSETLSD--- 543

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1269612287 184 pGVSATTV-LPFhTSTEMFQGMRVRfpNLFPPLKPETVARRTVDA 227
Cdd:PRK07201  544 -GITFTTIhMPL-VRTPMIAPTKRY--NNVPTISPEEAADMVVRA 584
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 22-225 1.34e-15

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: 74.18  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGigrhLAREFAERGARK---IVLWGRTEKCLKETTEEI-RQMGTECHYFICDVGNREEVYQMAKAVREKVgDITILVNN 97
Cdd:cd05356    11 DG----IGKAYAEELAKRgfnVILISRTQEKLDAVAKEIeEKYGVETKTIAADFSAGDDIYERIEKELEGL-DIGILVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  98 AAVVH--GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIP-GAIdYCTSKasafAFME 174
Cdd:cd05356    86 VGISHsiPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPlLAT-YSASK----AFLD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 175 SLTLGL---LDCPGVSATTVLPFHTSTEMFQgmrVRFPNLFPPlKPETVARRTV 225
Cdd:cd05356   161 FFSRALyeeYKSQGIDVQSLLPYLVATKMSK---IRKSSLFVP-SPEQFVRSAL 210
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 29-200 1.96e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 73.68  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIrqMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK12828   24 AAWLAARGAR-VALIGRGAAPLSQTLPGV--PADALRIGGIDLVDPQAARRAVDEVNRQFGRLDALVNIAGAFVWGTIAD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSA 188
Cdd:PRK12828  101 GDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEALAAELLD-RGITV 179

                         170
                  ....*....|..
gi 1269612287 189 TTVLPFHTSTEM 200
Cdd:PRK12828  180 NAVLPSIIDTPP 191
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 29-178 5.64e-15

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: 72.42  E-value: 5.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd05358    20 AIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDILVNNAGLQGDASSHE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLElQN--GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTL 178
Cdd:cd05358   100 MTLEDWNKVIDVNLTGQFLCAREAIKRFRK-SKikGKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQ 170
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 9-167 6.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 72.38  E-value: 6.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRtekclKETTEEI--RQMGTECHYFICDVGNREEVYQMAKAVRE 86
Cdd:PRK06841   12 DLSGKVAVVTGGASGIGHAIAELFAAKGAR-VALLDR-----SEDVAEVaaQLLGGNAKGLVCDVSDSQSVEAAVAAVIS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  87 KVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK06841   86 AFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASK 165


                  .
gi 1269612287 167 A 167
Cdd:PRK06841  166 A 166
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 22-223 6.87e-15

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: 72.32  E-value: 6.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIV-LWGRTEKCLKETTEEIRQmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:cd05367     9 RGIGRALAEELLKRGSPSVVvLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAGS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 V-HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRM-LELQNGHIVCLNSVLALSAIPGAIDYCTSKAS------AFAF 172
Cdd:cd05367    88 LgPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAArdmffrVLAA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 173 ME------SLTLGLLDCP-GVSATTVLPFHTSTEMFQGMRvrfpNLFPPLKPETVARR 223
Cdd:cd05367   168 EEpdvrvlSYAPGVVDTDmQREIRETSADPETRSRFRSLK----EKGELLDPEQSAEK 221
PRK05866 PRK05866
SDR family oxidoreductase;
29-229 9.01e-15

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 72.47  E-value: 9.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK05866   57 AEQFARRGATVVAV-ARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDD---DAlLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNS--VLAlSAIPGAIDYCTSKASAFAFMESLTLGLLDc 183
Cdd:PRK05866  136 SLDrwhDV-ERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgVLS-EASPLFSVYNASKAALSAVSRVIETEWGD- 212

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 184 PGVSATTV------LPFHTSTEMFQGMrvrfpnlfPPLKPETVARRTVDAVQ 229
Cdd:PRK05866  213 RGVHSTTLyyplvaTPMIAPTKAYDGL--------PALTADEAAEWMVTAAR 256
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 21-222 1.35e-14

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: 71.56  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGArKIVLWGRTEK--CLKETTEEIRqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:cd05323     9 ASGIGLATAKLLLKKGA-KVAILDRNENpgAAAELQAINP--KVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDILINNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLmdsDDDALLKSQHVNTL-----GQFWTTKAFLPRMLELQ---NGHIVCLNSVLALSAIPGAIDYCTSKASAF 170
Cdd:cd05323    86 GILDEKSY---LFAGKLPPPWEKTIdvnltGVINTTYLALHYMDKNKggkGGVIVNIGSVAGLYPAPQFPVYSASKHGVV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 171 AFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLK---PETVAR 222
Cdd:cd05323   163 GFTRSLADLLEYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPtqsPEVVAK 217
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 22-232 2.11e-14

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: 70.96  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLwGRTEKCLKETTEEIRQMgtecHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:COG3967    15 SGIGLALAKRLHARGNTVIIT-GRREEKLEEAAAANPGL----HTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDD-ALLKSQ-HVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLG 179
Cdd:COG3967    90 RAEDLLDEAEDlADAEREiTTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSLRHQ 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 180 LLDCPgVSATTVLPFHTSTEMFQGMRVRfPNLFPplkPETVARRTVDAVQQNQ 232
Cdd:COG3967   170 LKDTS-VKVIELAPPAVDTDLTGGQGGD-PRAMP---LDEFADEVMAGLETGK 217
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 28-221 2.93e-14

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


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 70.50  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVlwgrTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVH-GKSL 106
Cdd:cd05345    21 IARRFAQEGARVVI----ADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVNNAGITHrNKPM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLD---- 182
Cdd:cd05345    97 LEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTATKAMAVELAPrnir 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 183 ----CPGVSATTVLpfhtstEMFQG-----MRVRFPNLFPP---LKPETVA 221
Cdd:cd05345   177 vnclCPVAGETPLL------SMFMGedtpeNRAKFRATIPLgrlSTPDDIA 221
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 28-176 4.36e-14

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: 69.91  E-value: 4.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL- 106
Cdd:cd05365    15 IAGTLAKAGASVVIADLKSEGA-EAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNNAGGGGPKPFd 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:cd05365    94 MPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTRNL 163
PRK08589 PRK08589
SDR family oxidoreductase;
29-155 5.54e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 70.19  E-value: 5.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkiVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVH-GKSLM 107
Cdd:PRK08589   23 AIALAQEGAY--VLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVLFNNAGVDNaAGRIH 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSA 155
Cdd:PRK08589  101 EYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAA 147
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-222 5.85e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 69.60  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK08217   21 MAEYLAQKGA-KLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAGILRDGLLV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLK----SQ-----HVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVlALSAIPGAIDYCTSKAsAFAFMESLT 177
Cdd:PRK08217  100 KAKDGKVTSkmslEQfqsviDVNLTGVFLCGREAAAKMIESgSKGVIINISSI-ARAGNMGQTNYSASKA-GVAAMTVTW 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1269612287 178 LGLLDCPGVSATTVLPFHTSTEMFQGMrvrfpnlfpplKPETVAR 222
Cdd:PRK08217  178 AKELARYGIRVAAIAPGVIETEMTAAM-----------KPEALER 211
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 29-203 6.86e-14

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: 69.33  E-value: 6.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:cd05341    22 ARLLVAEGA-KVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVNNAGILTGGTVET 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL-LDCPGVS 187
Cdd:cd05341    98 TTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSAALECaTQGYGIR 177

                         170
                  ....*....|....*.
gi 1269612287 188 ATTVLPFHTSTEMFQG 203
Cdd:cd05341   178 VNSVHPGYIYTPMTDE 193
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 28-230 7.11e-14

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: 69.46  E-value: 7.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFI-CDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:cd05343    22 VARALVQHGM-KVVGCARRVDKIEALAAECQSAGYPTLFPYqCDLSNEEQILSMFSAIRTQHQGVDVCINNAGLARPEPL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLE--LQNGHIVCLNSVLALSAIPGAID--YCTSKASAFAFMESLTLGLLD 182
Cdd:cd05343   101 LSGKTEGWKEMFDVNVLALSICTREAYQSMKErnVDDGHIININSMSGHRVPPVSVFhfYAATKHAVTALTEGLRQELRE 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 183 CP-GVSATTVLPFHTSTEMFQGMRVRFPNL-------FPPLKPETVARRTVDAVQQ 230
Cdd:cd05343   181 AKtHIRATSISPGLVETEFAFKLHDNDPEKaaatyesIPCLKPEDVANAVLYVLST 236
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-167 7.73e-14

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 69.54  E-value: 7.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK08277   25 AMAKELARAGA-KVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCDILINGAGGNHPKAT 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 107 MDSDDDALLKS------------QHV---NTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSA---IPGaidYCTSKA 167
Cdd:PRK08277  104 TDNEFHELIEPtktffdldeegfEFVfdlNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPltkVPA---YSAAKA 179
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 28-205 9.66e-14

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: 69.10  E-value: 9.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd08945    19 IARRLGKEGLRVFVC-ARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLVNNAGRSGGGATA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPR--MLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCpG 185
Cdd:cd08945    98 ELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELART-G 176

                         170       180
                  ....*....|....*....|
gi 1269612287 186 VSATTVLPFHTSTEMFQGMR 205
Cdd:cd08945   177 ITVNAVCPGFVETPMAASVR 196
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 68-171 1.38e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 69.17  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  68 ICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCL 147
Cdd:PRK06180   56 LLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNI 135

                          90       100
                  ....*....|....*....|....
gi 1269612287 148 NSVLALSAIPGAIDYCTSKasaFA 171
Cdd:PRK06180  136 TSMGGLITMPGIGYYCGSK---FA 156
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-202 1.51e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 70.26  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwgrtEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV--HGKS 105
Cdd:PRK06484   21 ACQRFARAGDQVVVA----DRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGVTdpTMTA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 106 LMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGH-IVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcP 184
Cdd:PRK06484   97 TLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAA-K 175

                         170
                  ....*....|....*...
gi 1269612287 185 GVSATTVLPFHTSTEMFQ 202
Cdd:PRK06484  176 GIRVNAVLPGYVRTQMVA 193
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 28-166 1.58e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 68.77  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK13394   23 IALELARAGA-AVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDILVSNAGIQIVNPIE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQN-GHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK13394  102 NYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEASPLKSAYVTAK 161
PRK06138 PRK06138
SDR family oxidoreductase;
22-166 1.80e-13

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 68.25  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK06138   15 SGIGRATAKLFAREGAR-VVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAARWGRLDVLVNNAGFG 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 102 HGKSLMDSDD---DALLKsqhVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK06138   93 CGGTVVTTDEadwDAVMR---VNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASK 157
PRK06139 PRK06139
SDR family oxidoreductase;
29-225 2.26e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 68.98  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK06139   24 AEAFARRGAR-LVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRIDVWVNNVGVGAVGRFEE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSA 188
Cdd:PRK06139  103 TPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFSEALRGELADHPDIHV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1269612287 189 TTVLPFHTSTEMFQ------GMRVRFPnlfPP-LKPETVARRTV 225
Cdd:PRK06139  183 CDVYPAFMDTPGFRhganytGRRLTPP---PPvYDPRRVAKAVV 223
PRK12743 PRK12743
SDR family oxidoreductase;
22-200 2.41e-13

