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Conserved domains on  [gi|767979509|ref|XP_011534640|]
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dehydrogenase/reductase SDR family member 2, mitochondrial isoform X2 [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
1-199 1.54e-94

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd08936:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 256  Bit Score: 275.96  E-value: 1.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd08936   51 VATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRG-AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKN 159
Cdd:cd08936  131 VPEMEKRGGgSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08936  211 MKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGG 250
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
1-199 1.54e-94

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: 275.96  E-value: 1.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd08936   51 VATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRG-AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKN 159
Cdd:cd08936  131 VPEMEKRGGgSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08936  211 MKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGG 250
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
2-199 3.51e-65

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: 201.17  E-value: 3.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:COG1028   48 AELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNF 160
Cdd:COG1028  127 PHMrERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 161 KEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:COG1028  207 AARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDG 245
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
7-201 5.50e-58

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: 182.25  E-value: 5.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509    7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMe 85
Cdd:pfam13561  41 EELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQ 165
Cdd:pfam13561 120 KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAP 199
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767979509  166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:pfam13561 200 LGRLGTPEEVANAAAFLASDLASYITGQVLYVdGGYT 236
FabG-like PRK07231
SDR family oxidoreductase;
6-199 5.83e-57

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 180.03  E-value: 5.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:PRK07231  50 LAGGRAIAVAADVSDEADVEAAVAAALERFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMr 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkvfhgnESLWKNFKEHH 164
Cdd:PRK07231 130 GEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLL------EAFMGEPTPEN 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 165 Q--------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07231 204 RakflatipLGRLGTPEDIANAALFLASDEASWITGVTLVVDG 246
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
102-199 8.91e-15

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 70.73  E-value: 8.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  102 PVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIiktDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSF 181
Cdd:TIGR02685 166 PLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL---SLLPDAMPFEVQEDYRRKVPLGQREASAEQIADVVIF 242
                          90
                  ....*....|....*...
gi 767979509  182 LCSPDASYVNGENIAVAG 199
Cdd:TIGR02685 243 LVSPKAKYITGTCIKVDG 260
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
1-199 1.54e-94

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: 275.96  E-value: 1.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd08936   51 VATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRG-AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKN 159
Cdd:cd08936  131 VPEMEKRGGgSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08936  211 MKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGG 250
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
2-199 3.51e-65

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: 201.17  E-value: 3.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:COG1028   48 AELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNF 160
Cdd:COG1028  127 PHMrERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 161 KEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:COG1028  207 AARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDG 245
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
2-197 1.27e-58

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: 184.02  E-value: 1.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLL 81
Cdd:cd05233   39 AAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDED-WDRVLDVNLTGVFLLTRAAL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhGNESLWKNF 160
Cdd:cd05233  118 PHMkKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKL-GPEEAEKEL 196
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767979509 161 KEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV 197
Cdd:cd05233  197 AAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
7-201 5.50e-58

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: 182.25  E-value: 5.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509    7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMe 85
Cdd:pfam13561  41 EELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQ 165
Cdd:pfam13561 120 KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAP 199
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767979509  166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:pfam13561 200 LGRLGTPEEVANAAAFLASDLASYITGQVLYVdGGYT 236
FabG-like PRK07231
SDR family oxidoreductase;
6-199 5.83e-57

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 180.03  E-value: 5.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:PRK07231  50 LAGGRAIAVAADVSDEADVEAAVAAALERFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMr 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkvfhgnESLWKNFKEHH 164
Cdd:PRK07231 130 GEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLL------EAFMGEPTPEN 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 165 Q--------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07231 204 RakflatipLGRLGTPEDIANAALFLASDEASWITGVTLVVDG 246
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2-199 2.56e-47

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 155.32  E-value: 2.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK05653  47 AELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAAL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVfhGNESLWKNF 160
Cdd:PRK05653 126 PPMiKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEG--LPEEVKAEI 203
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 161 KEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK05653 204 LKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNG 242
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-199 3.11e-45

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 149.99  E-value: 3.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK05565  50 IKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESlwKNFKE 162
Cdd:PRK05565 129 MIKRKSGVIVnISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDK--EGLAE 206
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767979509 163 HHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK05565 207 EIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDG 243
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
2-199 3.62e-43

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 144.95  E-value: 3.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSPALLLS 78
Cdd:PRK05557  48 AEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNAGItrdNLL----MRMKEEDWDRVIDTNLTGVFNLTK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhgNESLW 157
Cdd:PRK05557 124 AVARPMmKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDAL--PEDVK 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK05557 202 EAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNG 243
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-199 1.01e-40

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 138.46  E-value: 1.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGstlgTSEQIWDKILSVNVKSPALLLS 78
Cdd:PRK12825  49 EAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDILVNNAGIfedKPLAD----MSDDEWDEVIDVNLSGVFHLLR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvfhgnesLW 157
Cdd:PRK12825 125 AVVPPMRKQRgGRIVNISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDM---------KE 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 158 KNFKEHHQ-------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12825 196 ATIEEAREakdaetpLGRSGTPEDIARAVAFLCSDASDYITGQVIEVTG 244
PRK12826 PRK12826
SDR family oxidoreductase;
4-199 2.63e-40

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 137.74  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK12826  50 VEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 M-ENRRGAVILVSSIAAynPVVA---LGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhGNESLWKN 159
Cdd:PRK12826 129 LiRAGGGRIVLTSSVAG--PRVGypgLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL-GDAQWAEA 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12826 206 IAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDG 245
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
2-199 6.03e-40

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: 136.14  E-value: 6.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgsT-----LGTSEQIWDKILSVNVKSPALL 76
Cdd:cd05333   42 EEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAGI------TrdnllMRMSEEDWDAVINVNLTGVFNV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  77 LSQLLPYM-ENRRGAVILVSSIAAY--NPVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhgN 153
Cdd:cd05333  116 TQAVIRAMiKRRSGRIINISSVVGLigNPGQA--NYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDAL--P 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 154 ESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05333  192 EKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNG 237
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
4-203 1.34e-39

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: 135.86  E-value: 1.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:cd05344   45 LRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-----FSKVFHGNE-SL 156
Cdd:cd05344  124 MKERGwGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTErvrrlLEARAEKEGiSV 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509 157 WKNFKEHHQ---LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYSTR 203
Cdd:cd05344  204 EEAEKEVASqipLGRVGKPEELAALIAFLASEKASYITGQAILVDGGLTR 253
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
2-199 7.17e-39

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: 133.55  E-value: 7.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:cd05362   46 AEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvFHGNES--LWKN 159
Cdd:cd05362  125 KRL-RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM---FYAGKTeeAVEG 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05362  201 YAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRANG 240
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
2-148 2.04e-38

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 131.20  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509    2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:pfam00106  42 KELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVL 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509   82 PYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:pfam00106 121 PAMIKGSGGRIVnISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-146 7.44e-38

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 131.15  E-value: 7.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:COG0300   47 AELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALL 125
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:COG0300  126 PLMrARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
PRK12829 PRK12829
short chain dehydrogenase; Provisional
7-199 1.52e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 130.95  E-value: 1.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-E 85
Cdd:PRK12829  56 PGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLkA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAynPVVALGV---YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT---------DFSKVFHGN 153
Cdd:PRK12829 136 SGHGGVIIALSSVA--GRLGYPGrtpYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGprmrrvieaRAQQLGIGL 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 154 ESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12829 214 DEMEQEYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDG 259
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
1-199 1.21e-36

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: 128.34  E-value: 1.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG-VDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSpALLLSQ 79
Cdd:cd05329   47 LTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGkLNILVNNAGTNIRKEAKDYTEED-YSLIMSTNFEA-AYHLSR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  80 LL-PYME-NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLW 157
Cdd:cd05329  125 LAhPLLKaSGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENL 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05329  205 DKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVDG 246
PRK07035 PRK07035
SDR family oxidoreductase;
7-199 2.10e-36

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 127.44  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-E 85
Cdd:PRK07035  55 AGGKAEALACHIGEMEQIDALFAHIRERHGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMkE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQ 165
Cdd:PRK07035 135 QGGGSIVNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIP 214
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07035 215 LRRHAEPSEMAGAVLYLASDASSYTTGECLNVDG 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
8-184 2.11e-36

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: 127.22  E-value: 2.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-EN 86
Cdd:COG4221   50 GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMrAR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  87 RRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS-KVFHGN-ESLWKNFKEHH 164
Cdd:COG4221  129 GSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLdSVFDGDaEAAAAVYEGLE 208
                        170       180
                 ....*....|....*....|
gi 767979509 165 QLQrigeSEDCAGIVSFLCS 184
Cdd:COG4221  209 PLT----PEDVAEAVLFALT 224
PRK09242 PRK09242
SDR family oxidoreductase;
5-199 6.34e-36

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 126.40  E-value: 6.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   5 QGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSpALLLSQLL-PY 83
Cdd:PRK09242  56 EFPEREVHGLAADVSDDEDRRAILDWVEDHWDGLHILVNNAGGN-IRKAAIDYTEDEWRGIFETNLFS-AFELSRYAhPL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKE 162
Cdd:PRK09242 134 LKQHaSSAIVNIGSVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIE 213
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767979509 163 HHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK09242 214 RTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIAVDG 250
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
18-202 1.11e-35

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: 125.54  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSS 96
Cdd:cd05359   57 VSQPQDVEEMFAAVKERFGRLDVLVSNAAAGAFR-PLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCA 176
Cdd:cd05359  136 LGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGTPQDVA 215
                        170       180
                 ....*....|....*....|....*..
gi 767979509 177 GIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:cd05359  216 DAVGFLCSDAARMITGQTLVVdGGLSI 242
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
2-202 1.35e-35

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 125.44  E-value: 1.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgsTLGT-SE----QIWDKILSVNVKSpALL 76
Cdd:PRK08213  54 AHLEALGIDALWIAADVADEADIERLAEETLERFGHVDILVNNAGA------TWGApAEdhpvEAWDKVMNLNVRG-LFL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  77 LSQLLP--YMENRR-GAVILVSSIA--AYNPVVALGV--YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKV 149
Cdd:PRK08213 127 LSQAVAkrSMIPRGyGRIINVASVAglGGNPPEVMDTiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRG 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767979509 150 FHgnESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:PRK08213 207 TL--ERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGGVS 257
PRK12939 PRK12939
short chain dehydrogenase; Provisional
2-199 2.56e-35

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 124.70  E-value: 2.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTlGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK12939  49 AALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSAT-ELDIDTWDAVMNVNVRGTFLMLRAAL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS---KVFHGNESLw 157
Cdd:PRK12939 128 PHLrDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATayvPADERHAYY- 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 knfKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12939 207 ---LKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPVNG 245
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
3-202 2.88e-35

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: 124.50  E-value: 2.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP 82
Cdd:cd05331   34 LLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGV-LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 YMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF----HGNESLW 157
Cdd:cd05331  113 HMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLwhdeDGAAQVI 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 158 KNFKEHHQ----LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:cd05331  193 AGVPEQFRlgipLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGGAT 241
PRK06172 PRK06172
SDR family oxidoreductase;
6-199 5.04e-35

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 124.09  E-value: 5.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAgivCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:PRK06172  56 GEALFVA---CDVTRDAEVKALVEQTIAAYGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMl 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNF-KEH 163
Cdd:PRK06172 133 AQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEFaAAM 212
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06172 213 HPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDG 248
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
18-199 6.10e-34

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: 120.96  E-value: 6.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSS 96
Cdd:cd05345   60 VTKRADVEAMVEAALSKFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIInIAS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNES--LWKNFKEHHQLQRIGESED 174
Cdd:cd05345  140 TAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDTpeNRAKFRATIPLGRLSTPDD 219
                        170       180
                 ....*....|....*....|....*
gi 767979509 175 CAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05345  220 IANAALYLASDEASFITGVALEVDG 244
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
2-199 1.11e-33

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: 120.37  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQL- 80
Cdd:cd05365   41 AAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFS-AFRLSQLc 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhGNESLWKN 159
Cdd:cd05365  120 APHMQKAGGGAILnISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASV-LTPEIERA 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05365  199 MLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSG 238
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
14-199 1.48e-33

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: 120.21  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL 93
Cdd:cd05364   60 VVADLTEEEGQDRIISTTLAKFGRLDILVNNAGI-LAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVN 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNF----KEHHQLQRI 169
Cdd:cd05364  139 VSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFlsraKETHPLGRP 218
                        170       180       190
                 ....*....|....*....|....*....|
gi 767979509 170 GESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05364  219 GTVDEVAEAIAFLASDASSFITGQLLPVDG 248
PRK09135 PRK09135
pteridine reductase; Provisional
10-199 2.54e-33

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 119.26  E-value: 2.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  10 SVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLvGSTlgtSEQIWDKILSVNVKSPaLLLSQ-LLPYME 85
Cdd:PRK09135  58 SAAALQADLLDPDALPELVAACVAAFGRLDALVNNASSfypTPL-GSI---TEAQWDDLFASNLKAP-FFLSQaAAPQLR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPkDIRVNCVVPGIIktdfskvfhgnesLW----KNFK 161
Cdd:PRK09135 133 KQRGAIVNITDIHAERPLKGYPVYCAAKAALEMLTRSLALELAP-EVRVNAVAPGAI-------------LWpedgNSFD 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 162 EHHQ--------LQRIGESEDCAGIVSFLCSpDASYVNGENIAVAG 199
Cdd:PRK09135 199 EEARqailartpLKRIGTPEDIAEAVRFLLA-DASFITGQILAVDG 243
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
6-199 2.84e-32

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 116.71  E-value: 2.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGivcHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:cd05358   53 GKAIAVQA---DVSKEEDVVALFQSAIKEFGTLDILVNNAGLQGDASSHEMTLED-WNKVIDVNLTGQFLCAREAIKRFr 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 -ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEH 163
Cdd:cd05358  129 kSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSL 208
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05358  209 IPMGRIGEPEEIAAAAAWLASDEASYVTGTTLFVDG 244
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
18-199 5.30e-32

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 116.02  E-value: 5.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSS 96
Cdd:PRK12824  61 VTDTEECAEALAEIEEEEGPVDILVNNAGITR-DSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhGNESLWKnFKEHHQLQRIGESEDCA 176
Cdd:PRK12824 140 VNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQM-GPEVLQS-IVNQIPMKRLGTPEEIA 217
                        170       180
                 ....*....|....*....|...
gi 767979509 177 GIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12824 218 AAVAFLVSEAAGFITGETISING 240
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
18-199 1.93e-31

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: 114.78  E-value: 1.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVS 95
Cdd:cd05366   61 VTDKDDVEALIDQAVEKFGSFDVMVNNAGIAP-ITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFkkLGHGGKIINAS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  96 SIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF--------SKVFHGNE-SLWKNFKEHHQL 166
Cdd:cd05366  140 SIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyideevGEIAGKPEgEGFAEFSSSIPL 219
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767979509 167 QRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05366  220 GRLSEPEDVAGLVSFLASEDSDYITGQTILVDG 252
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
7-202 1.96e-31

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 114.60  E-value: 1.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-E 85
Cdd:PRK08220  46 EDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAGILRM-GATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFrR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfhgneSLWKN------ 159
Cdd:PRK08220 125 QRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQR------TLWVDedgeqq 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 160 --------FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:PRK08220 199 viagfpeqFKLGIPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGGAT 249
PRK08265 PRK08265
short chain dehydrogenase; Provisional
7-201 4.30e-31

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 113.95  E-value: 4.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDR--EQLVAKALEHCGGVDFLV---CSagvnpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK08265  48 ASLGERARFIATDITDDAaiERAVATVVARFGRVDILVnlaCT-----YLDDGLASSRADWLAALDVNLVSAAMLAQAAH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMENRRGAVILVSSIAAynPVVALG--VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIktdFSKVFhgnESLWKN 159
Cdd:PRK08265 123 PHLARGGGAIVNFTSISA--KFAQTGrwLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWT---WSRVM---DELSGG 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 160 FKEH--------HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK08265 195 DRAKadrvaapfHLLGRVGDPEEVAQVVAFLCSDAASFVTGADYAVdGGYS 245
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
11-199 4.48e-31

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: 113.74  E-value: 4.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCH-------VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:cd08944   44 VAQIAGGalalrvdVTDEQQVAALFERAVEEFGGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK----VFHGNESLWK 158
Cdd:cd08944  124 MIARGGGSIVnLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLaklaGFEGALGPGG 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 159 NFKEHHQLQ-RIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08944  204 FHLLIHQLQgRLGRPEDVAAAVVFLLSDDASFITGQVLCVDG 245
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
2-199 8.58e-31

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 113.02  E-value: 8.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWdkILSVNVKSPaLLLSQL- 80
Cdd:PRK06113  53 DEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDILVNNAGGGGPKPFDMPMADFRR--AYELNVFSF-FHLSQLv 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKN 159
Cdd:PRK06113 130 APEMEKNGGGVILtITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKM 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKeHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06113 210 LQ-HTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSG 248
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
2-201 1.08e-30

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 112.51  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSA--GVN-PLvgstLGTSEQIWDKILSVNVKSPALLLS 78
Cdd:PRK08063  47 EEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVFVNNAasGVLrPA----MELEESHWDWTMNINAKALLFCAQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLW 157
Cdd:PRK08063 123 EAAKLMEKVGgGKIISLSSLGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELL 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK08063 203 EDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRGQTIIVdGGRS 247
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
10-199 5.84e-30

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: 110.75  E-value: 5.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  10 SVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTlGTSEQIWDKILSVNVKSPALLLSQLLPY-MENRR 88
Cdd:cd05369   54 RAHPIQCDVRDPEAVEAAVDETLKEFGKIDILINNAAGNFLAPAE-SLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKH 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  89 GAVILvsSIAAYNPV--VALGVYN-VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD--FSKVFHGNESLWKnFKEH 163
Cdd:cd05369  133 GGSIL--NISATYAYtgSPFQVHSaAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERLAPSGKSEKK-MIER 209
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05369  210 VPLGRLGTPEEIANLALFLLSDAASYINGTTLVVDG 245
PRK06398 PRK06398
aldose dehydrogenase; Validated
14-199 1.72e-29

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 109.92  E-value: 1.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL 93
Cdd:PRK06398  49 FKVDVSNKEQVIKGIDYVISKYGRIDILVNNAGIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVII 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 -VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTDF------SKVFHGNESLWKNFKE---H 163
Cdd:PRK06398 128 nIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLlewaaeLEVGKDPEHVERKIREwgeM 206
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06398 207 HPMKRVGKPEEVAYVVAFLASDLASFITGECVTVDG 242
PRK07856 PRK07856
SDR family oxidoreductase;
7-199 4.87e-28

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 105.79  E-value: 4.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEN 86
Cdd:PRK07856  45 DGRPAEFHAADVRDPDQVAALVDAIVERHGRLDVLVNNAGGSPYA-LAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  87 --RRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHH 164
Cdd:PRK07856 124 qpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHYGDAEGIAAVAATV 202
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767979509 165 QLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07856 203 PLGRLATPADIAWACLFLASDLASYVSGANLEVHG 237
PRK06138 PRK06138
SDR family oxidoreductase;
18-199 5.39e-28

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 105.62  E-value: 5.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILvsSI 97
Cdd:PRK06138  62 VGSAEAVEALVDFVAARWGRLDVLVNNAGFGCG-GTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIV--NT 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  98 AAYNPVVAL---GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-FSKVF--HGN-ESLWKNFKEHHQLQRIG 170
Cdd:PRK06138 139 ASQLALAGGrgrAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPyFRRIFarHADpEALREALRARHPMNRFG 218
                        170       180
                 ....*....|....*....|....*....
gi 767979509 171 ESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06138 219 TAEEVAQAALFLASDESSFATGTTLVVDG 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
8-199 6.35e-28

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: 105.49  E-value: 6.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSpALLLSQL--LPYME 85
Cdd:cd05352   57 GVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQ-WNKVIDVNLNG-VFNCAQAaaKIFKK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVAL--GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNesLWKNFKEH 163
Cdd:cd05352  135 QGKGSLIITASMSGTIVNRPQpqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKE--LRKKWESY 212
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05352  213 IPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDG 248
PRK12937 PRK12937
short chain dehydrogenase; Provisional
18-199 6.69e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 105.21  E-value: 6.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVILVSSI 97
Cdd:PRK12937  64 VADAAAVTRLFDAAETAFGRIDVLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  98 AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskVFHGNES-LWKNFKEHHQLQRIGESEDCA 176
Cdd:PRK12937 142 VIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL--FFNGKSAeQIDQLAGLAPLERLGTPEEIA 219
                        170       180
                 ....*....|....*....|...
gi 767979509 177 GIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12937 220 AAVAFLAGPDGAWVNGQVLRVNG 242
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
1-199 1.55e-27

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: 104.36  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd05347   46 QQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNNAGII-RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKN 159
Cdd:cd05347  125 ARHMiKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDD 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05347  205 ILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDG 244
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-199 2.75e-27

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 104.05  E-value: 2.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSpALLLSQLLP- 82
Cdd:PRK06935  61 EGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILVNNAGTirrAPL----LEYKDEDWNAVMDINLNS-VYHLSQAVAk 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 -YMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESlwknfK 161
Cdd:PRK06935 136 vMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKN-----R 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 162 EHHQLQRI-----GESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06935 211 NDEILKRIpagrwGEPDDLMGAAVFLASRASDYVNGHILAVDG 253
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
18-199 3.06e-27

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: 103.62  E-value: 3.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVnpLVGSTL--GTSEQiWDKILSVNVKSPALLLSQLLPYMENR-RGAVILV 94
Cdd:cd05341   60 VTDEDGWTAVVDTAREAFGRLDVLVNNAGI--LTGGTVetTTLEE-WRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINM 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  95 SSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKD--IRVNCVVPGIIKTDFSKVFHGNESLWKNFKEhHQLQRIGES 172
Cdd:cd05341  137 SSIEGLVGDPALAAYNASKGAVRGLTKSAALECATQGygIRVNSVHPGYIYTPMTDELLIAQGEMGNYPN-TPMGRAGEP 215
                        170       180
                 ....*....|....*....|....*..
gi 767979509 173 EDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05341  216 DEIAYAVVYLASDESSFVTGSELVVDG 242
PRK12827 PRK12827
short chain dehydrogenase; Provisional
33-199 4.39e-27