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 68.14  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK12743   12 SGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDVLVNNAGAM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK12743   92 TKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALEL 171

                         170       180
                  ....*....|....*....|
gi 1269612287 181 LDcPGVSATTVLPFHTSTEM 200
Cdd:PRK12743  172 VE-HGILVNAVAPGAIATPM 190
PRK09072 PRK09072
SDR family oxidoreductase;
9-262 2.48e-13

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 68.04  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGtECHYFICDVGNREEVYQMAKAVREkV 88
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGAR-LLLVGRNAEKLEALAARLPYPG-RHRWVVADLTSEAGREAVLARARE-M 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKAS 168
Cdd:PRK09072   79 GGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 169 AFAFMESLTLGLLDCPgVSATTVLPFHTST--------EMFQGMRVRFPNlfpplkPETVARRTVDAVQQNQALLLLPWT 240
Cdd:PRK09072  159 LRGFSEALRRELADTG-VRVLYLAPRATRTamnseavqALNRALGNAMDD------PEDVAAAVLQAIEKERAERWLGWP 231

                         250       260
                  ....*....|....*....|....*....
gi 1269612287 241 MNILIILKSILPQAA-------LEEIHRF 262
Cdd:PRK09072  232 EKLFVRLNGLLPSLVdralrkqLPVIHRF 260
PRK06172 PRK06172
SDR family oxidoreductase;
29-202 2.56e-13

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 67.85  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKS-LM 107
Cdd:PRK06172   24 ALAFAREGA-KVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDYAFNNAGIEIEQGrLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVS 187
Cdd:PRK06172  103 EGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAK-KGIR 181

                         170
                  ....*....|....*
gi 1269612287 188 ATTVLPFHTSTEMFQ 202
Cdd:PRK06172  182 VNAVCPAVIDTDMFR 196
PRK07454 PRK07454
SDR family oxidoreductase;
29-176 3.62e-13

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 67.29  E-value: 3.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK07454   23 ALAFAKAGW-DLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGMAYTGPLLE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK07454  102 MPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCL 169
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 10-221 4.03e-13

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: 67.44  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  10 LSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFIC---DVGNREEVYQMAKAVRE 86
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGAR-LALTGRDAERLEETRQSCLQAGVSEKKILLvvaDLTEEEGQDRIISTTLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  87 KVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQnGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:cd05364    80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 167 ASAFAFMESLTLGLLD--------CPGVSATTV-----LPFHTSTEMFQGMRVRFPnLFPPLKPETVA 221
Cdd:cd05364   159 AALDQFTRCTALELAPkgvrvnsvSPGVIVTGFhrrmgMPEEQYIKFLSRAKETHP-LGRPGTVDEVA 225
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 22-200 4.64e-13

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 67.34  E-value: 4.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK12935   16 KGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDILVNNAGIT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL 181
Cdd:PRK12935   96 RDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELA 175

                         170
                  ....*....|....*....
gi 1269612287 182 DCpGVSATTVLPFHTSTEM 200
Cdd:PRK12935  176 KT-NVTVNAICPGFIDTEM 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 28-201 4.73e-13

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 67.07  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK12937   21 IARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTIA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMleLQNGHIVCLN-SVLALSaIPGAIDYCTSKASafafMESLTLGL---LDC 183
Cdd:PRK12937  101 DFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLStSVIALP-LPGYGPYAASKAA----VEGLVHVLaneLRG 173

                         170
                  ....*....|....*...
gi 1269612287 184 PGVSATTVLPFHTSTEMF 201
Cdd:PRK12937  174 RGITVNAVAPGPVATELF 191
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
29-178 5.54e-13

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 68.72  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHyFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK08324  439 AKRLAAEGAC-VVLADLDEEAAEAAAAELGGPDRALG-VACDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEE 516

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTK-AFlpRMLELQN--GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTL 178
Cdd:PRK08324  517 TSDEDWRRSFDVNATGHFLVAReAV--RIMKAQGlgGSIVFIASKNAVNPGPNFGAYGAAKAAELHLVRQLAL 587
PRK07831 PRK07831
SDR family oxidoreductase;
29-172 6.15e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 66.98  E-value: 6.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIR-QMGTE-CHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK07831   35 ARRALEEGAR-VVISDIHERRLGETADELAaELGLGrVEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQTPV 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKASAFAF 172
Cdd:PRK07831  114 VDMTDDEWSRVLDVTLTGTFRATRAALRYMRARgHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMAL 180
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 11-190 6.70e-13

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: 66.63  E-value: 6.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  11 SRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGD 90
Cdd:cd05366     1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  91 ITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCTSKASA 169
Cdd:cd05366    81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAV 160

                         170       180
                  ....*....|....*....|....*....
gi 1269612287 170 FAFMESLTLGLLD--------CPGVSATT 190
Cdd:cd05366   161 RGLTQTAAQELAPkgitvnayAPGIVKTE 189
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 7-217 8.44e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 66.62  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLwGRTEKCLKETTEEIRQMgtECHYFICDVGNREEVYQMAKAVRE 86
Cdd:PRK12829    6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVC-DVSEAALAATAARLPGA--KVTATVADVADPAQVERVFDTAVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  87 KVGDITILVNNAAVV-HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVC-LNSVLALSAIPGAIDYCT 164
Cdd:PRK12829   83 RFGGLDVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIaLSSVAGRLGYPGRTPYAA 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 165 SKASAFAFMESLTLGLLDcPGVSATTVLPFHTSTEMFQG-MRVRFPNLFPPLKP 217
Cdd:PRK12829  163 SKWAVVGLVKSLAIELGP-LGIRVNAILPGIVRGPRMRRvIEARAQQLGIGLDE 215
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 22-189 9.48e-13

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: 66.33  E-value: 9.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA--A 99
Cdd:cd05337    11 RGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLVNNAgiA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 100 VVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQN------GHIVCLNSVLALSAIPGAIDYCTSKASAFAFM 173
Cdd:cd05337    91 VRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRGEYCISKAGLSMAT 170

                         170       180
                  ....*....|....*....|....
gi 1269612287 174 ESLTLGLLD--------CPGVSAT 189
Cdd:cd05337   171 RLLAYRLADegiavheiRPGLIHT 194
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 28-145 9.55e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 66.62  E-value: 9.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK07097   26 IAKAYAKAGA-TIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDILVNNAGIIKRIPML 104

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:PRK07097  105 EMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKII 142
PRK06398 PRK06398
aldose dehydrogenase; Validated
 66-193 1.13e-12

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 66.01  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  66 YFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:PRK06398   48 YFKVDVSNKEQVIKGIDYVISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVII 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1269612287 146 CLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLldCPGVSATTVLP 193
Cdd:PRK06398  128 NIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDY--APTIRCVAVCP 173
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 28-180 1.35e-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: 66.03  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-VHGKSL 106
Cdd:cd08936    26 IARRLAQDGAH-VVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILVSNAAVnPFFGNI 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:cd08936   105 LDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPEL 178
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 29-202 1.56e-12

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: 65.59  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVlwgrTEKCLKETTEEIRQMGteCHYFIC--DVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKS- 105
Cdd:cd08944    20 AARLAREGARVVV----ADIDGGAAQAVVAQIA--GGALALrvDVTDEQQVAALFERAVEEFGGLDLLVNNAGAMHLTPa 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 106 LMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLTLGL---LD 182
Cdd:cd08944    94 IIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA----IRNLTRTLaaeLR 169

                         170       180
                  ....*....|....*....|
gi 1269612287 183 CPGVSATTVLPFHTSTEMFQ 202
Cdd:cd08944   170 HAGIRCNALAPGLIDTPLLL 189
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 22-199 2.23e-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: 65.39  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGAR-KIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:cd05355    36 SGIGRAVAIAFAREGADvAINYLPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAY 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VH-GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLG 179
Cdd:cd05355   116 QHpQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQ 193

                         170       180
                  ....*....|....*....|....*...
gi 1269612287 180 LLD--------CPGVSATTVLPFHTSTE 199
Cdd:cd05355   194 LAEkgirvnavAPGPIWTPLIPSSFPEE 221
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 22-187 2.34e-12

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: 63.74  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCL---KETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:pfam08659  10 GGLGRELARWLAERGARHLVLLSRSAAPRpdaQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVIHAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqngHIVCLNSVLALSAIPGAIDYCTskASAF--AFMESL 176
Cdd:pfam08659  90 GVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLD----FFVLFSSIAGLLGSPGQANYAA--ANAFldALAEYR 163

                         170
                  ....*....|..
gi 1269612287 177 -TLGLldcPGVS 187
Cdd:pfam08659 164 rSQGL---PATS 172
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-222 2.95e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 64.98  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA--AVVHGKSL 106
Cdd:PRK12745   19 ARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCLVNNAgvGVKVRGDL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGH------IVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK12745   99 LDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 181 ldCP-GVSATTVLPFHTSTEMFQGMRVRFPNLFP----PLK----PETVAR 222
Cdd:PRK12745  179 --AEeGIGVYEVRPGLIKTDMTAPVTAKYDALIAkglvPMPrwgePEDVAR 227
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 29-221 3.67e-12

(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: 64.65  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIV--------LWGRTEKCLKETTEEIRQMGTEChyfICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:cd05353    22 ALAFAERGAKVVVndlggdrkGSGKSSSAADKVVDEIKAAGGKA---VANYDSVEDGEKIVKTAIDAFGRVDILVNNAGI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:cd05353    99 LRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEG 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 181 LDCpGVSATTVLPfHTSTEMFQG-MRvrfPNLFPPLKPETVA 221
Cdd:cd05353   179 AKY-NITCNTIAP-AAGSRMTETvMP---EDLFDALKPEYVA 215
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-209 3.99e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 64.42  E-value: 3.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  30 REFAERGAR----------KIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA 99
Cdd:PRK12859   26 KELAEAGADifftywtaydKEMPWGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 100 vvHGKSLMDSDDDALLKSQH--VNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLT 177
Cdd:PRK12859  106 --YSTNNDFSNLTAEELDKHymVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLA 183

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1269612287 178 LGLLDCpGVSATTVLPFHTST-----EMFQGMRVRFP 209
Cdd:PRK12859  184 AEVAHL-GITVNAINPGPTDTgwmteEIKQGLLPMFP 219
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 21-223 4.01e-12