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 103.26  E-value: 4.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  33 EHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYN 110
Cdd:PRK12827  83 EEFGRLDILVNNAGIATDAAFAELSIEE-WDDVIDVNLDGFFNVTQAALPPMirARRGGRIVNIASVAGVRGNRGQVNYA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 111 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfhgNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYV 190
Cdd:PRK12827 162 ASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMAD----NAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYV 237

                 ....*....
gi 767979509 191 NGENIAVAG 199
Cdd:PRK12827 238 TGQVIPVDG 246
PRK06841 PRK06841
short chain dehydrogenase; Provisional
12-201 5.41e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 103.20  E-value: 5.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  12 AGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGA 90
Cdd:PRK06841  64 KGLVCDVSDSQSVEAAVAAVISAFGRIDILVNSAGVALL-APAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMiAAGGGK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAynpVVALG---VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfhgneSLWKNFK-EHHQL 166
Cdd:PRK06841 143 IVNLASQAG---VVALErhvAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK------KAWAGEKgERAKK 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 167 Q----RIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK06841 214 LipagRFAYPEEIAAAALFLASDAAAMITGENLVIdGGYT 253
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
18-199 6.36e-27

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: 102.92  E-value: 6.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGV----NPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQLLPYMENRR-GAV 91
Cdd:cd05349   56 VRDRDQVQAMIEEAKNHFGPVDTIVNNALIdfpfDPDQRKTFDTIDwEDYQQQLEGAVKGALNLLQAVLPDFKERGsGRV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  92 ILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK-TDFSKVfhGNESLWKNFKEHHQLQRIG 170
Cdd:cd05349  136 INIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKvTDASAA--TPKEVFDAIAQTTPLGKVT 213
                        170       180
                 ....*....|....*....|....*....
gi 767979509 171 ESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05349  214 TPQDIADAVLFFASPWARAVTGQNLVVDG 242
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
25-153 8.10e-27

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: 102.31  E-value: 8.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPV 103
Cdd:cd05374   62 KAAVKEVIERFGRIDVLVNNAGYG-LFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGRIVNVSSVAGLVPT 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509 104 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGN 153
Cdd:cd05374  141 PFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGS 190
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
16-199 9.31e-27

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: 102.53  E-value: 9.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVIL 93
Cdd:cd05326   58 CDVTVEADVRAAVDTAVARFGRLDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMiPAKKGSIVS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF------------SKVFHGNESLwknfk 161
Cdd:cd05326  138 VASVAGVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLltagfgvedeaiEEAVRGAANL----- 212
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 162 ehhqLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05326  213 ----KGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDG 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
11-199 9.61e-27

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: 102.41  E-value: 9.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGT--SEQIWDKILSVNVKSpALLLSQ--LLPYMEN 86
Cdd:cd08930   54 VIALELDITSKESIKELIESYLEKFGRIDILINNAYPSPKVWGSRFEefPYEQWNEVLNVNLGG-AFLCSQafIKLFKKQ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  87 RRGAVILVSSIAA--------------YNPVValgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTdfskvFHG 152
Cdd:cd08930  133 GKGSIINIASIYGviapdfriyentqmYSPVE----YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILN-----NQP 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 153 NESLwKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08930  204 SEFL-EKYTKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDG 249
PRK12828 PRK12828
short chain dehydrogenase; Provisional
11-199 2.24e-26

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 101.03  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKA-----EDREQLVAKALEHCGGVDFLVCSAGVnpLVGSTL--GTSEQiWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK12828  51 VPADALRIGGIdlvdpQAARRAVDEVNRQFGRLDALVNIAGA--FVWGTIadGDADT-WDRMYGVNVKTTLNASKAALPA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 M-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT----------DFSkvfhg 152
Cdd:PRK12828 128 LtASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTppnradmpdaDFS----- 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 153 neslwknfkehhqlqRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12828 203 ---------------RWVTPEQIAAVIAFLLSDEAQAITGASIPVDG 234
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
25-199 3.40e-26

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: 100.43  E-value: 3.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPV 103
Cdd:cd05357   66 ADLVAAAFRAFGRCDVLVNNASAFY-PTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLaGSRNGSIINIIDAMTDRPL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 104 VALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIktdfSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLC 183
Cdd:cd05357  145 TGYFAYCMSKAALEGLTRSAALELAPN-IRVNGIAPGLI----LLPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLL 219
                        170
                 ....*....|....*.
gi 767979509 184 SPDasYVNGENIAVAG 199
Cdd:cd05357  220 DSN--YITGQIIKVDG 233
PRK07890 PRK07890
short chain dehydrogenase; Provisional
2-199 6.77e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 100.42  E-value: 6.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQL- 80
Cdd:PRK07890  47 AEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLG-TLRLTQAf 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGII-----KTDFSKVFHGN-- 153
Cdd:PRK07890 126 TPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIwgdplKGYFRHQAGKYgv 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767979509 154 --ESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07890 206 tvEQIYAETAANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNC 253
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
27-199 1.15e-25

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: 100.06  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  27 LVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnrRGAVIL-VSSIAAYNPVVA 105
Cdd:cd05355   95 LVKEVVKEFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIInTTSVTAYKGSPH 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 106 LGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVfHGNEslwKNFKEHHQ---LQRIGESEDCAGIVSFL 182
Cdd:cd05355  173 LLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPS-SFPE---EKVSEFGSqvpMGRAGQPAEVAPAYVFL 248
                        170
                 ....*....|....*..
gi 767979509 183 CSPDASYVNGENIAVAG 199
Cdd:cd05355  249 ASQDSSYVTGQVLHVNG 265
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-199 1.24e-25

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 99.59  E-value: 1.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSpALLLSQLL 81
Cdd:PRK12481  48 AQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILINNAGI-IRRQDLLEFGNKDWDDVININQKT-VFFLSQAV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM---ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWK 158
Cdd:PRK12481 126 AKQfvkQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNE 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767979509 159 NFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12481 206 AILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDG 246
PRK08589 PRK08589
SDR family oxidoreductase;
18-199 1.37e-25

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 99.85  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSI 97
Cdd:PRK08589  63 ISDEQQVKDFASEIKEQFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSF 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  98 AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHG--NESLWKNFKEHHQ----LQRIGE 171
Cdd:PRK08589 143 SGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGtsEDEAGKTFRENQKwmtpLGRLGK 222
                        170       180
                 ....*....|....*....|....*...
gi 767979509 172 SEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08589 223 PEEVAKLVVFLASDDSSFITGETIRIDG 250
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
13-201 1.46e-25

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: 99.08  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  13 GIVCHVGKAEDREQlVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAV 91
Cdd:cd05368   47 GITTRVLDVTDKEQ-VAALAKEEGRIDVLFNCAGFVH-HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  92 ILVSSIAA-YNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT----DFSKVFHGNESLWKNFKEHHQL 166
Cdd:cd05368  125 INMSSVASsIKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTpsleERIQAQPDPEEALKAFAARQPL 204
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 167 QRIGESEDCAGIVSFLCSPDASYVNG-ENIAVAGYS 201
Cdd:cd05368  205 GRLATPEEVAALAVYLASDESAYVTGtAVVIDGGWS 240
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-199 1.48e-25

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 99.27  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:PRK12745  45 QELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRG-------AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-------- 145
Cdd:PRK12745 125 AKRMLAQPEpeelphrSIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDmtapvtak 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767979509 146 FSKVFHGNESLWKnfkehhqlqRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12745 205 YDALIAKGLVPMP---------RWGEPEDVARAVAALASGDLPYSTGQAIHVDG 249
PRK07063 PRK07063
SDR family oxidoreductase;
5-199 1.50e-25

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 99.35  E-value: 1.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   5 QGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM 84
Cdd:PRK07063  54 DVAGARVLAVPADVTDAASVAAAVAAAEEAFGPLDVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 -ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvfhgNESLWKNFKEH 163
Cdd:PRK07063 133 vERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQL------TEDWWNAQPDP 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 164 ----------HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07063 207 aaaraetlalQPMKRIGRPEEVAMTAVFLASDEAPFINATCITIDG 252
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
28-199 2.42e-25

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 98.11  E-value: 2.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYnpvVAL 106
Cdd:PRK06550  58 LEPLFDWVPSVDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMlERKSGIIINMCSIASF---VAG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 107 G---VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-----DFSkvfhgNESLWKNFKEHHQLQRIGESEDCAGI 178
Cdd:PRK06550 135 GggaAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTpmtaaDFE-----PGGLADWVARETPIKRWAEPEEVAEL 209
                        170       180
                 ....*....|....*....|.
gi 767979509 179 VSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06550 210 TLFLASGKADYMQGTIVPIDG 230
PRK06484 PRK06484
short chain dehydrogenase; Validated
13-199 3.24e-25

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 101.85  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  13 GIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGA 90
Cdd:PRK06484  55 ALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGVtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMiEQGHGA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskVFHGNESLWKnFKEHHQLQRI 169
Cdd:PRK06484 135 AIVnVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQ---MVAELERAGK-LDPSAVRSRI 210
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767979509 170 -----GESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06484 211 plgrlGRPEEIAEAVFFLASDQASYITGSTLVVDG 245
PRK07060 PRK07060
short chain dehydrogenase; Provisional
25-203 3.32e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 98.25  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNP 102
Cdd:PRK07060  65 DAAIRAALAAAGAFDGLVNCAGIASL-ESALDMTAEGFDRVMAVNARGAALVARHVARAMiaAGRGGSIVNVSSQAALVG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 103 VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkvfhgnESLWKN------FKEHHQLQRIGESEDCA 176
Cdd:PRK07060 144 LPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMA------AEAWSDpqksgpMLAAIPLGRFAEVDDVA 217
                        170       180
                 ....*....|....*....|....*...
gi 767979509 177 GIVSFLCSPDASYVNGENIAV-AGYSTR 203
Cdd:PRK07060 218 APILFLLSDAASMVSGVSLPVdGGYTAR 245
PRK07774 PRK07774
SDR family oxidoreductase;
2-199 3.63e-25

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 98.28  E-value: 3.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnpLVG----STLGTSEQIWDKILSVNVKSPALLL 77
Cdd:PRK07774  48 KQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDYLVNNAAI--YGGmkldLLITVPWDYYKKFMSVNLDGALVCT 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  78 SQLLPYMENRRGAVIL-VSSIAAYnpvVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNEsL 156
Cdd:PRK07774 126 RAVYKHMAKRGGGAIVnQSSTAAW---LYSNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKE-F 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 157 WKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07774 202 VADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQIFNVDG 244
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
27-203 3.88e-25

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: 98.04  E-value: 3.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  27 LVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEqiWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVA 105
Cdd:cd09761   65 VVYAMLEKLGRIDVLVNNAARgSKGILSSLLLEE--WDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 106 LGVYNVSKTALLGLTRTLALELAPkDIRVNCVVPGIIKTDFSKVFHGnESLWKNFKEHHQLQRIGESEDCAGIVSFLCSP 185
Cdd:cd09761  143 SEAYAASKGGLVALTHALAMSLGP-DIRVNCISPGWINTTEQQEFTA-APLTQEDHAQHPAGRVGTPKDIANLVLFLCQQ 220
                        170
                 ....*....|....*...
gi 767979509 186 DASYVNGENIAVAGYSTR 203
Cdd:cd09761  221 DAGFITGETFIVDGGMTK 238
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
2-199 3.90e-25