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: 64.24  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARKIVLWGRTEKCLKEtTEEIRQMGTECHYFICDVGNreEVYQMAKAVREKVGD--ITILVNNA 98
Cdd:cd05325     7 SRGIGLELVRQLLARGNNTVIATCRDPSAATE-LAALGASHSRLHILELDVTD--EIAESAEAVAERLGDagLDVLINNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLMDS-DDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVClnsvlaLSAIPGAID---------YCTSKAS 168
Cdd:cd05325    84 GILHSYGPASEvDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIIN------ISSRVGSIGdntsggwysYRASKAA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 169 AFAFMESLTLGLLDcPGVSATTVLPFHTSTEMFQGmrvrFPNLFPPLKPETVARR 223
Cdd:cd05325   158 LNMLTKSLAVELKR-DGITVVSLHPGWVRTDMGGP----FAKNKGPITPEESVAG 207
PRK07074 PRK07074
SDR family oxidoreductase;
28-237 4.44e-12

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 64.41  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETteeIRQMGTEchYF---ICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK 104
Cdd:PRK07074   18 LARRFLAAGDR-VLALDIDAAALAAF---ADALGDA--RFvpvACDLTDAASLAAALANAAAERGPVDVLVANAGAARAA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIpGAIDYCTSKASAFAFMESLT--LGLLd 182
Cdd:PRK07074   92 SLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAAL-GHPAYSAAKAGLIHYTKLLAveYGRF- 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 183 cpGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLL 237
Cdd:PRK07074  170 --GIRANAVAPGTVKTQAWEARVAANPQVFEELKKWYPLQDFATPDDVANAVLFL 222
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 28-166 6.12e-12

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: 64.01  E-value: 6.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVL--WGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKS 105
Cdd:cd08940    18 IARALAAAGA-NIVLngFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQHVAP 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 106 LMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:cd08940    97 IEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 27-99 7.72e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 63.54  E-value: 7.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287  27 HLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA 99
Cdd:PRK07677   16 AMAKRFAEEGAN-VVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAA 87
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 59-176 8.60e-12

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 63.40  E-value: 8.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  59 QMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK---SLMDSDDDALLKsqhVNTLGQFWTTKAFLPR 135
Cdd:PRK12936   49 ELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGITKDGlfvRMSDEDWDSVLE---VNLTATFRLTRELTHP 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1269612287 136 MLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK12936  126 MMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSL 166
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 9-185 9.34e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 63.49  E-value: 9.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKV 88
Cdd:PRK06198    3 RLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDalLKSQH--VNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCTS 165
Cdd:PRK06198   83 GRLDALVNAAGLTDRGTILDTSPE--LFDRHfaVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYCAS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1269612287 166 KA--------SAFAFM------ESLTLGLLDCPG 185
Cdd:PRK06198  161 KGalatltrnAAYALLrnrirvNGLNIGWMATEG 194
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 65-175 9.48e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 63.49  E-value: 9.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  65 HYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDS---------DDDALLKSQHVNTLGQFWTTKAFLPR 135
Cdd:PRK06171   52 QFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINIPRLLVDEkdpagkyelNEAAFDKMFNINQKGVFLMSQAVARQ 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1269612287 136 MLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMES 175
Cdd:PRK06171  132 MVKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRS 171
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 28-177 9.83e-12

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: 63.17  E-value: 9.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd05373    15 IARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPIL 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLT 177
Cdd:cd05373    95 ETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMA 164
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 28-166 1.42e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 62.86  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK07523   26 LAEGLAQAGA-EVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK07523  105 DFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATK 163
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-176 2.08e-11

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: 62.86  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVH---- 102
Cdd:cd08935    20 AMARALAQAGAKVAAL-GRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDILINGAGGNHpdat 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 103 ----------GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAF 172
Cdd:cd08935    99 tdpehyepetEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNF 178


                  ....
gi 1269612287 173 MESL 176
Cdd:cd08935   179 TQWL 182
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 37-213 3.67e-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: 61.71  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  37 ARKIVLWGRTEKCLKETTEeIRQMgtechyficDVGNREEVYQMAKAVREkvGDITILVNNAAVVHGKSLMDSDDDALLK 116
Cdd:cd09806    38 KKKGRLWEAAGALAGGTLE-TLQL---------DVCDSKSVAAAVERVTE--RHVDVLVCNAGVGLLGPLEALSEDAMAS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 117 SQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCpGVSATTVL--PF 194
Cdd:cd09806   106 VFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEGLCESLAVQLLPF-NVHLSLIEcgPV 184

                         170       180
                  ....*....|....*....|..
gi 1269612287 195 HTSTE---MFQGMRVRFPNLFP 213
Cdd:cd09806   185 HTAFMekvLGSPEEVLDRTADD 206
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-204 6.07e-11

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 61.28  E-value: 6.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK06077   22 IAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVADILVNNAGLGLFSPFL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLldCPGVS 187
Cdd:PRK06077  102 NVDDKLIDKHISTDFKSVIYCSQELAKEMRE--GGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLALEL--APKIR 177

                         170
                  ....*....|....*..
gi 1269612287 188 ATTVLPFHTSTEMFQGM 204
Cdd:PRK06077  178 VNAIAPGFVKTKLGESL 194
PRK08219 PRK08219
SDR family oxidoreductase;
22-229 6.38e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 60.72  E-value: 6.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERgaRKIVLWGRTEKCLKETTEEIRQMGTechyFICDVGNREEvyqMAKAVrEKVGDITILVNNAAVV 101
Cdd:PRK08219   13 RGIGAAIARELAPT--HTLLLGGRPAERLDELAAELPGATP----FPVDLTDPEA---IAAAV-EQLGRLDVLVHNAGVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRmLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGll 181
Cdd:PRK08219   83 DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPA-LRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADALREE-- 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 182 DCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPP---LKPETVARRTVDAVQ 229
Cdd:PRK08219  160 EPGNVRVTSVHPGRTDTDMQRGLVAQEGGEYDPeryLRPETVAKAVRFAVD 210
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 9-204 7.72e-11

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 60.67  E-value: 7.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARKIVLwgrtekclkeTTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKV 88
Cdd:PRK08220    5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGF----------DQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKAS 168
Cdd:PRK08220   75 GPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAA 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1269612287 169 AFAFmeSLTLGL-LDCPGVSATTVLPFHTSTEMFQGM 204
Cdd:PRK08220  155 LTSL--AKCVGLeLAPYGVRCNVVSPGSTDTDMQRTL 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 9-200 8.42e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 60.50  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEirqmgTECHYFICDVGNREEvyqmAKAVREKV 88
Cdd:PRK07060    6 DFSGKSVLVTGASSGIGRACAVALAQRGAR-VVAAARNAAALDRLAGE-----TGCEPLRLDVGDDAA----IRAALAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCTSKA 167
Cdd:PRK07060   76 GAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGrGGSIVNVSSQAALVGLPDHLAYCASKA 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1269612287 168 SAFAFMESLTLGLldCP-GVSATTVLPFHTSTEM 200
Cdd:PRK07060  156 ALDAITRVLCVEL--GPhGIRVNSVNPTVTLTPM 187
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 28-229 9.16e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 60.82  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAE----RGARkIVLWGRTEKCLKETTEeirQMGTECHYFICDVGNREEVYQ-MAKAVrEKVGDITILVNNAAVVH 102
Cdd:PRK08263   15 FGRAWTEaaleRGDR-VVATARDTATLADLAE---KYGDRLLPLALDVTDRAAVFAaVETAV-EHFGRLDIVVNNAGYGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 103 GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLD 182
Cdd:PRK08263   90 FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQEVAE 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1269612287 183 CpGVSATTVLPFHTSTEMFQ-GMRVRFPN-LFPPLKPETVARRTVDAVQ 229
Cdd:PRK08263  170 F-GIKVTLVEPGGYSTDWAGtSAKRATPLdAYDTLREELAEQWSERSVD 217
PRK07326 PRK07326
SDR family oxidoreductase;
22-231 1.51e-10

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 59.64  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGtECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK07326   16 KGIGFAIAEALLAEGY-KVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGGLDVLIANAGVG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL 181
Cdd:PRK07326   94 HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKR-GGGYIINISSLAGTNFFAGGAAYNASKFGLVGFSEAAMLDLR 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 182 DcPGVSATTVLPFHTSTEmfqgmrvrFPNLFPP------LKPETVARRTVDAVQQN 231
Cdd:PRK07326  173 Q-YGIKVSTIMPGSVATH--------FNGHTPSekdawkIQPEDIAQLVLDLLKMP 219
PRK06124 PRK06124
SDR family oxidoreductase;
28-224 1.64e-10

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 60.11  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK06124   27 IARALAGAGAHVLVN-GRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLT--LGLLdcpG 185
Cdd:PRK06124  106 ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLMRALAaeFGPH---G 182

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1269612287 186 VSATTVLPFHTSTEMFQGMrVRFPNLFPPLkpetvARRT 224
Cdd:PRK06124  183 ITSNAIAPGYFATETNAAM-AADPAVGPWL-----AQRT 215
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 21-200 2.13e-10

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: 59.17  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:cd05324     9 NRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDILVNNAGI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VhgkslMDSDDDALLKSQ------HVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPgaidYCTSKASAFAFME 174
Cdd:cd05324    89 A-----FKGFDDSTPTREqaretmKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSKAALNALTR 159

                         170       180
                  ....*....|....*....|....*.
gi 1269612287 175 SLTLGLLDcPGVSATTVLPFHTSTEM 200
Cdd:cd05324   160 ILAKELKE-TGIKVNACCPGWVKTDM 184
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
22-205 2.16e-10

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 59.39  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK12824   12 RGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDILVNNAGIT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLL 181
Cdd:PRK12824   92 RDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFTKALASEGA 171

                         170       180
                  ....*....|....*....|....
gi 1269612287 182 DcPGVSATTVLPFHTSTEMFQGMR 205
Cdd:PRK12824  172 R-YGITVNCIAPGYIATPMVEQMG 194
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-228 3.41e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 58.89  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRTEKClKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK07067   21 AVAERYLAEGARVVIADIKPARA-RLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAALFDMAPI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPG 185
Cdd:PRK07067   97 LDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIR-HG 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1269612287 186 VSATTVLPFHTSTEMFQGMRVRFPNlFPPLKPETVARRTVDAV 228
Cdd:PRK07067  176 INVNAIAPGVVDTPMWDQVDALFAR-YENRPPGEKKRLVGEAV 217
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-190 4.58e-10

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 58.56  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   8 RDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREK 87
Cdd:PRK08642    1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  88 VG-DITILVNNAAV------VHGKSLMDSDDDALLKsQHVNTL-GQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGA 159
Cdd:PRK08642   78 FGkPITTVVNNALAdfsfdgDARKKADDITWEDFQQ-QLEGSVkGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1269612287 160 IDYCTSKASAFAFMESL--------------TLGLLDCPGVSATT 190
Cdd:PRK08642  157 HDYTTAKAALLGLTRNLaaelgpygitvnmvSGGLLRTTDASAAT 201
PRK05867 PRK05867
SDR family oxidoreductase;
7-202 7.02e-10

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 58.12  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVRE 86
Cdd:PRK05867    4 LFDLHGKRALITGASTGIGKRVALAYVEAGAQ-VAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  87 KVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLA--LSAIPGAID-YC 163
Cdd:PRK05867   83 ELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSghIINVPQQVShYC 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1269612287 164 TSKASAFAFMESLTLGLldCP-GVSATTVLPFHTSTEMFQ 202
Cdd:PRK05867  163 ASKAAVIHLTKAMAVEL--APhKIRVNSVSPGYILTELVE 200
PRK07063 PRK07063
SDR family oxidoreductase;
21-166 7.58e-10

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 58.14  E-value: 7.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGT--ECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:PRK07063   16 AQGIGAAIARAFAREGAA-VALADLDAALAERAAAAIARDVAgaRVLAVPADVTDAASVAAAVAAAEEAFGPLDVLVNNA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287  99 AV-VHGKSLMDSDDDaLLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK07063   95 GInVFADPLAMTDED-WRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAK 162
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 28-229 8.69e-10

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: 57.15  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTechyfICDVGNREEVYqmakAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd11730    14 LARALAGRGWR-LLLSGRDAGALAGLAAEVGALAR-----PADVAAELEVW----ALAQELGPLDLLVYAAGAILGKPLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTlglLDCPGVS 187
Cdd:cd11730    84 RTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVAR---KEVRGLR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 188 ATTVLPFHTSTEMFQgMRVRFPNlfPPLKPETVARRTVDAVQ 229
Cdd:cd11730   159 LTLVRPPAVDTGLWA-PPGRLPK--GALSPEDVAAAILEAHQ 197
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 22-176 9.40e-10

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: 58.53  E-value: 9.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKE-----TTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVN 96
Cdd:cd08953   215 GGIGRALARALARRYGARLVLLGRSPLPPEEewkaqTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIH 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  97 NAAVVHGKSLMDSDDDALL-----KSQHVNTLGQfwttkAFLPRMLELqnghIVCLNSVLALSAIPGAIDYctskASAFA 171
Cdd:cd08953   295 AAGVLRDALLAQKTAEDFEavlapKVDGLLNLAQ-----ALADEPLDF----FVLFSSVSAFFGGAGQADY----AAANA 361


                  ....*
gi 1269612287 172 FMESL 176
Cdd:cd08953   362 FLDAF 366
PRK07035 PRK07035
SDR family oxidoreductase;
7-171 1.30e-09

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 57.33  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVRE 86
Cdd:PRK07035    3 LFDLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGC-QAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  87 KVGDITILVNNAAV--VHGkSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSaiPGAID--Y 162
Cdd:PRK07035   82 RHGRLDILVNNAAAnpYFG-HILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVS--PGDFQgiY 158

                         170
                  ....*....|....*
gi 1269612287 163 CTSKAS------AFA 171
Cdd:PRK07035  159 SITKAAvismtkAFA 173
PRK06947 PRK06947
SDR family oxidoreductase;
12-200 1.46e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 57.12  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  12 RESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDI 91
Cdd:PRK06947    2 RKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  92 TILVNNAAVVH-GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGH---IVCLNSVLALSAIPGA-IDYCTSK 166
Cdd:PRK06947   82 DALVNNAGIVApSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEyVDYAGSK 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1269612287 167 ASafafMESLTLGL---LDCPGVSATTVLPFHTSTEM 200
Cdd:PRK06947  162 GA----VDTLTLGLakeLGPHGVRVNAVRPGLIETEI 194
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 55-156 1.49e-09

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: 57.07  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  55 EEIRQMGTECHYFICDVgnREEVyQMAKAVR---EKVGDITILVNNAAVVhgkSLMDSDDDALLK---SQHVNTLGQFWT 128
Cdd:cd09762    52 EEIEAAGGKALPCIVDI--RDED-QVRAAVEkavEKFGGIDILVNNASAI---SLTGTLDTPMKRydlMMGVNTRGTYLC 125

                          90       100
                  ....*....|....*....|....*...
gi 1269612287 129 TKAFLPRMLELQNGHIVCLNSVLALSAI 156
Cdd:cd09762   126 SKACLPYLKKSKNPHILNLSPPLNLNPK 153
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-209 1.53e-09

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 57.01  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGAR----------KIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:PRK12748   24 CRRLAAKGIDifftywspydKTMPWGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYAPNRVFYAVSERLGDPSILINNA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTL 178
Cdd:PRK12748  104 AYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAP 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1269612287 179 GLLDcPGVSATTVLPFHTST-----EMFQGMRVRFP 209
Cdd:PRK12748  184 ELAE-KGITVNAVNPGPTDTgwiteELKHHLVPKFP 218
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 28-226 1.59e-09

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: 57.15  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARkIVLWGRTEKCLkETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA-VVHGKSL 106
Cdd:cd08937    20 VAERLAGEGAR-VLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVLINNVGgTIWAKPY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVlalsAIPGA--IDYCTSKASAFAFMESLTLGLLDcP 184
Cdd:cd08937    98 EHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI----ATRGIyrIPYSAAKGGVNALTASLAFEHAR-D 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1269612287 185 GVSATTVLPFHTSTEmfqgMRVRFPNLFPPLKPETV-ARRTVD 226
Cdd:cd08937   173 GIRVNAVAPGGTEAP----PRKIPRNAAPMSEQEKVwYQRIVD 211
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-166 1.68e-09

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 56.89  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLwgrtekclkeTTEEIRQMGTECHYFICDVGNREEvyqmakAVREKVGDITILVNNAAVVHG-KSLM 107
Cdd:PRK06550   22 ARAFLAQGAQVYGV----------DKQDKPDLSGNFHFLQLDLSDDLE------PLFDWVPSVDILCNTAGILDDyKPLL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:PRK06550   86 DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASK 144
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 15-200 1.72e-09

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 57.04  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGARKIVLWG---RTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDI 91
Cdd:PRK12827    9 VLITGGSGGLGRAIAVRLAADGADVIVLDIhpmRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFGRL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  92 TILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKASAF 170
Cdd:PRK12827   89 DILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRArRGGRIVNIASVAGVRGNRGQVNYAASKAGLI 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 1269612287 171 AFMESLTLGLLDcPGVSATTVLPFHTSTEM 200
Cdd:PRK12827  169 GLTKTLANELAP-RGITVNAVAPGAINTPM 197
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 28-180 2.43e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 56.30  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEEirqMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHG---- 103
Cdd:PRK10538   16 ITRRFIQQGH-KVIATGRRQERLQELKDE---LGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGLALGlepa 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 104 -KSLMDsDDDALLKSqhvNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKasafAFMESLTLGL 180
Cdd:PRK10538   92 hKASVE-DWETMIDT---NNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATK----AFVRQFSLNL 161
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 21-167 2.81e-09

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: 56.19  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:cd05352    17 SRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAGI 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGhivclnSVLALSAIPGAI--------DYCTSKA 167
Cdd:cd05352    97 TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKG------SLIITASMSGTIvnrpqpqaAYNASKA 165
PRK07069 PRK07069
short chain dehydrogenase; Validated
 29-208 4.17e-09

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 55.87  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLWGRTEKCLKETTEEIR-QMGTECHY-FICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK07069   16 ARRMAEQGAKVFLTDINDAAGLDAFAAEINaAHGEGVAFaAVQDVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFGAI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTlglLDCP-- 184
Cdd:PRK07069   96 EQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTKSIA---LDCArr 172

                         170       180
                  ....*....|....*....|....*.
gi 1269612287 185 --GVSATTVLPFHTSTEMFQGMRVRF 208
Cdd:PRK07069  173 glDVRCNSIHPTFIRTGIVDPIFQRL 198
PRK08278 PRK08278
SDR family oxidoreductase;
22-180 4.81e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 55.68  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRT-------EKCLKETTEEIRQMGTECHYFICDVGNREEVYQ-MAKAVrEKVGDITI 93
Cdd:PRK08278   16 RGIGLAIALRAARDGAN-IVIAAKTaephpklPGTIHTAAEEIEAAGGQALPLVGDVRDEDQVAAaVAKAV-ERFGGIDI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  94 LVNNAAVVhgkSLMDSDDDALLK---SQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSA--IPGAIDYCTSKAS 168
Cdd:PRK08278   94 CVNNASAI---NLTGTEDTPMKRfdlMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPkwFAPHTAYTMAKYG 170

                         170
                  ....*....|..
gi 1269612287 169 afafMESLTLGL 180
Cdd:PRK08278  171 ----MSLCTLGL 178
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 21-176 8.25e-09

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: 54.03  E-value: 8.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   21 GRGIGRHLAREFAERGARKIVLWGRT---EKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNN 97
Cdd:smart00822   9 LGGLGRALARWLAERGARRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVIHA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   98 AAVVHGKSLMDSDDDALlksQHVntlgqfWTTK---------AFLPRMLElqngHIVCLNSVLALSAIPGAIDYctskAS 168
Cdd:smart00822  89 AGVLDDGVLASLTPERF---AAV------LAPKaagawnlheLTADLPLD----FFVLFSSIAGVLGSPGQANY----AA 151


                   ....*...
gi 1269612287  169 AFAFMESL 176
Cdd:smart00822 152 ANAFLDAL 159
PRK09242 PRK09242
SDR family oxidoreductase;
29-224 8.56e-09

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 54.75  E-value: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQ--MGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSL 106
Cdd:PRK09242   26 AREFLGLGA-DVLIVARDADALAQARDELAEefPEREVHGLAADVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASafafMESLTLGLL---DC 183
Cdd:PRK09242  105 IDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAA----LLQMTRNLAvewAE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1269612287 184 PGVSATTVLPFHTSTEMFQGMrvrfpnLFPPLKPETVARRT 224
Cdd:PRK09242  181 DGIRVNAVAPWYIRTPLTSGP------LSDPDYYEQVIERT 215
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 27-155 8.81e-09

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: 54.65  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFA----ERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-- 100
Cdd:cd08930    13 LIGKAFCkallSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRIDILINNAYPsp 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 101 -VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSA 155
Cdd:cd08930    93 kVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIA 148
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
70-205 1.07e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 54.63  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  70 DVGNREEVYQMAKAVREKVGDITILVNNAAVVHG---KSLMDSDDDALLKSqhvNTLGQFWTTKAFLPRMLELQNGHIVC 146
Cdd:PRK12938   61 NVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDvvfRKMTREDWTAVIDT---NLTSLFNVTKQVIDGMVERGWGRIIN 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 147 LNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLdCPGVSATTVLPFHTSTEMFQGMR 205
Cdd:PRK12938  138 ISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVA-TKGVTVNTVSPGYIGTDMVKAIR 195
PRK07775 PRK07775
SDR family oxidoreductase;
36-204 1.19e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 54.76  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  36 GARkivlwgRTEKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALL 115
Cdd:PRK07775   40 GAR------RVEKC-EELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 116 KSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGlLDCPGVSATTVLPFH 195
Cdd:PRK07775  113 SQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQME-LEGTGVRASIVHPGP 191