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: 98.30  E-value: 3.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd05337   44 AEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLVNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYM-------ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS-KVFHG 152
Cdd:cd05337  124 ARRMveqpdrfDGPHRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTaPVKEK 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 153 NESLWKnfKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05337  204 YDELIA--AGLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDG 248
PRK05867 PRK05867
SDR family oxidoreductase;
3-201 4.10e-25

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 98.18  E-value: 4.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAG---VNPLVGSTLGTSEQIWDkilsVNVKSPALLLSQ 79
Cdd:PRK05867  52 EIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCNAGiitVTPMLDMPLEEFQRLQN----TNVTGVFLTAQA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  80 LLPYM--ENRRGAVILVSSIAAY--NPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNES 155
Cdd:PRK05867 128 AAKAMvkQGQGGVIINTASMSGHiiNVPQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQP 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 156 LWknfKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK05867 208 LW---EPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDIVIdGGYT 251
PRK12743 PRK12743
SDR family oxidoreductase;
2-199 9.42e-25

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 97.41  E-value: 9.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNplVGST-LGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:PRK12743  45 EEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDVLVNNAGAM--TKAPfLDMDFDEWRKIFTVDVDGAFLCSQIA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfHGNESLWK 158
Cdd:PRK12743 123 ARHMvkQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNG--MDDSDVKP 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767979509 159 NFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12743 201 DSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDG 241
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
16-199 1.50e-24

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: 96.60  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVN-PLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME----NRRGA 90
Cdd:cd05323   56 CDVTSWEQLAAAFKKAIEKFGRVDILINNAGILdEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDknkgGKGGV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPK-DIRVNCVVPGIIKTDfskVFHGNESLWKNFKEHHQLQri 169
Cdd:cd05323  136 IVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTP---LLPDLVAKEAEMLPSAPTQ-- 210
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767979509 170 gESEDCA-GIVSFLCSPDAsyvNGENIAVAG 199
Cdd:cd05323  211 -SPEVVAkAIVYLIEDDEK---NGAIWIVDG 237
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
26-201 1.88e-24

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: 96.39  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  26 QLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--GAVILVSSIAAYNPV 103
Cdd:cd05351   65 DATEEALGSVGPVDLLVNNAAV-AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpGSIVNVSSQASQRAL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 104 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLC 183
Cdd:cd05351  144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLL 223
                        170
                 ....*....|....*....
gi 767979509 184 SPDASYVNGENIAV-AGYS 201
Cdd:cd05351  224 SDKSSMTTGSTLPVdGGFL 242
PRK07478 PRK07478
short chain dehydrogenase; Provisional
6-192 2.21e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 96.15  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGIVCHVGKAEDreqLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME 85
Cdd:PRK07478  55 GEAVALAGDVRDEAYAKA---LVALAVERFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAML 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRR-GAVILVSSIAAYN---PVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFK 161
Cdd:PRK07478 132 ARGgGSLIFTSTFVGHTagfPGMA--AYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVA 209
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767979509 162 EHHQLQRIGESEDCAGIVSFLCSPDASYVNG 192
Cdd:PRK07478 210 GLHALKRMAQPEEIAQAALFLASDAASFVTG 240
PRK05875 PRK05875
short chain dehydrogenase; Provisional
22-199 3.46e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 96.02  E-value: 3.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  22 EDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAY 100
Cdd:PRK05875  71 DQVARAVDAATAWHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELvRGGGGSFVGISSIAAS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 101 NPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVS 180
Cdd:PRK05875 151 NTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAM 230
                        170
                 ....*....|....*....
gi 767979509 181 FLCSPDASYVNGENIAVAG 199
Cdd:PRK05875 231 FLLSDAASWITGQVINVDG 249
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-199 3.87e-24

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 95.71  E-value: 3.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSpALLLSQL 80
Cdd:PRK08993  49 IEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDILVNNAGL-IRREDAIEFSEKDWDDVMNLNIKS-VFFMSQA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYM---ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLW 157
Cdd:PRK08993 127 AAKHfiaQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRS 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08993 207 AEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDG 248
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
3-199 4.12e-24

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: 95.68  E-value: 4.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP 82
Cdd:cd08945   46 ELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVLK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 ---YMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS-KVFHGNESLWK 158
Cdd:cd08945  125 aggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAaSVREHYADIWE 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 159 --------NFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08945  205 vsteeafdRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVTAQALNVCG 253
PRK07814 PRK07814
SDR family oxidoreductase;
2-199 4.50e-24

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 95.62  E-value: 4.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAG---VNPLvgstLGTSEQIWDKILSVNVKSPALLLS 78
Cdd:PRK07814  52 EQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDIVVNNVGgtmPNPL----LSTSTKDLADAFTFNVATAHALTV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRR--GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTDFSKVFHGNESL 156
Cdd:PRK07814 128 AAVPLMLEHSggGSVINISSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAANDEL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 157 WKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07814 207 RAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDG 249
PRK06500 PRK06500
SDR family oxidoreductase;
8-199 6.66e-24

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 95.02  E-value: 6.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgSTLG----TSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK06500  51 GESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINAGV-----AKFApledWDEAMFDRSFNTNVKGPYFLIQALLPL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MeNRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-FSKVfhG-----NESLW 157
Cdd:PRK06500 126 L-ANPASIVLNGSINAHIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPlYGKL--GlpeatLDAVA 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06500 203 AQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEIIVDG 244
PRK06198 PRK06198
short chain dehydrogenase; Provisional
2-192 7.38e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 95.07  E-value: 7.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK06198  49 AELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDALVNAAGL-TDRGTILDTSPELFDRHFAVNVRAPFFLMQEAI 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMENRR--GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD----FSKVFHGNES 155
Cdd:PRK06198 128 KLMRRRKaeGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedrIQREFHGAPD 207
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 156 LWKNFKEHHQ-LQRIGESEDCAGIVSFLCSPDASYVNG 192
Cdd:PRK06198 208 DWLEKAAATQpFGRLLDPDEVARAVAFLLSDESGLMTG 245
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
2-199 7.92e-24

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 94.79  E-value: 7.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLL 81
Cdd:PRK08643  44 DKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQF-DKVYNINVGGVIWGIQAAQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM--ENRRGAVILVSSIAAY--NPvvALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT----DFSKVFHGN 153
Cdd:PRK08643 123 EAFkkLGHGGKIINATSQAGVvgNP--ELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTpmmfDIAHQVGEN 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 154 -----ESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08643 201 agkpdEWGMEQFAKDITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIVDG 251
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-202 8.94e-24

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 94.87  E-value: 8.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLP 82
Cdd:PRK08226  48 ELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRL-GSFLDMSDEDRDFHIDINIKGVWNVTKAVLP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 YM-ENRRGAVILVSSIAAyNPVVALG--VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF------HGN 153
Cdd:PRK08226 127 EMiARKDGRIVMMSSVTG-DMVADPGetAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpEDP 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 154 ESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:PRK08226 206 ESVLTEMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGGST 254
PRK06181 PRK06181
SDR family oxidoreductase;
1-148 1.09e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 94.66  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgSTLGTSEQIWD-----KILSVNVKSPAL 75
Cdd:PRK06181  42 AQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDILVNNAGI-----TMWSRFDELTDlsvfeRVMRVNYLGAVY 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979509  76 LLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:PRK06181 117 CTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRK 189
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
16-199 1.63e-23

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: 93.70  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNplVGSTLGT-SEQIWDKILSVNVKSPALLLSQLLPYMenRRGA---- 90
Cdd:cd08942   61 ADLSSEEGIEALVARVAERSDRLDVLVNNAGAT--WGAPLEAfPESGWDKVMDINVKSVFFLTQALLPLL--RAAAtaen 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 ---VILVSSIAAynpVVALGV----YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEH 163
Cdd:cd08942  137 parVINIGSIAG---IVVSGLenysYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKS 213
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08942  214 IPLGRWGRPEDMAGLAIMLASRAGAYLTGAVIPVDG 249
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
2-147 3.23e-23

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: 92.57  E-value: 3.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:cd08929   39 AAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAP 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979509  82 PYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:cd08929  119 ALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFA 184
PRK07074 PRK07074
SDR family oxidoreductase;
11-192 4.74e-23

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 92.91  E-value: 4.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRG 89
Cdd:PRK07074  51 FVPVACDLTDAASLAAALANAAAERGPVDVLVANAGAARAA-SLHDTTPASWRADNALNLEAAYLCVEAVLEGMlKRSRG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  90 AVILVSSIaayNPVVALG--VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-FSKVFHGNESLWKNFKEHHQL 166
Cdd:PRK07074 130 AVVNIGSV---NGMAALGhpAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQaWEARVAANPQVFEELKKWYPL 206
                        170       180
                 ....*....|....*....|....*.
gi 767979509 167 QRIGESEDCAGIVSFLCSPDASYVNG 192
Cdd:PRK07074 207 QDFATPDDVANAVLFLASPAARAITG 232
PRK08339 PRK08339
short chain dehydrogenase; Provisional
9-199 4.93e-23

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 93.00  E-value: 4.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   9 LSVAGIVCHVGKAEDREQLVaKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR 88
Cdd:PRK08339  58 VDVSYIVADLTKREDLERTV-KELKNIGEPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  89 -GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF------SKVFHGNESLWKNFK 161
Cdd:PRK08339 136 fGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRviqlaqDRAKREGKSVEEALQ 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767979509 162 EHHQ---LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08339 216 EYAKpipLGRLGEPEEIGYLVAFLASDLGSYINGAMIPVDG 256
PRK05717 PRK05717
SDR family oxidoreductase;
28-203 5.41e-23

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 92.64  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVAL 106
Cdd:PRK05717  75 VAEVLGQFGRLDALVCNAAIADPHNTTLESLSlAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDT 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 107 GVYNVSKTALLGLTRTLALELAPkDIRVNCVVPGIIKTDfSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPD 186
Cdd:PRK05717 155 EAYAASKGGLLALTHALAISLGP-EIRVNAVSPGWIDAR-DPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQ 232
                        170
                 ....*....|....*..
gi 767979509 187 ASYVNGENIAVAGYSTR 203
Cdd:PRK05717 233 AGFVTGQEFVVDGGMTR 249
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-199 1.01e-22

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 94.91  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK08324 463 AAELGGPDRALGVACDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAI-SGPIEETSDEDWRRSFDVNATGHFLVAREAV 541
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYME--NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfSKVFHG------- 152
Cdd:PRK08324 542 RIMKaqGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVRG-SGIWTGewieara 620
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767979509 153 ------NESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08324 621 aayglsEEELEEFYRARNLLKREVTPEDVAEAVVFLASGLLSKTTGAIITVDG 673
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
2-184 1.04e-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: 91.27  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVgsTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:cd08932   38 AALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIgRPTT--LREGSDAELEAHFSINVIAPAELTRAL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvfhgneSLWKN 159
Cdd:cd08932  116 LPALrEAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM--------AQGLT 187
                        170       180
                 ....*....|....*....|....*
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCS 184
Cdd:cd08932  188 LVGAFPPEEMIQPKDIANLVRMVIE 212
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
6-192 1.13e-22

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 91.71  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGivcHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:PRK08936  57 GEAIAVKG---DVTVESDVVNLIQTAVKEFGTLDVMINNAGIENAVPSHEMSLED-WNKVINTNLTGAFLGSREAIKYFv 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 -ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEH 163
Cdd:PRK08936 133 eHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESM 212
                        170       180
                 ....*....|....*....|....*....
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNG 192
Cdd:PRK08936 213 IPMGYIGKPEEIAAVAAWLASSEASYVTG 241
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
12-199 1.20e-22

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 91.40  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  12 AGIVCHVGKAEDREQLVAKALEHCGGV-DFLVCSAGVNPLVGStlgtseqiwDKILSVNVKSPALLLSQLLPYME-NRRG 89
Cdd:cd05328   34 ADVIADLSTPEGRAAAIADVLARCSGVlDGLVNCAGVGGTTVA---------GLVLKVNYFGLRALMEALLPRLRkGHGP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  90 AVILVSSIAAYNP------------------VVALG---------VYNVSKTALLGLTRTLALE-LAPKDIRVNCVVPGI 141
Cdd:cd05328  105 AAVVVSSIAGAGWaqdklelakalaagtearAVALAehagqpgylAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGP 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979509 142 IKT----DFSKVFHGNESLWKNFKehhQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05328  185 VETpilqAFLQDPRGGESVDAFVT---PMGRRAEPDEIAPVIAFLASDAASWINGANLFVDG 243
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
14-202 1.56e-22

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 91.24  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCS---AGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGA 90
Cdd:COG0623   60 LPCDVTDDEQIDALFDEIKEKWGKLDFLVHSiafAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLM-NEGGS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAynpVVALGVYN---VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFHGNEslwknf 160
Cdd:COG0623  139 IVTLTYLGA---ERVVPNYNvmgVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTlaasgipGFDKLLDYAE------ 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 161 kEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:COG0623  210 -ERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVdGGYHI 251
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-182 2.26e-22

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 90.94  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLsvaGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYME 85
Cdd:PRK06077  56 GEGI---GVLADVSTREGCETLAKATIDRYGVADILVNNAGLG-LFSPFLNVDDKLIDKHISTDFKS-VIYCSQELAKEM 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTDFS----KVFHGNEslwKNFK 161
Cdd:PRK06077 131 REGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGeslfKVLGMSE---KEFA 206
                        170       180
                 ....*....|....*....|..
gi 767979509 162 EHHQL-QRIGESEDCAGIVSFL 182
Cdd:PRK06077 207 EKFTLmGKILDPEEVAEFVAAI 228
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
14-202 4.06e-22

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: 89.95  E-value: 4.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGA 90
Cdd:cd05372   57 LPCDVSNDEEIKELFAEVKKDWGKLDGLVHSIAFAPkvqLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIM-NPGGS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIG 170
Cdd:cd05372  136 IVTLSYLGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKMLEYSEQRAPLGRNV 215
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767979509 171 ESEDCAGIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:cd05372  216 TAEEVGNTAAFLLSDLSSGITGEIIYVdGGYHI 248
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
23-199 6.03e-22

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 89.59  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQLVA---KALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL-PYMENRRGAVILVSSIA 98
Cdd:PRK12936  63 DRDEVKAlgqKAEADLEGVDILVNNAGITK-DGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  99 AY--NPVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFhgNESLWKNFKEHHQLQRIGESEDCA 176
Cdd:PRK12936 142 GVtgNPGQA--NYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKL--NDKQKEAIMGAIPMKRMGTGAEVA 217
                        170       180
                 ....*....|....*....|...
gi 767979509 177 GIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12936 218 SAVAYLASSEAAYVTGQTIHVNG 240
PRK12747 PRK12747
short chain dehydrogenase; Provisional
39-201 7.97e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 89.36  E-value: 7.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  39 DFLVCSAGVNPlvGSTLG-TSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRgaVILVSSIAAYNPVVALGVYNVSKTAL 116
Cdd:PRK12747  90 DILINNAGIGP--GAFIEeTTEQFFDRMVSVNAKAPFFIIQQALSRLrDNSR--IINISSAATRISLPDFIAYSMTKGAI 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 117 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIA 196
Cdd:PRK12747 166 NTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLGEVEDIADTAAFLASPDSRWVTGQLID 245

                 ....*
gi 767979509 197 VAGYS 201
Cdd:PRK12747 246 VSGGS 250
PRK07326 PRK07326
SDR family oxidoreductase;
11-182 8.42e-22

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.91  E-value: 8.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA 90
Cdd:PRK07326  56 VLGLAADVRDEADVQRAVDAIVAAFGGLDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGY 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKnfkehhqLQrig 170
Cdd:PRK07326 135 IINISSLAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWK-------IQ--- 204
                        170
                 ....*....|..
gi 767979509 171 eSEDCAGIVSFL 182
Cdd:PRK07326 205 -PEDIAQLVLDL 215
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
14-199 1.58e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 88.69  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVI 92
Cdd:PRK06463  56 IKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLM-PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKlSKNGAIV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNpVVALGV--YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS---KVFHGNESLWKNFKEHHQLQ 167
Cdd:PRK06463 135 NIASNAGIG-TAAEGTtfYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgKSQEEAEKLRELFRNKTVLK 213
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767979509 168 RIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06463 214 TTGKPEDIANIVLFLASDDARYITGQVIVADG 245
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
3-199 1.98e-21

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 88.52  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP 82
Cdd:PRK12935  50 ELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDILVNNAGITR-DRTFKKLNREDWERVIDVNLSSVFNTTSAVLP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 YM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskVFHGNESLWKNFK 161
Cdd:PRK12935 129 YItEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM--VAEVPEEVRQKIV 206
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 162 EHHQLQRIGESEDCAGIVSFLCSpDASYVNGENIAVAG 199
Cdd:PRK12935 207 AKIPKKRFGQADEIAKGVVYLCR-DGAYITGQQLNING 243
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
14-203 2.33e-21

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 88.53  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVN-P--LV-----GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM- 84
Cdd:PRK06171  54 VPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINiPrlLVdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMv 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGII-KTDFSKVFHGNESLWKNFKEH 163
Cdd:PRK06171 134 KQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLRTPEYEEALAYTRGITV 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767979509 164 HQLQ------------RIGESEDCAGIVSFLCSPDASYVNGENIAVAGYSTR 203
Cdd:PRK06171 214 EQLRagytktstiplgRSGKLSEVADLVCYLLSDRASYITGVTTNIAGGKTR 265
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
21-199 2.34e-21

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 88.02  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  21 AEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAA 99
Cdd:cd05361   56 EQKPEELVDAVLQAGGAIDVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGsIIFITSAVP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 100 YNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvFHGNESLWKNFKEHHQ-------LQRIGES 172
Cdd:cd05361  136 KKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSP----TYFPTSDWENNPELRErvkrdvpLGRLGRP 211
                        170       180
                 ....*....|....*....|....*..
gi 767979509 173 EDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05361  212 DEMGALVAFLASRRADPITGQFFAFAG 238
PRK06128 PRK06128
SDR family oxidoreductase;
26-199 4.85e-21

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 88.38  E-value: 4.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  26 QLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENrrGA-VILVSSIAAYNPVV 104
Cdd:PRK06128 123 QLVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GAsIINTGSIQSYQPSP 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 105 ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCS 184
Cdd:PRK06128 201 TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLAS 280
                        170
                 ....*....|....*
gi 767979509 185 PDASYVNGENIAVAG 199
Cdd:PRK06128 281 QESSYVTGEVFGVTG 295
PRK06484 PRK06484
short chain dehydrogenase; Validated
25-199 5.50e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.91  E-value: 5.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMenRRGAVIL-VSSIAAYNPV 103
Cdd:PRK06484 331 ESAFAQIQARWGRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVnLGSIASLLAL 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 104 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-DFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFL 182
Cdd:PRK06484 409 PPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETpAVLALKASGRADFDSIRRRIPLGRLGDPEEVAEAIAFL 488
                        170
                 ....*....|....*..
gi 767979509 183 CSPDASYVNGENIAVAG 199
Cdd:PRK06484 489 ASPAASYVNGATLTVDG 505
PRK06124 PRK06124
SDR family oxidoreductase;
2-204 6.25e-21

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 87.08  E-value: 6.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGTSEQIwdkiLSVNVKSPALLLS 78
Cdd:PRK06124  53 AALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDILVNNVGArdrRPLAELDDAAIRAL----LETDLVAPILLSR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRR-GAVILVSSIAAynPVVALG--VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNES 155
Cdd:PRK06124 129 LAAQRMKRQGyGRIIAITSIAG--QVARAGdaVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPA 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509 156 LWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYSTRL 204
Cdd:PRK06124 207 VGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVdGGYSVHF 256
PRK07069 PRK07069
short chain dehydrogenase; Validated
22-199 6.64e-21

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 87.07  E-value: 6.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  22 EDREQ-LVAKALEHCGGVDFLVCSAGVnplvGStLGTSEQI----WDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVS 95
Cdd:PRK07069  63 EAQWQaLLAQAADAMGGLSVLVNNAGV----GS-FGAIEQIeldeWRRVMAINVESIFLGCKHALPYLrASQPASIVNIS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  96 SIAAYNPVVALGVYNVSKTALLGLTRTLALELAPK--DIRVNCVVPGIIKTD----FSKVFhGNESLWKNFKEHHQLQRI 169
Cdd:PRK07069 138 SVAAFKAEPDYTAYNASKAAVASLTKSIALDCARRglDVRCNSIHPTFIRTGivdpIFQRL-GEEEATRKLARGVPLGRL 216
                        170       180       190
                 ....*....|....*....|....*....|
gi 767979509 170 GESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07069 217 GEPDDVAHAVLYLASDESRFVTGAELVIDG 246
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
2-148 1.03e-20

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: 85.75  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:cd05324   43 EKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALL 122
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509  82 PYMENRRGA-VILVSSIAAynpVVALGvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:cd05324  123 PLLKKSPAGrIVNVSSGLG---SLTSA-YGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGG 186
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
18-176 1.06e-20

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: 86.49  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSS 96
Cdd:cd05332   62 MSDLEDAEQVVEEALKLFGGLDILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLiERSQGSIVVVSS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNE--SLWKNFKEhhqlQRIGES-E 173
Cdd:cd05332  141 IAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDgsMSAKMDDT----TANGMSpE 216

                 ...
gi 767979509 174 DCA 176
Cdd:cd05332  217 ECA 219
PRK06701 PRK06701
short chain dehydrogenase; Provisional
25-199 1.18e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 87.01  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVV 104
Cdd:PRK06701 112 KDAVEETVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK-QGSAIINTGSITGYEGNE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 105 ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-----DFS--KVfhgneslwKNFKEHHQLQRIGESEDCAG 177
Cdd:PRK06701 191 TLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTplipsDFDeeKV--------SQFGSNTPMQRPGQPEELAP 262
                        170       180
                 ....*....|....*....|..
gi 767979509 178 IVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06701 263 AYVFLASPDSSYITGQMLHVNG 284
PRK07985 PRK07985
SDR family oxidoreductase;
27-199 1.20e-20

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 86.97  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  27 LVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnrRGA-VILVSSIAAYNPVVA 105
Cdd:PRK07985 118 LVHEAHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP--KGAsIITTSSIQAYQPSPH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 106 LGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSP 185
Cdd:PRK07985 196 LLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQ 275
                        170
                 ....*....|....
gi 767979509 186 DASYVNGENIAVAG 199
Cdd:PRK07985 276 ESSYVTAEVHGVCG 289
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
3-199 2.32e-20