                  ....*....
gi 1269612287 196 TSTEMfqGM 204
Cdd:PRK07775  192 TLTGM--GW 198
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 15-176 1.63e-08

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: 54.00  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITIL 94
Cdd:cd05349     3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEA---GERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  95 VNNAAV------VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKAS 168
Cdd:cd05349    80 VNNALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAA 159


                  ....*...
gi 1269612287 169 AFAFMESL 176
Cdd:cd05349   160 LLGFTRNM 167
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 30-178 2.34e-08

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: 53.76  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  30 REFAERGARKI-------VLWGRTEKCLKETTEEIRQM--GTECHYFICDVGNREEVYQMAKAVREKVG----DITILVN 96
Cdd:TIGR01500  14 RTIAQELAKCLkspgsvlVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKALRELPRpkglQRLLLIN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  97 NAAVVH--GKSLMD-SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ--NGHIVCLNSVLALSAIPGAIDYCTSKASAFA 171
Cdd:TIGR01500  94 NAGTLGdvSKGFVDlSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPglNRTVVNISSLCAIQPFKGWALYCAGKAARDM 173


                  ....*..
gi 1269612287 172 FMESLTL 178
Cdd:TIGR01500 174 LFQVLAL 180
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-134 2.51e-08

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: 53.64  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLkETTEEIRQMGtECHYFICDVGNREEVYQMAKAVRE 86
Cdd:cd08942     1 LFSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACA-DAAEELSAYG-ECIAIPADLSSEEGIEALVARVAE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1269612287  87 KVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLP 134
Cdd:cd08942    79 RSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLP 126
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-145 4.72e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 52.74  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIR---QMGTECHyfICDVGNREEVYQMAkavr 85
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCH-LHLVARDADALEALAADLRaahGVDVAVH--ALDLSSPEAREQLA---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  86 EKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:PRK06125   77 AEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV 136
PRK06123 PRK06123
SDR family oxidoreductase;
11-200 4.81e-08

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 52.47  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  11 SRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGD 90
Cdd:PRK06123    1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  91 ITILVNNAAVVHGKSLMDSDDDA-LLKSQHVNTLGQFWTTKAFLPRMLELQNGH---IVCLNSVLALSAIPGA-IDYCTS 165
Cdd:PRK06123   81 LDALVNNAGILEAQMRLEQMDAArLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEyIDYAAS 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1269612287 166 KASafafMESLTLGL---LDCPGVSATTVLPFHTSTEM 200
Cdd:PRK06123  161 KGA----IDTMTIGLakeVAAEGIRVNAVRPGVIYTEI 194
PRK07102 PRK07102
SDR family oxidoreductase;
29-250 4.88e-08

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 52.62  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIRQMG---TECHYF-ICDVGNREEVYQMAKAVRekvgDITIlvnnaaVVHG- 103
Cdd:PRK07102   18 ARRYAAAGAR-LYLAARDVERLERLADDLRARGavaVSTHELdILDTASHAAFLDSLPALP----DIVL------IAVGt 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 104 ---KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK07102   87 lgdQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLRNRL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 181 LDcPGVSATTVLPFHTSTEMFQGMRvrfpnLFPPL--KPETVARRTVDAVQQNQALLLLPWT-MNILIILKSI 250
Cdd:PRK07102  167 FK-SGVHVLTVKPGFVRTPMTAGLK-----LPGPLtaQPEEVAKDIFRAIEKGKDVIYTPWFwRLIMLIIRSI 233
PRK06949 PRK06949
SDR family oxidoreductase;
9-206 4.98e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 52.84  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKV 88
Cdd:PRK06949    6 NLEGKVALVTGASSGLGARFAQVLAQAGA-KVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  89 GDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRML--------ELQNGHIVCLNSVLALSAIPGAI 160
Cdd:PRK06949   85 GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIarakgagnTKPGGRIINIASVAGLRVLPQIG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 161 DYCTSKASAFAFMESLTL-----GL---LDCPGVSATTVLPFHTSTEmfQGMRV 206
Cdd:PRK06949  165 LYCMSKAAVVHMTRAMALewgrhGInvnAICPGYIDTEINHHHWETE--QGQKL 216
PRK06914 PRK06914
SDR family oxidoreductase;
70-181 7.31e-08

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 52.33  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  70 DVGNREEVYQMAKAVREkVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNS 149
Cdd:PRK06914   62 DVTDQNSIHNFQLVLKE-IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISS 140

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1269612287 150 VLALSAIPGAIDYCTSKASAFAFMESLTLGLL 181
Cdd:PRK06914  141 ISGRVGFPGLSPYVSSKYALEGFSESLRLELK 172
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 27-176 8.27e-08

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 52.67  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRT---EKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVhg 103
Cdd:cd08955   164 LVAEWLVERGARHLVLTGRRapsAAA-RQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRGVIHAAGVL-- 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 104 kslmdsdDDALLKSQhvnTLGQFwtTKAFLPRMLELQNGH----------IVCLNSVLALSAIPGAIDYctskASAFAFM 173
Cdd:cd08955   241 -------DDGVLANQ---DWERF--RKVLAPKVQGAWNLHqltqdlpldfFVLFSSVASLLGSPGQANY----AAANAFL 304


                  ...
gi 1269612287 174 ESL 176
Cdd:cd08955   305 DAL 307
PRK06484 PRK06484
short chain dehydrogenase; Validated
 22-222 9.21e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 52.54  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTE--KCLKETteeirqMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA 99
Cdd:PRK06484  279 RGIGRAVADRFAAAGDRLLIIDRDAEgaKKLAEA------LGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAG 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 100 VVHG-KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMleLQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTL 178
Cdd:PRK06484  353 IAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLAC 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 179 GLLD--------CPGVSAT-TVLPFHTSTEM-FQGMRVRFPnLFPPLKPETVAR 222
Cdd:PRK06484  431 EWAPagirvntvAPGYIETpAVLALKASGRAdFDSIRRRIP-LGRLGDPEEVAE 483
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 15-193 1.01e-07

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 51.89  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGARkiVLWGrtekCLKETTEEIRQMGTEC----HYFICDVGNREEVYQMAKAVREKVGD 90
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFT--VLAG----CLTKNGPGAKELRRVCsdrlRTLQLDVTKPEQIKRAAQWVKEHVGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  91 ITI--LVNNAAVVH-----GKSLMDSdddaLLKSQHVNTLGQFWTTKAFLPrMLELQNGHIVCLNSVLALSAIPGAIDYC 163
Cdd:cd09805    77 KGLwgLVNNAGILGfggdeELLPMDD----YRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYC 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1269612287 164 TSKASAFAFMESLTLGlLDCPGVSATTVLP 193
Cdd:cd09805   152 ASKAAVEAFSDSLRRE-LQPWGVKVSIIEP 180
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 22-182 1.20e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 51.57  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGN----REEVyqmAKAVREkVGDITILVNN 97
Cdd:PRK06701   56 SGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDeafcKDAV---EETVRE-LGRLDILVNN 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  98 AAV-VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMleLQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK06701  132 AAFqYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSL 209


                  ....*.
gi 1269612287 177 TLGLLD 182
Cdd:PRK06701  210 AQSLVQ 215
PRK06114 PRK06114
SDR family oxidoreductase;
5-200 1.21e-07

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 51.32  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   5 PKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREevyQMAKAV 84
Cdd:PRK06114    1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKA---DLRAAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  85 R---EKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSvlalsaIPGAI- 160
Cdd:PRK06114   78 ArteAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIAS------MSGIIv 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1269612287 161 -------DYCTSKASAFAFMESLTLGLLDcPGVSATTVLPFHTSTEM 200
Cdd:PRK06114  152 nrgllqaHYNASKAGVIHLSKSLAMEWVG-RGIRVNSISPGYTATPM 197
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
51-171 1.32e-07

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 51.27  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  51 KETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTK 130
Cdd:PRK08643   40 QAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQ 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 131 AFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKasaFA 171
Cdd:PRK08643  120 AAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTK---FA 158
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 28-208 1.53e-07

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: 51.08  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAER----GARkIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHG 103
Cdd:cd05363    15 IGRAFAQAyvreGAR-VAIADINLEAARATAAEI---GPAACAISLDVTDQASIDRCVAALVDRWGSIDILVNNAALFDL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 104 KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRML-ELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLD 182
Cdd:cd05363    91 APIVDITRESYDRLFAINVSGTLFMMQAVARAMIaQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIR 170

                         170       180
                  ....*....|....*....|....*.
gi 1269612287 183 cPGVSATTVLPFHTSTEMFQGMRVRF 208
Cdd:cd05363   171 -HGINVNAIAPGVVDGEHWDGVDAKF 195
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 27-228 1.68e-07

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 51.19  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRTEKcLKETTEEIRQMGTECHY--FICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK 104
Cdd:PRK12384   17 FLCHGLAEEGYRVAVADINSEK-AANVAQEINAEYGEGMAygFGADATSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQN--GHIVCLNSVlalSAIPGAIDYCTSKASAFA---FMESLTLG 179
Cdd:PRK12384   96 FITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIR-DGiqGRIIQINSK---SGKVGSKHNSGYSAAKFGgvgLTQSLALD 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 180 LLDcPGVSATTVLPFH-TSTEMFQGmrvrfpnLFPP------LKPETVARRTVDAV 228
Cdd:PRK12384  172 LAE-YGITVHSLMLGNlLKSPMFQS-------LLPQyakklgIKPDEVEQYYIDKV 219
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 15-204 1.74e-07

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: 50.93  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQmgtechyFICDVGNREEVYQMAKAVREKVGDITIL 94
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGAT-VIALDLPFVLLLEYGDPLRL-------TPLDVADAAAVREVCSRLLAEHGPIDAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  95 VNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFme 174
Cdd:cd05331    73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASL-- 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1269612287 175 SLTLGLLDCP-GVSATTVLPFHTSTEMFQGM 204
Cdd:cd05331   151 SKCLGLELAPyGVRCNVVSPGSTDTAMQRTL 181
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 27-158 2.31e-07

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: 50.66  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA----VVH 102
Cdd:cd05372    18 GIAKALHEAGA-ELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDGLVHSIAfapkVQL 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 103 GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPG 158
Cdd:cd05372    97 KGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNP--GGSIVTLSYLGSERVVPG 150
PRK05693 PRK05693
SDR family oxidoreductase;
14-261 3.47e-07

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 50.17  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  14 SVLITGGGRGIGRHLAREFAERGARkivLWGRTEKclKETTEEIRQMGTECHYFicDVGNREEVYQMAKAVREKVGDITI 93
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYE---VWATARK--AEDVEALAAAGFTAVQL--DVNDGAALARLAEELEAEHGGLDV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  94 LVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPrMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFM 173
Cdd:PRK05693   76 LINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 174 ESLTLGLldCP-GVSATTVLP------F--HTSTEMFQGMRVRFPnlFPPLKP----------------ETVARRTVDAV 228
Cdd:PRK05693  155 DALRLEL--APfGVQVMEVQPgaiasqFasNASREAEQLLAEQSP--WWPLREhiqararasqdnptpaAEFARQLLAAV 230

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1269612287 229 QQNQ--ALLLLPWTMNILIILKSILPQAALEEIHR 261
Cdd:PRK05693  231 QQSPrpRLVRLGNGSRALPLLARLLPRGLLDRVLR 265
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 21-155 3.62e-07

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: 50.30  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQM--GTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:cd05327    10 NSGIGKETARELAKRGAH-VIIACRNEEKGEEAAAEIKKEtgNAKVEVIQLDLSSLASVRQFAEEFLARFPRLDILINNA 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287  99 AVVHGKSLMDSDDdalLKSQ-HVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSA 155
Cdd:cd05327    89 GIMAPPRRLTKDG---FELQfAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAG 143
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
21-178 3.70e-07

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 50.07  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARKIVLwGRTEKclKETTEEIRQMGTECHYFICDVGNREEVYQMAKAV-----REKVGDITiLV 95
Cdd:PRK06924   10 SQGLGEAIANQLLEKGTHVISI-SRTEN--KELTKLAEQYNSNLTFHSLDLQDVHELETNFNEIlssiqEDNVSSIH-LI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  96 NNAAVVHG-KSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCTSKASAFAFM 173
Cdd:PRK06924   86 NNAGMVAPiKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYFGWSAYCSSKAGLDMFT 165


                  ....*
gi 1269612287 174 ESLTL 178
Cdd:PRK06924  166 QTVAT 170
PRK08251 PRK08251
SDR family oxidoreductase;
28-200 3.73e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 49.93  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERG------ARkivlwgRTEKclketTEEIRQMGTECHYFI------CDVGNREEVYQMAKAVREKVGDITILV 95
Cdd:PRK08251   18 MAREFAAKGrdlalcAR------RTDR-----LEELKAELLARYPGIkvavaaLDVNDHDQVFEVFAEFRDELGGLDRVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  96 NNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLpRMLELQN-GHIVCLNSVLALSAIPGAID-YCTSKASAFAFM 173
Cdd:PRK08251   87 VNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAM-EIFREQGsGHLVLISSVSAVRGLPGVKAaYAASKAGVASLG 165

                         170       180
                  ....*....|....*....|....*..
gi 1269612287 174 ESLTLGLLDCPgVSATTVLPFHTSTEM 200
Cdd:PRK08251  166 EGLRAELAKTP-IKVSTIEPGYIRSEM 191
PRK07774 PRK07774
SDR family oxidoreductase;
29-145 3.80e-07

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 50.13  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHG---KS 105
Cdd:PRK07774   23 AEALAREGA-SVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDYLVNNAAIYGGmklDL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1269612287 106 LMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:PRK07774  102 LITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIV 141
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 22-193 4.14e-07

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: 49.70  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVL---WGRTEKCLKETTEEIRQMGtechyFICDVGNREEVYQMAKAVREKVGDITILVNNA 98
Cdd:cd08943    11 SGIGLAIAKRLAAEGAAVVVAdidPEIAEKVAEAAQGGPRALG-----VQCDVTSEAQVQSAFEQAVLEFGGLDIVVSNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLMDSDDDALLKSQHVNTLGQFWTTK-AFlpRMLELQN--GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMES 175
Cdd:cd08943    86 GIATSSPIAETSLEDWNRSMDINLTGHFLVSReAF--RIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARC 163

                         170
                  ....*....|....*...
gi 1269612287 176 LTLGLLDcPGVSATTVLP 193
Cdd:cd08943   164 LALEGGE-DGIRVNTVNP 180
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 22-204 5.00e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 49.54  E-value: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVgnREEVYQ---MAKAVREkVGDITILVNNA 98
Cdd:PRK07478   16 SGIGRAAAKLFAREGA-KVVVGARRQAELDQLVAEIRAEGGEAVALAGDV--RDEAYAkalVALAVER-FGGLDIAFNNA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVV-HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSA-IPGAIDYCTSKASAFAFMESL 176
Cdd:PRK07478   92 GTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAgFPGMAAYAASKAGLIGLTQVL 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 1269612287 177 T--LGlldCPGVSATTVLPFHTSTEMFQGM 204
Cdd:PRK07478  172 AaeYG---AQGIRVNALLPGGTDTPMGRAM 198
PRK09291 PRK09291
SDR family oxidoreductase;
90-176 5.28e-07

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 49.61  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  90 DITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASA 169
Cdd:PRK09291   73 DVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152


                  ....*..
gi 1269612287 170 FAFMESL 176
Cdd:PRK09291  153 EAIAEAM 159
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 22-168 5.35e-07

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: 49.37  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKV-GDITILVNNAAV 100
Cdd:cd05329    16 KGIGYAIVEELAGLGA-EVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVNNAGT 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKAS 168
Cdd:cd05329    95 NIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 27-176 7.12e-07

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: 49.69  E-value: 7.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  27 HLAREFAERGARKIVLWGRTEKCLKETTEEI--RQMGTECHYFICDVGNREEVYQMAKAVREKVGdITILVNNAAVVHGK 104
Cdd:cd05274   165 LVARWLAARGARHLVLLSRRGPAPRAAARAAllRAGGARVSVVRCDVTDPAALAALLAELAAGGP-LAGVIHAAGVLRDA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALlksqhvntlgqfwtTKAFLPRMLELQNGH----------IVCLNSVLALSAIPGAIDYctskASAFAFME 174
Cdd:cd05274   244 LLAELTPAAF--------------AAVLAAKVAGALNLHeltpdlpldfFVLFSSVAALLGGAGQAAY----AAANAFLD 305


                  ..
gi 1269612287 175 SL 176
Cdd:cd05274   306 AL 307
PRK12746 PRK12746
SDR family oxidoreductase;
7-200 1.06e-06

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 48.88  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDV----GNREEVYQMAK 82
Cdd:PRK12746    1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLnsidGVKKLVEQLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  83 AVREKVG--DITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPrmLELQNGHIVCLNSVLALSAIPGAI 160
Cdd:PRK12746   81 ELQIRVGtsEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISSAEVRLGFTGSI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1269612287 161 DYCTSKASafafMESLTLGL---LDCPGVSATTVLPFHTSTEM 200
Cdd:PRK12746  159 AYGLSKGA----LNTMTLPLakhLGERGITVNTIMPGYTKTDI 197
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 25-204 1.10e-06

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: 48.62  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  25 GRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK 104
Cdd:cd05322    15 GEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQN-GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDc 183
Cdd:cd05322    95 KITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAE- 173

                         170       180
                  ....*....|....*....|..
gi 1269612287 184 PGVSATTVLPFH-TSTEMFQGM 204
Cdd:cd05322   174 HGITVNSLMLGNlLKSPMFQSL 195
PRK07832 PRK07832
SDR family oxidoreductase;
22-235 1.14e-06

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 48.89  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFIC-DVGNREEVYQMAKAVREKVGDITILVNNAav 100
Cdd:PRK07832   10 SGIGRATALRLAAQGAE-LFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAHGSMDVVMNIA-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 vhGKSLMDSDDDalLKSQH------VNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFM 173
Cdd:PRK07832   87 --GISAWGTVDR--LTHEQwrrmvdVNLMGPIHVIETFVPPMVAAgRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLS 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 174 ESLTLGL--------LDCPG------VSATTVLPFHTSTEMFQGMRVRFPNLfpPLKPETVARRTVDAVQQNQALL 235
Cdd:PRK07832  163 EVLRFDLarhgigvsVVVPGavktplVNTVEIAGVDREDPRVQKWVDRFRGH--AVTPEKAAEKILAGVEKNRYLV 236
PRK08340 PRK08340
SDR family oxidoreductase;
15-157 2.41e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 47.49  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGtECHYFICDVGNREEVYQMAKAVREKVGDITIL 94
Cdd:PRK08340    3 VLVTASSRGIGFNVARELLKKGAR-VVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287  95 VNNAAVVHGKSLM--DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIP 157
Cdd:PRK08340   81 VWNAGNVRCEPCMlhEAGYSDWLEAALLHLVAPGYLTTLLIQAWLEKKmKGVLVYLSSVSVKEPMP 146
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
29-152 2.42e-06

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 47.81  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARKIVLWGRTEkcLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMD 108
Cdd:PRK06935   32 AVALAKAGADIIITTHGTN--WDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLE 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLA 152
Cdd:PRK06935  110 YKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLS 153
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 8-178 2.87e-06

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 47.41  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   8 RDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREK 87
Cdd:PRK08936    3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  88 VGDITILVNNAAV-----VHGKSLMDSDddallKSQHVNTLGQFWTTKAFLPRMLEL-QNGHIVCLNSVLALSAIPGAID 161
Cdd:PRK08936   83 FGTLDVMINNAGIenavpSHEMSLEDWN-----KVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVH 157

                         170
                  ....*....|....*..
gi 1269612287 162 YCTSKASAFAFMESLTL 178
Cdd:PRK08936  158 YAASKGGVKLMTETLAM 174
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 32-182 3.12e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 47.06  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  32 FAERGARKIVLWGRTEKCLKETTEEIRQMGtECHYFICDVGNREEvyqmAKAVREKVGDITILVNNAAVVHGKSLMDS-D 110
Cdd:PRK05786   24 FALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTES----ARNVIEKAAKVLNAIDGLVVTVGGYVEDTvE 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1269612287 111 DDALLKSQHVNTL-GQFWTTKAFLPRMLElqNGHIVCLNSVLAL-SAIPGAIDYCTSKASAFAFMESLTLGLLD 182
Cdd:PRK05786   99 EFSGLEEMLTNHIkIPLYAVNASLRFLKE--GSSIVLVSSMSGIyKASPDQLSYAVAKAGLAKAVEILASELLG 170
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 29-150 3.55e-06