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 85.58  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP 82
Cdd:cd08940   47 LAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALP 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 YMENRR-GAVIlvsSIAAYNPVVAL---GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKV--------- 149
Cdd:cd08940  126 HMKKQGwGRII---NIASVHGLVASankSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKqisalaqkn 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 150 FHGNESLWKN-FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08940  203 GVPQEQAARElLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDG 253
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
2-144 3.40e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 85.32  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAG---VNPLVgsTLGTSEqiWDKILSVNVKSPALLLS 78
Cdd:PRK12429  46 EALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILVNNAGiqhVAPIE--DFPTEK--WKKMIAIMLDGAFLTTK 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979509  79 QLLPYMENRRGAVILvsSIAAYNPVVAL---GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK12429 122 AALPIMKAQGGGRII--NMASVHGLVGSagkAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK12746 PRK12746
SDR family oxidoreductase;
38-199 6.21e-20

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 84.32  E-value: 6.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  38 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVVALGVYNVSKTALL 117
Cdd:PRK12746  91 IDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSIAYGLSKGALN 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 118 GLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLwKNFKEHHQL-QRIGESEDCAGIVSFLCSPDASYVNGENIA 196
Cdd:PRK12746 169 TMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEI-RNFATNSSVfGRIGQVEDIADAVAFLASSDSRWVTGQIID 247

                 ...
gi 767979509 197 VAG 199
Cdd:PRK12746 248 VSG 250
PRK06057 PRK06057
short chain dehydrogenase; Provisional
16-199 6.33e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 84.40  E-value: 6.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVIL 93
Cdd:PRK06057  58 TDVTDEDAVNALFDTAAETYGSVDIAFNNAGISPPEdDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMvRQGKGSIIN 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 VSSIAAYNPVVALGV-YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK-VFHGNESLWKNFKEHHQLQRIGE 171
Cdd:PRK06057 138 TASFVAVMGSATSQIsYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQeLFAKDPERAARRLVHVPMGRFAE 217
                        170       180
                 ....*....|....*....|....*...
gi 767979509 172 SEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06057 218 PEEIAAAVAFLASDDASFITASTFLVDG 245
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-199 9.10e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 83.92  E-value: 9.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTlgtsEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK07067  50 IGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAALfdmAPILDIS----RDSYDRLFAVNVKGLFFLMQAVARH 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 M--ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFK 161
Cdd:PRK07067 126 MveQGRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDALFARYENRP 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 162 EHHQLQRIGES---------EDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07067 206 PGEKKRLVGEAvplgrmgvpDDLTGMALFLASADADYIVAQTYNVDG 252
PRK06523 PRK06523
short chain dehydrogenase; Provisional
18-199 1.01e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 83.80  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGvnplvGST------LGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGA 90
Cdd:PRK06523  58 LTTAEGCAAVARAVLERLGGVDILVHVLG-----GSSapaggfAALTDEEWQDELNLNLLAAVRLDRALLPGMiARGSGV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAA----YNPVVAlgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF------HGNESLWKNF 160
Cdd:PRK06523 133 IIHVTSIQRrlplPESTTA---YAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALaerlaeAAGTDYEGAK 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 161 KEHHQ------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06523 210 QIIMDslggipLGRPAEPEEVAELIAFLASDRAASITGTEYVIDG 254
PRK07454 PRK07454
SDR family oxidoreductase;
2-144 1.10e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 83.47  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK07454  48 AELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGM-AYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVL 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK07454 127 PGMrARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
2-144 2.37e-19

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: 82.69  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVN-PLVGSTLgTSEQIwDKILSVNVKSPALLLSQL 80
Cdd:cd08939   47 AEANASGQKVSYISADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISiPGLFEDL-TAEEF-ERGMDVNYFGSLNVAHAV 124
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979509  81 LPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:cd08939  125 LPLMkEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-201 2.39e-19

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 82.82  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV---CSAGVNPLvgSTLgTSEQIwDKILSVNVKSPALLLS 78
Cdd:PRK12748  60 EEIESYGVRCEHMEIDLSQPYAPNRVFYAVSERLGDPSILInnaAYSTHTRL--EEL-TAEQL-DKHYAVNVRATMLLSS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkvfhgNESLW 157
Cdd:PRK12748 136 AFAKQYDGKAgGRIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWI-----TEELK 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENI-AVAGYS 201
Cdd:PRK12748 211 HHLVPKFPQGRVGEPVDAARLIAFLVSEEAKWITGQVIhSEGGFS 255
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
14-199 4.64e-19

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 82.20  E-value: 4.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL 93
Cdd:cd08933   64 VPCDVTKEEDIKTLISVTVERFGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIIN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT----DFSKVFHGNESLWKNFKEHHQLQRI 169
Cdd:cd08933  144 LSSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTplweELAAQTPDTLATIKEGELAQLLGRM 223
                        170       180       190
                 ....*....|....*....|....*....|
gi 767979509 170 GESEDCAGIVSFLCSpDASYVNGENIAVAG 199
Cdd:cd08933  224 GTEAESGLAALFLAA-EATFCTGIDLLLSG 252
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
8-199 9.23e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 81.48  E-value: 9.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAG---VNPLVGstlgTSEQIWDKILSVNVKSPALLLSQLLPYM 84
Cdd:PRK13394  55 GGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDILVSNAGiqiVNPIEN----YSFADWKKMQAIHVDGAFLTTKAALKHM 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 --ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfhgneslwKNFKE 162
Cdd:PRK13394 131 ykDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVD---------KQIPE 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509 163 hhQLQRIGES---------------------EDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK13394 202 --QAKELGISeeevvkkvmlgktvdgvfttvEDVAQTVLFLSSFPSAALTGQSFVVSH 257
PRK07577 PRK07577
SDR family oxidoreductase;
16-199 9.30e-19

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 80.93  E-value: 9.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHcGGVDFLVCSAGV---NPLVGSTLGTSEQIWDkilsVNVKSPALLLSQLLPYMENRR-GAV 91
Cdd:PRK07577  48 CDLADIEQTAATLAQINEI-HPVDAIVNNVGIalpQPLGKIDLAALQDVYD----LNVRAAVQVTQAFLEGMKLREqGRI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  92 ILVSSIAAynpvvaLGV-----YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFH--GNEsLWKNFKEHH 164
Cdd:PRK07577 123 VNICSRAI------FGAldrtsYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRpvGSE-EEKRVLASI 195
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767979509 165 QLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07577 196 PMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDG 230
PRK07825 PRK07825
short chain dehydrogenase; Provisional
28-147 1.07e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 81.53  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPaLLLSQL-LPYM-ENRRGAVILVSSIAAYNPVVA 105
Cdd:PRK07825  69 LDAVEADLGPIDVLVNNAGVMP-VGPFLDEPDAVTRRILDVNVYGV-ILGSKLaAPRMvPRGRGHVVNVASLAGKIPVPG 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767979509 106 LGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:PRK07825 147 MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
8-184 1.30e-18

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 81.15  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV----NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK06200  51 GDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVGNAGIwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPkDIRVNCVVPGIIKTDfskvFHGNESLwkNFKEH 163
Cdd:PRK06200 131 LKASGGSMIFTLSNSSFYPGGGGPLYTASKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTD----LRGPASL--GQGET 203
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 H---------------QLQRIGESEDCAGIVSFLCS 184
Cdd:PRK06200 204 SisdspgladmiaaitPLQFAPQPEDHTGPYVLLAS 239
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
11-199 1.83e-18

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: 80.64  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRG 89
Cdd:cd05330   56 VLLIKADVSDEAQVEAYVDATVEQFGRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMrEQGSG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  90 AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-----DFSKVFHGN-ESLWKNFKEH 163
Cdd:cd05330  136 MIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTpmvegSLKQLGPENpEEAGEEFVSV 215
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05330  216 NPMKRFGEPEEVAAVVAFLLSDDAGYVNAAVVPIDG 251
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
21-199 1.86e-18

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 80.58  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  21 AEDREQLVAKAlehcGGVDFLVCSAGVN-------------PLVGSTLGTSEQIWDKILSVNVKSpALLLSQLL--PYME 85
Cdd:cd08935   70 ERAREEIVAQF----GTVDILINGAGGNhpdattdpehyepETEQNFFDLDEEGWEFVFDLNLNG-SFLPSQVFgkDMLE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNE-----SLWKNF 160
Cdd:cd08935  145 QKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPdgsytDRSNKI 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 161 KEHHQLQRIGESEDCAGIVSFLCSPDAS-YVNGENIAVAG 199
Cdd:cd08935  225 LGRTPMGRFGKPEELLGALLFLASEKASsFVTGVVIPVDG 264
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
8-184 3.50e-18

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 79.70  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQ----IWDKILSVNVKSPALLLSQLLPY 83
Cdd:cd05348   49 GDAVVGVEGDVRSLADNERAVARCVERFGKLDCFIGNAGIWDYSTSLVDIPEEkldeAFDELFHINVKGYILGAKAALPA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTD---FSKVFHGNESLWKN- 159
Cdd:cd05348  129 LYATEGSVIFTVSNAGFYPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDlrgPASLGQGETSISTPp 207
                        170       180
                 ....*....|....*....|....*....
gi 767979509 160 ----FKEHHQLQRIGESEDCAGIVSFLCS 184
Cdd:cd05348  208 lddmLKSILPLGFAPEPEDYTGAYVFLAS 236
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
18-199 5.38e-18

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: 79.20  E-value: 5.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAG---VNPLVGSTlgtsEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVI 92
Cdd:cd05363   58 VTDQASIDRCVAALVDRWGSIDILVNNAAlfdLAPIVDIT----RESYDRLFAINVSGTLFMMQAVARAMiaQGRGGKII 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF----SKVFHGNESLWKNFK-----EH 163
Cdd:cd05363  134 NMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHwdgvDAKFARYENRPRGEKkrlvgEA 213
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 164 HQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05363  214 VPFGRMGRAEDLTGMAIFLASTDADYIVAQTYNVDG 249
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
18-199 7.28e-18

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 78.98  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCG-GVDFLVCSAGV----NPLVGSTLGTSEqiWD---KILSVNVKSPALLLSQLLPYMENRR- 88
Cdd:PRK08642  61 VTDREQVQAMFATATEHFGkPITTVVNNALAdfsfDGDARKKADDIT--WEdfqQQLEGSVKGALNTIQAALPGMREQGf 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  89 GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK-TDFSKVfhGNESLWKNFKEHHQLQ 167
Cdd:PRK08642 139 GRIINIGTNLFQNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRtTDASAA--TPDEVFDLIAATTPLR 216
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767979509 168 RIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08642 217 KVTTPQEFADAVLFFASPWARAVTGQNLVVDG 248
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
6-161 1.53e-17

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: 77.67  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTlgtSEQIwDKILSVNVKSPALLLSQLLP 82
Cdd:cd05339   45 KAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVvsgKKLLELP---DEEI-EKTFEVNTLAHFWTTKAFLP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  83 YM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAP---KDIRVNCVVPGIIKTDFskvFHGNESLWK 158
Cdd:cd05339  121 DMlERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLELKAygkPGIKTTLVCPYFINTGM---FQGVKTPRP 197

                 ...
gi 767979509 159 NFK 161
Cdd:cd05339  198 LLA 200
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
2-199 1.59e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 77.87  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSPALLLS 78
Cdd:PRK08085  51 AKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAGIqrrHPF----TEFPEQEWNDVIAVNQTAVFLVSQ 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLW 157
Cdd:PRK08085 127 AVARYMVKRqAGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFT 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 158 KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK08085 207 AWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDG 248
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-148 1.96e-17

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 77.42  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK07666  49 EEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSIDILINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVL 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509  82 PYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:PRK07666 128 PSMiERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAV 195
PRK07062 PRK07062
SDR family oxidoreductase;
15-199 2.62e-17

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 77.39  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  15 VCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvgSTLG-TSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVI 92
Cdd:PRK07062  65 RCDVLDEADVAAFAAAVEARFGGVDMLVNNAGQGRV--STFAdTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIV 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-----FSKVFHGNESlWKNF------K 161
Cdd:PRK07062 143 CVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGqwrrrYEARADPGQS-WEAWtaalarK 221
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 162 EHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07062 222 KGIPLGRLGRPDEAARALFFLASPLSSYTTGSHIDVSG 259
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
38-149 3.31e-17

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 76.87  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  38 VDFLVCSAGVNPLVGSTLG-TSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 115
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLeTPEDELQDIINVNVMATLKMTRLILPGMvKRKKGAIVNISSFAGLIPTPLLATYSASKAF 158
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767979509 116 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKV 149
Cdd:cd05356  159 LDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKI 192
PRK06180 PRK06180
short chain dehydrogenase; Provisional
13-147 3.31e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 77.26  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  13 GIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgSTLGTSEQIWD----KILSVNVKSPALLLSQLLPYM-ENR 87
Cdd:PRK06180  54 ARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGY-----GHEGAIEESPLaemrRQFEVNVFGAVAMTKAVLPGMrARR 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  88 RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:PRK06180 129 RGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTDWA 188
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-195 3.42e-17

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 77.13  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQL 80
Cdd:PRK12859  60 QEELLKNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEEL-DKHYMVNVRATTLLSSQF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGA-VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkvfhgNESLWKN 159
Cdd:PRK12859 139 ARGFDKKSGGrIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWM-----TEEIKQG 213
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENI 195
Cdd:PRK12859 214 LLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQII 249
PRK06114 PRK06114
SDR family oxidoreductase;
4-199 5.02e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 76.74  E-value: 5.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKspALLLS---QL 80
Cdd:PRK06114  53 IEAAGRRAIQIAADVTSKADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQ-WQTVMDINLT--GVFLScqaEA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGAVILVSSIAAYnpVVALGV----YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK---VFHgn 153
Cdd:PRK06114 130 RAMLENGGGSIVNIASMSGI--IVNRGLlqahYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTrpeMVH-- 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 154 esLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06114 206 --QTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVDLLVDG 249
PRK07677 PRK07677
short chain dehydrogenase; Provisional
10-199 5.03e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 76.64  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  10 SVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVnVKSPALLLSQLLP--YMENR 87
Cdd:PRK07677  51 QVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAAGNFIC-PAEDLSVNGWNSVIDI-VLNGTFYCSQAVGkyWIEKG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  88 RGAVILvSSIAAYNPVVALGVYN--VSKTALLGLTRTLALELAPK-DIRVNCVVPGII-KTDfskvfhGNESLWKNFKEH 163
Cdd:PRK07677 129 IKGNII-NMVATYAWDAGPGVIHsaAAKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIeRTG------GADKLWESEEAA 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767979509 164 HQ------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07677 202 KRtiqsvpLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDG 243
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
5-195 1.22e-16

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: 75.40  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   5 QGEGLSVAGIVC-----HVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGT------SEQIWDKILSVNV--- 70
Cdd:cd05371   38 PGETVAKLGDNCrfvpvDVTSEKDVKAALALAKAKFGRLDIVVNCAGIAV-AAKTYNKkgqqphSLELFQRVINVNLigt 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  71 ----KSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:cd05371  117 fnviRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPL 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 147 SKvfhGNESLWKNF--KEHHQLQRIGESEDCAGIVSFLCspDASYVNGENI 195
Cdd:cd05371  197 LA---GLPEKVRDFlaKQVPFPSRLGDPAEYAHLVQHII--ENPYLNGEVI 242
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
2-199 1.36e-16

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 75.71  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVN--------------PLVGSTLGTSEQIWDKILS 67
Cdd:PRK08277  52 AEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCDILINGAGGNhpkattdnefheliEPTKTFFDLDEEGFEFVFD 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  68 VNvkspalLLSQLLPY------MENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 140
Cdd:PRK08277 132 LN------LLGTLLPTqvfakdMVGRKGGNIInISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPG 205
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509 141 IIKTDfskvfhGNESLWKN-----------FKEHHQLQRIGESEDCAGIVSFLCSPDAS-YVNGENIAVAG 199
Cdd:PRK08277 206 FFLTE------QNRALLFNedgslterankILAHTPMGRFGKPEELLGTLLWLADEKASsFVTGVVLPVDG 270
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
5-142 2.99e-16

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: 74.35  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   5 QGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM 84
Cdd:cd05338   60 EAAGGQALPIVVDVRDEDQVRALVEATVDQFGRLDILVNNAGAIWL-SLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHM 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979509  85 ENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGII 142
Cdd:cd05338  139 VKAGQGHILnISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
PRK05650 PRK05650
SDR family oxidoreductase;
16-153 4.40e-16

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 74.31  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVILV 94
Cdd:PRK05650  56 CDVRDYSQLTALAQACEEKWGGIDVIVNNAGVAS-GGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKrQKSGRIVNI 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979509  95 SSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGN 153
Cdd:PRK05650 135 ASMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFRGP 193
PRK07831 PRK07831
SDR family oxidoreductase;
11-197 5.38e-16

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 73.91  E-value: 5.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGvnpLVGSTL---GTSEQiWDKILSVNVKSPALLLSQLLPYMENR 87
Cdd:PRK07831  71 VEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAG---LGGQTPvvdMTDDE-WSRVLDVTLTGTFRATRAALRYMRAR 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  88 --RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF-SKVfhGNESLWKNFKEHH 164
Cdd:PRK07831 147 ghGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFlAKV--TSAELLDELAARE 224
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767979509 165 QLQRIGESEDCAGIVSFLCSPDASYVNGENIAV 197
Cdd:PRK07831 225 AFGRAAEPWEVANVIAFLASDYSSYLTGEVVSV 257
PRK12742 PRK12742
SDR family oxidoreductase;
23-192 1.24e-15

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 72.48  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQLVAkALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVILVSSIAAYN- 101
Cdd:PRK12742  62 DRDAVID-VVRKSGALDILVVNAGI-AVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSVNGDRm 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 102 PVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNF---KEHhqlqriGESEDCAGI 178
Cdd:PRK12742 139 PVAGMAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMMHSFmaiKRH------GRPEEVAGM 212
                        170
                 ....*....|....
gi 767979509 179 VSFLCSPDASYVNG 192
Cdd:PRK12742 213 VAWLAGPEASFVTG 226
PRK09730 PRK09730
SDR family oxidoreductase;
11-199 1.34e-15

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 72.58  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  11 VAGIVCHVGKA-------EDREQLVA--KALEHCGG-VDFLVCSAGVnPLVGSTLG--TSEQIwDKILSVNVKSPALLLS 78
Cdd:PRK09730  43 VNLITQAGGKAfvlqadiSDENQVVAmfTAIDQHDEpLAALVNNAGI-LFTQCTVEnlTAERI-NRVLSTNVTGYFLCCR 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYMENRRG----AVILVSSIAAynpvvALGV------YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfsk 148
Cdd:PRK09730 121 EAVKRMALKHGgsggAIVNVSSAAS-----RLGApgeyvdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTE--- 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767979509 149 vFH---GNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK09730 193 -MHasgGEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLAG 245
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
23-202 1.45e-15

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: 72.56  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQLVAKALEHCGGVDFLVCSAG----VNPLVGSTLGTSEQIWDKILSvnvksPALLLSQ-LLPYM-ENRRGAVILVSS 96
Cdd:cd08937   66 GAQGVVRAAVERFGRVDVLINNVGgtiwAKPYEHYEEEQIEAEIRRSLF-----PTLWCCRaVLPHMlERQQGVIVNVSS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNpvVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQ----------- 165
Cdd:cd08937  141 IATRG--IYRIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEKVWYQrivdqtldssl 218
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:cd08937  219 MGRYGTIDEQVRAILFLASDEASYITGTVLPVGGGDL 255
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
14-204 1.47e-15

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 72.49  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGvnplvGSTLGTSEQI--WDKILSVNVKSPALLLSQLLPYMenRRGA- 90
Cdd:PRK05786  58 VVGDVSSTESARNVIEKAAKVLNAIDGLVVTVG-----GYVEDTVEEFsgLEEMLTNHIKIPLYAVNASLRFL--KEGSs 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSI-AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfhgnESLWKnfkehhQLQRI 169
Cdd:PRK05786 131 IVLVSSMsGIYKASPDQLSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEP-----ERNWK------KLRKL 199
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 170 GES----EDCAGIVSFLCSPDASYVNGENIAVAGySTRL 204
Cdd:PRK05786 200 GDDmappEDFAKVIIWLLTDEADWVDGVVIPVDG-GARL 237
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
2-197 1.56e-15

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: 72.55  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEG-LSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTlgTSEqiWDKILSVNVKSPALLL 77
Cdd:cd05343   48 AECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQGVDVCINNAGLarpEPLLSGK--TEG--WKEMFDVNVLALSICT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  78 SQLLPYMENR---RGAVILVSSIAAYN--PVVALGVYNVSKTALLGLTRTLALEL--APKDIRVNCVVPGIIKTDFSKVF 150
Cdd:cd05343  124 REAYQSMKERnvdDGHIININSMSGHRvpPVSVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKL 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509 151 HGN--ESLWKNFKEHHQLQRigesEDCAGIVSF-LCSPDasYVNGENIAV 197
Cdd:cd05343  204 HDNdpEKAAATYESIPCLKP----EDVANAVLYvLSTPP--HVQIHDILL 247
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
22-144 1.67e-15

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: 72.36  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  22 EDREQLVAKALE-HCGGVDFLVCSAGVNplvGSTLGTSEQIWD--KILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSI 97
Cdd:cd05350   59 EERNQLVIAELEaELGGLDLVIINAGVG---KGTSLGDLSFKAfrETIDTNLLGAAAILEAALPQFrAKGRGHLVLISSV 135
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509  98 AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:cd05350  136 AALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDT 182
PRK08219 PRK08219
SDR family oxidoreductase;
28-145 2.56e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 71.50  E-value: 2.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALG 107
Cdd:PRK08219  62 IAAAVEQLGRLDVLVHNAGVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWG 140
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767979509 108 VYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIIKTD 145
Cdd:PRK08219 141 SYAASKFALRALADALREEEPGN-VRVTSVHPGRTDTD 177
PRK08628 PRK08628
SDR family oxidoreductase;
25-199 2.70e-15