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 47.25  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEkCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNaavVHG----- 103
Cdd:PRK12823   25 ALRAAAEGAR-VVLVDRSE-LVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVLINN---VGGtiwak 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 104 ---------------KSLMDsdddallksqhvnTLgqfWTTKAFLPRMLELQNGHIVCLNSV 150
Cdd:PRK12823  100 pfeeyeeeqieaeirRSLFP-------------TL---WCCRAVLPHMLAQGGGAIVNVSSI 145
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 22-225 4.28e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 47.03  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMgtechYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK06057   17 SGIGLATARRLAAEGA-TVVVGDIDPEAGKAAADEVGGL-----FVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAGIS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 --HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLA-LSAIPGAIDYCTSKASAFAFmeSLTL 178
Cdd:PRK06057   91 ppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAvMGSATSQISYTASKGGVLAM--SREL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 179 GL----------LDCPGVSATTVLpfhtsTEMFQGmrvrfpnlfpplKPETVARRTV 225
Cdd:PRK06057  169 GVqfarqgirvnALCPGPVNTPLL-----QELFAK------------DPERAARRLV 208
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 15-145 4.37e-06

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: 46.80  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMG-TECHYFICDVGN--REEVYQMAKAVREKVGDI 91
Cdd:cd05340     7 ILVTGASDGIGREAALTYARYGA-TVILLGRNEEKLRQVADHINEEGgRQPQWFILDLLTctSENCQQLAQRIAVNYPRL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287  92 TILVNNAAVVHGKSLMDSDDDALLKS-QHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:cd05340    86 DGVLHNAGLLGDVCPLSEQNPQVWQDv*QVNVNATFMLTQALLPLLLKSDAGSLV 140
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 21-210 5.00e-06

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: 46.76  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMGT-ECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAA 99
Cdd:cd08933    18 SRGIGRGIVRAFVENGA-KVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGRIDCLVNNAG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 100 vVH--GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQnGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLT 177
Cdd:cd08933    97 -WHppHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQAAPYVATKGAITAMTKALA 174

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1269612287 178 LGllDCP-GVSATTVLPFHTSTEMFQGMRVRFPN 210
Cdd:cd08933   175 VD--ESRyGVRVNCISPGNIWTPLWEELAAQTPD 206
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 66-176 5.15e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 46.82  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  66 YFICDVGNREEVYQMAKAVREKVGDITILVNNAAV-VHG----------KSLMDsdddallksqhVNTLGQFWTTKAFLP 134
Cdd:PRK06179   49 LLELDVTDDASVQAAVDEVIARAGRIDVLVNNAGVgLAGaaeessiaqaQALFD-----------TNVFGILRMTRAVLP 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1269612287 135 RMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:PRK06179  118 HMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESL 159
PRK09730 PRK09730
SDR family oxidoreductase;
22-200 8.04e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 46.00  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:PRK09730   11 RGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAALVNNAGIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 102 HGKSLMDSdddalLKSQHVNTL------GQFWTTKAFLPRMLEL---QNGHIVCLNSVLALSAIPGA-IDYCTSKASafa 171
Cdd:PRK09730   91 FTQCTVEN-----LTAERINRVlstnvtGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEyVDYAASKGA--- 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1269612287 172 fMESLTLGL---LDCPGVSATTVLPFHTSTEM 200
Cdd:PRK09730  163 -IDTLTTGLsleVAAQGIRVNCVRPGFIYTEM 193
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 22-221 8.24e-06

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: 45.91  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQmgTECHYFICDVGNREEVyqmAKAVREKV---GDITILVNNA 98
Cdd:cd05326    14 SGIGEATARLFAKHGAR-VVIADIDDDAGQAVAAELGD--PDISFVHCDVTVEADV---RAAVDTAVarfGRLDIMFNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVV--HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESL 176
Cdd:cd05326    88 GVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGLTRSA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 177 TlGLLDCPGVSATTVLPFHTSTEMF-QGMRVR-------FPNLF----PPLKPETVA 221
Cdd:cd05326   168 A-TELGEHGIRVNCVSPYGVATPLLtAGFGVEdeaieeaVRGAAnlkgTALRPEDIA 223
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 22-180 1.11e-05

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: 45.35  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVV 101
Cdd:cd05357    10 KRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVNNASAF 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 102 HGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:cd05357    90 YPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALEL 168
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 22-106 1.62e-05

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: 45.13  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGArKIVLWGRT-EKCLKETTEEIRQMGTECHYFICDVGNREEVYQM-AKAVREKVGDITILVNNAA 99
Cdd:cd09763    13 RGIGRGIALQLGEAGA-TVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALfERVAREQQGRLDILVNNAY 91


                  ....*..
gi 1269612287 100 VVHGKSL 106
Cdd:cd09763    92 AAVQLIL 98
PRK06500 PRK06500
SDR family oxidoreductase;
21-202 1.64e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 44.95  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEirqMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:PRK06500   15 TSGIGLETARQFLAEGAR-VAITGRDPASLEAARAE---LGESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINAGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRmleLQNGHIVCLN-SVLALSAIPGAIDYCTSKASAFAFMESLTLG 179
Cdd:PRK06500   91 AKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPL---LANPASIVLNgSINAHIGMPNSSVYAASKAALLSLAKTLSGE 167

                         170       180
                  ....*....|....*....|...
gi 1269612287 180 LLDcPGVSATTVLPFHTSTEMFQ 202
Cdd:PRK06500  168 LLP-RGIRVNAVSPGPVQTPLYG 189
PRK08628 PRK08628
SDR family oxidoreductase;
21-210 2.30e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.56  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARKIVLwGRTEKCLkETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV 100
Cdd:PRK08628   16 ASGIGAAISLRLAEEGAIPVIF-GRSAPDD-EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VHGKSLmDSDDDALLKSQHVNTLGQFWTTKAFLPrMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK08628   94 NDGVGL-EAGREAFVASLERNLIHYYVMAHYCLP-HLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALTREWAVAL 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 1269612287 181 LDCpGVSATTVLPFHTSTEMFQGMRVRFPN 210
Cdd:PRK08628  172 AKD-GVRVNAVIPAEVMTPLYENWIATFDD 200
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 28-169 2.34e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 44.84  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAvVHGKSLM 107
Cdd:PRK06113   27 IAITFATAGASVVVSDINADAA-NHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDILVNNAG-GGGPKPF 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASA 169
Cdd:PRK06113  105 DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 28-257 7.47e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 43.32  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARK---IVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVG--DITILVNNAAVVH 102
Cdd:PLN02780   65 IGKGFAFQLARKglnLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEglDVGVLINNVGVSY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 103 --GKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALsAIPGAIDYCTSkASAFAFMESLTLGL 180
Cdd:PLN02780  145 pyARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAI-VIPSDPLYAVY-AATKAYIDQFSRCL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 181 ---LDCPGVSATTVLPFHTSTEMFQGMRVRFpnLFPplKPETVARRTVDAVQQnQALLLLPWTMNILIILKSILPQAALE 257
Cdd:PLN02780  223 yveYKKSGIDVQCQVPLYVATKMASIRRSSF--LVP--SSDGYARAALRWVGY-EPRCTPYWPHSLIWGLISALPESAVD 297
PRK07577 PRK07577
SDR family oxidoreductase;
10-209 7.87e-05

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 42.79  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  10 LSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTekclketteeirQMGTECHYFICDVGNREEVYQMAKAVREKvG 89
Cdd:PRK07577    1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSA------------IDDFPGELFACDLADIEQTAATLAQINEI-H 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  90 DITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSvlalSAIPGAIDYcTSKASA 169
Cdd:PRK07577   68 PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICS----RAIFGALDR-TSYSAA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1269612287 170 FAFMESLT---LGLLDCPGVSATTVLPFHTSTEMFqgmRVRFP 209
Cdd:PRK07577  143 KSALVGCTrtwALELAEYGITVNAVAPGPIETELF---RQTRP 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 15-166 9.45e-05

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: 42.89  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  15 VLITGGGRGIGRHLAREFAERGArKIVLWGRTEKCLKETTEEIRQMG--TECHYFICDVGNREEVYQMAKAVREKVGDIT 92
Cdd:cd05330     6 VLITGGGSGLGLATAVRLAKEGA-KLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEAYVDATVEQFGRID 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287  93 ILVNNAAvVHGK--SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSK 166
Cdd:cd05330    85 GFFNNAG-IEGKqnLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAK 159
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 21-167 1.07e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 42.58  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  21 GRGIGRHLAREFAERGARkIVLWGRTekCLKETTEEIrqmgtecHYFICDVGNREEVYQMAKAVREKVGDITILVNNA-- 98
Cdd:PRK06523   18 TKGIGAATVARLLEAGAR-VVTTARS--RPDDLPEGV-------EFVAADLTTAEGCAAVARAVLERLGGVDILVHVLgg 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  99 AVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGA-IDYCTSKA 167
Cdd:PRK06523   88 SSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAYAAAKA 157
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 28-180 1.07e-04

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: 42.57  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGArKIVLWGRTEKCLKETTEeirQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:cd09761    17 ICLDFLEAGD-KVVFADIDEERGADFAE---AEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNAARGSKGILS 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:cd09761    93 SLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHALAMSL 164
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 9-177 1.52e-04

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: 42.07  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   9 DLSRESVLITGGGRGIGRHLAREFAERGARKIVLwGRTEkclkettEEIRQMGTECHYF--IC-DVGNREEVyqmaKAVR 85
Cdd:cd05351     4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAV-SRTQ-------ADLDSLVRECPGIepVCvDLSDWDAT----EEAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  86 EKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQ-NGHIVCLNSVLALSAIPGAIDYCT 164
Cdd:cd05351    72 GSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCS 151

                         170
                  ....*....|...
gi 1269612287 165 SKASafafMESLT 177
Cdd:cd05351   152 TKAA----LDMLT 160
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 75-193 2.01e-04

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: 41.54  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  75 EEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDddaLLKSQH----VNTLGQFWTTKAFLPRMLElqNGHIVCLNSV 150
Cdd:cd05334    53 EQAKQVVASVARLSGKVDALICVAGGWAGGSAKSKS---FVKNWDlmwkQNLWTSFIASHLATKHLLS--GGLLVLTGAK 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1269612287 151 LALSAIPGAIDYCTSKASAFAFMESL---TLGLLdcPGVSATTVLP 193
Cdd:cd05334   128 AALEPTPGMIGYGAAKAAVHQLTQSLaaeNSGLP--AGSTANAILP 171
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 13-217 2.15e-04

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: 41.68  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  13 ESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKClKETTEEIRQmGTECHYFIC---DVGNREEVYQMAKAVREKVG 89
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKC-EEAAAEIRR-DTLNHEVIVrhlDLASLKSIRAFAAEFLAEED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  90 DITILVNNAAVV---HGKSlmdsdDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSvlaLSAIPGAID----- 161
Cdd:cd09807    80 RLDVLINNAGVMrcpYSKT-----EDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSS---LAHKAGKINfddln 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269612287 162 ----------YCTSKASAFAFMESLTlGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKP 217
Cdd:cd09807   152 seksyntgfaYCQSKLANVLFTRELA-RRLQGTGVTVNALHPGVVRTELGRHTGIHHLFLSTLLNP 216
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 29-167 2.16e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 41.92  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  29 AREFAERGARkIVLWGRTEKCLKETTEEIrqmGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAvVHGKSLMD 108
Cdd:PRK08265   23 ARALVAAGAR-VAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDILVNLAC-TYLDDGLA 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 109 SDDDALLKSQHVNTLGQFWTTKAFLPRMLElQNGHIVCLNSVLALSAIPGAIDYCTSKA 167
Cdd:PRK08265   98 SSRADWLAALDVNLVSAAMLAQAAHPHLAR-GGGAIVNFTSISAKFAQTGRWLYPASKA 155
PLN02253 PLN02253
xanthoxin dehydrogenase
 66-200 2.26e-04

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 41.73  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  66 YFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVhGKSLMDSDDDALLKSQHV---NTLGQFWTTKAFLPRMLELQNG 142
Cdd:PLN02253   70 FFHCDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLT-GPPCPDIRNVELSEFEKVfdvNVKGVFLGMKHAARIMIPLKKG 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 143 HIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTlGLLDCPGVSATTVLPFHTSTEM 200
Cdd:PLN02253  149 SIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVA-AELGKHGIRVNCVSPYAVPTAL 205
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 7-149 3.31e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 41.28  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287   7 LRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKClKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVRE 86
Cdd:PRK08085    4 LFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERA-ELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1269612287  87 KVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNS 149
Cdd:PRK08085   83 DIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICS 145
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 22-234 4.34e-04

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: 40.51  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIrqmGTE-CHYFICDVGNREEVYQ-MAKAVREKVGDITILVNNAA 99
Cdd:cd08931    10 SGIGRETALLFARNGWF-VGLYDIDEDGLAALAAEL---GAEnVVAGALDVTDRAAWAAaLADFAAATGGRLDALFNNAG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 100 VVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLG 179
Cdd:cd08931    86 VGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVE 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 180 LLDCpGVSATTVLPFHTSTEMFQGMR---VRFPNLFPPLKPETVARRTVDAVQQNQAL 234
Cdd:cd08931   166 WARH-GIRVADVWPWFVDTPILTKGEtgaAPKKGLGRVLPVSDVAKVVWAAAHGVPKL 222
PRK09134 PRK09134
SDR family oxidoreductase;
28-167 5.56e-04

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 40.68  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLM 107
Cdd:PRK09134   25 IALDLAAHGFDVAVHYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPITLLVNNASLFEYDSAA 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269612287 108 DSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCL--NSVLALSaiPGAIDYCTSKA 167
Cdd:PRK09134  105 SFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMidQRVWNLN--PDFLSYTLSKA 164
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 94-222 6.06e-04

Short-chain dehydrogenases/reductases (SDR); 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 (KR) 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: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 39.81  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  94 LVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFM 173
Cdd:cd02266    35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1269612287 174 ES---------LTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPplkPETVAR 222
Cdd:cd02266   115 QQwasegwgngLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMP---PEEVAR 169
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 10-200 1.41e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 39.29  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  10 LSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVG 89
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  90 DIT------ILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYC 163
Cdd:PRK12747   82 NRTgstkfdILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD--NSRIINISSAATRISLPDFIAYS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1269612287 164 TSKASafafMESLTLGL---LDCPGVSATTVLPFHTSTEM 200
Cdd:PRK12747  160 MTKGA----INTMTFTLakqLGARGITVNAILPGFIKTDM 195
PRK08017 PRK08017
SDR family oxidoreductase;
121-261 1.44e-03

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 39.30  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 121 NTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSATTVLPFHTSTEM 200
Cdd:PRK08017  105 NFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDALRMELRH-SGIKVSLIEPGPIRTRF 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269612287 201 FQ--------------GMRVRFpnlfpPLKPETVARRTVDAVQQNQALLLLPWTM--NILIILKSILPQAALEEIHR 261
Cdd:PRK08017  184 TDnvnqtqsdkpvenpGIAARF-----TLGPEAVVPKLRHALESPKPKLRYPVTLvtHAVMVLKRLLPGRMMDKILR 255
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 28-157 1.53e-03

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 39.07  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLKETTEEIRQMG-TECHYFICDVGNREEVYQMAKAVREkVGDITILVNNAAVVHGKSL 106
Cdd:PRK08339   24 VARVLARAGADVILL-SRNEENLKKAREKIKSESnVDVSYIVADLTKREDLERTVKELKN-IGEPDIFFFSTGGPKPGYF 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1269612287 107 MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIP 157
Cdd:PRK08339  102 MEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIP 152
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 22-145 1.74e-03

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 39.09  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLwGRTEKCLKETTEEIRQMG-TECHYFICDV-GNREEVYQ-MAKAVREKVGDITILVNNA 98
Cdd:PRK08945   22 DGIGREAALTYARHGATVILL-GRTEEKLEAVYDEIEAAGgPQPAIIPLDLlTATPQNYQqLADTIEEQFGRLDGVLHNA 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1269612287  99 AVVHGKSLMDSDDDALLKS-QHVNTLGQFWTTKAFLPRMLELQNGHIV 145
Cdd:PRK08945  101 GLLGELGPMEQQDPEVWQDvMQVNVNATFMLTQALLPLLLKSPAASLV 148
PRK06101 PRK06101
SDR family oxidoreductase;
28-256 1.82e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 38.70  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLwGRTEKCLkettEEIRQMGTECHYFICDVGNREEVYQmAKAVREKVGDITILvnNAAvvHGKSLM 107
Cdd:PRK06101   17 LALDYAKQGWQVIAC-GRNQSVL----DELHTQSANIFTLAFDVTDHPGTKA-ALSQLPFIPELWIF--NAG--DCEYMD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 108 DSDDDALLKSQ--HVNTLGQFWTTKAFLPRmleLQNGH-IVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGlLDCP 184
Cdd:PRK06101   87 DGKVDATLMARvfNVNVLGVANCIEGIQPH---LSCGHrVVIVGSIASELALPRAEAYGASKAAVAYFARTLQLD-LRPK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 185 GVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAvqqNQALLLLPWTMNILIILKSILP---QAAL 256
Cdd:PRK06101  163 GIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRAQLAR---GKSHIYFPARFTWLIRLLGLLPyawQGRL 234
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
52-205 1.93e-03

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 38.73  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  52 ETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKA 131
Cdd:PRK12481   45 ETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269612287 132 FLPRMLELQN-GHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcPGVSATTVLPFHTSTEMFQGMR 205
Cdd:PRK12481  125 VAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQ-YNINVNAIAPGYMATDNTAALR 198
PRK07023 PRK07023
SDR family oxidoreductase;
93-226 2.46e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 38.46  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  93 ILVNNAAVVHGKSLMDS-DDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFA 171
Cdd:PRK07023   80 LLINNAGTVEPIGPLATlDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDH 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 172 FMESLTlglLDCP-GVSATTVLPFHTSTEMFQGMR----VRFPNL--FPPLK-------PETVARRTVD 226
Cdd:PRK07023  160 HARAVA---LDANrALRIVSLAPGVVDTGMQATIRatdeERFPMRerFRELKasgalstPEDAARRLIA 225
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 22-204 3.36e-03

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: 38.04  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRqmgteCHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAV- 100
Cdd:cd05371    12 SGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDN-----CRFVPVDVTSEKDVKAALALAKAKFGRLDIVVNCAGIa 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 -----VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLE---LQNGH---IVCLNSVLALSAIPGAIDYCTSKASa 169
Cdd:cd05371    87 vaaktYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKnepDQGGErgvIINTASVAAFEGQIGQAAYSASKGG- 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1269612287 170 fafMESLTLGL---LDCPGVSATTVLPFHTSTEMFQGM 204
Cdd:cd05371   166 ---IVGMTLPIardLAPQGIRVVTIAPGLFDTPLLAGL 200
PRK12744 PRK12744
SDR family oxidoreductase;
28-203 3.42e-03

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 38.18  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLW---GRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGK 104
Cdd:PRK12744   24 IARDLAAQGAKAVAIHynsAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGRPDIAINTVGKVLKK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 105 SLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCLNSVLALSAIPGAIDYCTSK--------ASAFAFMESl 176
Cdd:PRK12744  104 PIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLND--NGKIVTLVTSLLGAFTPFYSAYAGSKapvehftrAASKEFGAR- 180

                         170       180
                  ....*....|....*....|....*..
gi 1269612287 177 tlglldcpGVSATTVLPFHTSTEMFQG 203
Cdd:PRK12744  181 --------GISVTAVGPGPMDTPFFYP 199
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
28-147 5.00e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 37.79  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  28 LAREFAERGARKIVLWG--RTEKCLKETTEEIRQmgTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKS 105
Cdd:PRK08594   25 IARSLHNAGAKLVFTYAgeRLEKEVRELADTLEG--QESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCIAFANKED 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1269612287 106 L----MDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVCL 147
Cdd:PRK08594  103 LrgefLETSRDGFLLAQNISAYSLTAVAREAKKLMTE--GGSIVTL 146
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 67-230 6.30e-03

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: 36.79  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  67 FICDVGNREEVyqmaKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLElqNGHIVC 146
Cdd:cd11731    35 YQVDITDEASI----KALFEKVGHFDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND--GGSITL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 147 LNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDcpG-----VSATTVlpfHTSTEMFQGMrvrFPNlFPPLKPETVA 221
Cdd:cd11731   109 TSGILAQRPIPGGAAAATVNGALEGFVRAAAIELPR--GirinaVSPGVV---EESLEAYGDF---FPG-FEPVPAEDVA 179


                  ....*....
gi 1269612287 222 RRTVDAVQQ 230
Cdd:cd11731   180 KAYVRSVEG 188
PRK08267 PRK08267
SDR family oxidoreductase;
22-234 8.12e-03

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 36.84  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287  22 RGIGRHLAREFAERGARkIVLWGRTEKCLKETTEEIRQMGTECHYFicDVGNREEVYQ-MAKAVREKVGDITILVNNAAV 100
Cdd:PRK08267   11 SGIGRATALLFAAEGWR-VGAYDINEAGLAALAAELGAGNAWTGAL--DVTDRAAWDAaLADFAAATGGRLDVLFNNAGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269612287 101 VHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGL 180
Cdd:PRK08267   88 LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEALDLEW 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1269612287 181 LDcPGVSATTVLPFHTSTEMFQG-----MRVRFPNLFPPLKPETVARRTVDAVQQNQAL 234
Cdd:PRK08267  168 RR-HGIRVADVMPLFVDTAMLDGtsnevDAGSTKRLGVRLTPEDVAEAVWAAVQHPTRL 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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