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 71.91  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPLVGstLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVV 104
Cdd:PRK08628  71 RDAVEQTVAKFGRIDGLVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 105 ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT----DFSKVFHGNESLWKNFKEHHQL-QRIGESEDCAGIV 179
Cdd:PRK08628 149 GTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTplyeNWIATFDDPEAKLAAITAKIPLgHRMTTAEEIADTA 228
                        170       180
                 ....*....|....*....|
gi 767979509 180 SFLCSPDASYVNGENIAVAG 199
Cdd:PRK08628 229 VFLLSERSSHTTGQWLFVDG 248
PRK08416 PRK08416
enoyl-ACP reductase;
89-202 4.21e-15

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 71.34  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  89 GAVILVSSIA--AYNPVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQL 166
Cdd:PRK08416 145 GSIISLSSTGnlVYIENYA--GHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEEVKAKTEELSPL 222
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767979509 167 QRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYST 202
Cdd:PRK08416 223 NRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGGTT 258
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
22-144 4.30e-15

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: 70.30  E-value: 4.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  22 EDREQlVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYN 101
Cdd:cd11731   40 TDEAS-IKALFEKVGHFDAIVSTAGDAEFAPLAELTDAD-FQRGLNSKLLGQINLVRHGLPYL-NDGGSITLTSGILAQR 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767979509 102 PVVALGVYNVSKTALLGLTRTLALELaPKDIRVNCVVPGIIKT 144
Cdd:cd11731  117 PIPGGAAAATVNGALEGFVRAAAIEL-PRGIRINAVSPGVVEE 158
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
19-140 4.49e-15

(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: 71.20  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  19 GKA-------EDREQLVAKALEHCGGVDFLVCSAGVnpLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRG 89
Cdd:cd05353   63 GKAvanydsvEDGEKIVKTAIDAFGRVDILVNNAGI--LRdRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMrKQKFG 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509  90 AVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 140
Cdd:cd05353  141 RIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
13-199 4.79e-15

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: 71.27  E-value: 4.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  13 GIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGA 90
Cdd:cd08943   53 GVQCDVTSEAQVQSAFEQAVLEFGGLDIVVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMksQGIGGN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  91 VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPgiiktdfSKVFHGN---ESLWKN-------- 159
Cdd:cd08943  132 IVFNASKNAVAPGPNAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNP-------DAVFRGSkiwEGVWRAarakaygl 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767979509 160 ----FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd08943  205 leeeYRTRNLLKREVLPEDVAEAVVAMASEDFGKTTGAIVTVDG 248
PRK08263 PRK08263
short chain dehydrogenase; Provisional
23-147 5.01e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 71.61  E-value: 5.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DRE---QLVAKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQ-LLPYMENRR-GAVILVSSI 97
Cdd:PRK08263  60 DRAavfAAVETAVEHFGRLDIVVNNAG-YGLFGMIEEVTESEARAQIDTNFFG-ALWVTQaVLPYLREQRsGHIIQISSI 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509  98 AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:PRK08263 138 GGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
25-201 5.31e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 72.56  E-value: 5.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVnpLVGSTLG-TSEQIWDKILSVNVKSP-----ALLLSQLLpymeNRRGAVILVSSIA 98
Cdd:PRK08261 272 ARIAEHLAERHGGLDIVVHNAGI--TRDKTLAnMDEARWDSVLAVNLLAPlriteALLAAGAL----GDGGRIVGVSSIS 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  99 --AYNpvvaLGV--YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF----------------Skvfhgneslwk 158
Cdd:PRK08261 346 giAGN----RGQtnYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMtaaipfatreagrrmnS----------- 410
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767979509 159 nfkehhqLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYS 201
Cdd:PRK08261 411 -------LQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQS 446
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
102-199 8.91e-15

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 70.73  E-value: 8.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  102 PVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIiktDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSF 181
Cdd:TIGR02685 166 PLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL---SLLPDAMPFEVQEDYRRKVPLGQREASAEQIADVVIF 242
                          90
                  ....*....|....*...
gi 767979509  182 LCSPDASYVNGENIAVAG 199
Cdd:TIGR02685 243 LVSPKAKYITGTCIKVDG 260
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
1-184 9.77e-15

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: 70.39  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGE-----GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgsTLGT------SEQIWDKILSVN 69
Cdd:cd05346   37 LQELADElgakfPVKVLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAGL------ALGLdpaqeaDLEDWETMIDTN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  70 VKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:cd05346  111 VKGLLNVTRLILPIMIARnQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSL 190
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 149 V-FHGNESLWKN-FKEHHQLQrigeSEDCAGIVSFLCS 184
Cdd:cd05346  191 VrFHGDKEKADKvYEGVEPLT----PEDIAETILWVAS 224
PRK08264 PRK08264
SDR family oxidoreductase;
28-145 1.41e-14

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 69.53  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVAL 106
Cdd:PRK08264  64 VAAAAEAASDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVnVLSVLSWVNFPNL 143
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767979509 107 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:PRK08264 144 GTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTD 182
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
2-199 1.64e-14

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 69.97  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSagvnplVGSTLG-------TSEQIWDKILsvnvKS-- 72
Cdd:PRK12823  49 AELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVLINN------VGGTIWakpfeeyEEEQIEAEIR----RSlf 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  73 PALLLSQ-LLPYM-ENRRGAVILVSSIAAYnpvvalGVYNV----SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK12823 119 PTLWCCRaVLPHMlAQGGGAIVNVSSIATR------GINRVpysaAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPP 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979509 147 SKVFHG------NESLW-----KNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12823 193 RRVPRNaapqseQEKAWyqqivDQTLDSSLMKRYGTIDEQVAAILFLASDEASYITGTVLPVGG 256
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
76-199 2.02e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 69.26  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  76 LLSQLLPYMeNRRGAVILVSSIAAY---------------------------NPVVALGVYNVSKTALLGLTRTLALE-L 127
Cdd:PRK12428  78 LTEALLPRM-APGGAIVNVASLAGAewpqrlelhkalaatasfdegaawlaaHPVALATGYQLSKEALILWTMRQAQPwF 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979509 128 APKDIRVNCVVPGIIKT----DFSKVFhGNESLWKNFKehhQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12428 157 GARGIRVNCVAPGPVFTpilgDFRSML-GQERVDSDAK---RMGRPATADEQAAVLVFLCSDAARWINGVNLPVDG 228
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-154 2.19e-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: 69.42  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQ---GEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV--NPLVGSTLGTSEQIwDKILSVNVKSPAL 75
Cdd:COG3967   39 EEKLEeaaAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGImrAEDLLDEAEDLADA-EREITTNLLGPIR 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  76 LLSQLLPY-MENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNE 154
Cdd:COG3967  118 LTAAFLPHlKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDP 197
PRK06125 PRK06125
short chain dehydrogenase; Provisional
12-199 2.85e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 69.30  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  12 AGIVCHV---GKAEDREQLVAKAlehcGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR 88
Cdd:PRK06125  57 VDVAVHAldlSSPEAREQLAAEA----GDIDILVNNAGAIP-GGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  89 GAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD-FSKVFH-------GNESLWKN 159
Cdd:PRK06125 132 SGVIVnVIGAAGENPDADYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDrMLTLLKgraraelGDESRWQE 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767979509 160 FKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06125 212 LLAGLPLGRPATPEEVADLVAFLASPRSGYTSGTVVTVDG 251
PRK06949 PRK06949
SDR family oxidoreductase;
2-196 3.62e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.02  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK06949  51 AEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDILVNNSGVST-TQKLVDVTPADFDFVFDTNTRGAFFVAQEVA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMENR-RGA--------VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvfhg 152
Cdd:PRK06949 130 KRMIARaKGAgntkpggrIINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI------ 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 153 NESLWKNFKEHHQLQ-----RIGESEDCAGIVSFLCSPDASYVNGENIA 196
Cdd:PRK06949 204 NHHHWETEQGQKLVSmlprkRVGKPEDLDGLLLLLAADESQFINGAIIS 252
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
22-145 5.61e-14

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: 67.82  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  22 EDREQLVAKAlEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAY 100
Cdd:cd05354   60 TDPESIKAAA-AQAKDVDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLkANGGGAIVNLNSVASL 138
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 101 NPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:cd05354  139 KNFPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTR 183
PRK07576 PRK07576
short chain dehydrogenase; Provisional
2-199 5.63e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 68.44  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIW------DKILSVNVkspal 75
Cdd:PRK07576  51 AQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVLVSGAAGN-FPAPAAGMSANGFktvvdiDLLGTFNV----- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  76 lLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK-TDFSKVFHGNE 154
Cdd:PRK07576 125 -LKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLAPSP 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 155 SLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07576 204 ELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDG 248
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
2-191 7.61e-14

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: 67.95  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:cd08934   45 DELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAAL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvfHGNESLWKNF 160
Cdd:cd08934  124 PHHLLRNKGTIVnISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRD--HITHTITKEA 201
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767979509 161 KEhHQLQRIG--ESEDCAGIVSF-LCSPDASYVN 191
Cdd:cd08934  202 YE-ERISTIRklQAEDIAAAVRYaVTAPHHVTVN 234
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
17-199 8.26e-14

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 67.73  E-value: 8.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  17 HVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVS 95
Cdd:PRK12938  61 NVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDVVFRKMTRED-WTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINIS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  96 SIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHgnESLWKNFKEHHQLQRIGESEDC 175
Cdd:PRK12938 140 SVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIR--PDVLEKIVATIPVRRLGSPDEI 217
                        170       180
                 ....*....|....*....|....
gi 767979509 176 AGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12938 218 GSIVAWLASEESGFSTGADFSLNG 241
PRK09134 PRK09134
SDR family oxidoreductase;
25-199 1.25e-13

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 67.26  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVnpLVGSTLGT-SEQIWDKILSVNVKSPALL---LSQLLPymENRRGAVILVSSIAAY 100
Cdd:PRK09134  75 RALVARASAALGPITLLVNNASL--FEYDSAASfTRASWDRHMATNLRAPFVLaqaFARALP--ADARGLVVNMIDQRVW 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 101 NPVVALGVYNVSKTALLGLTRTLALELAPKdIRVNCVVPGIiktdfskVFHGNESLWKNFKEHHQ---LQRIGESEDCAG 177
Cdd:PRK09134 151 NLNPDFLSYTLSKAALWTATRTLAQALAPR-IRVNAIGPGP-------TLPSGRQSPEDFARQHAatpLGRGSTPEEIAA 222
                        170       180
                 ....*....|....*....|..
gi 767979509 178 IVSFLCspDASYVNGENIAVAG 199
Cdd:PRK09134 223 AVRYLL--DAPSVTGQMIAVDG 242
PRK12744 PRK12744
SDR family oxidoreductase;
1-203 1.30e-13

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 67.46  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQL 80
Cdd:PRK12744  53 VAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGRPDIAINTVG-KVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  81 LPYMENRRGAVILVSSI-AAYNPVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFskvFHGNESlwKN 159
Cdd:PRK12744 132 GRHLNDNGKIVTLVTSLlGAFTPFYS--AYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPF---FYPQEG--AE 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767979509 160 FKEHHQLQRIGES---------EDCAGIVSFLCSpDASYVNGENIAV-AGYSTR 203
Cdd:PRK12744 205 AVAYHKTAAALSPfsktgltdiEDIVPFIRFLVT-DGWWITGQTILInGGYTTK 257
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
21-192 1.96e-13

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: 66.45  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  21 AEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAA 99
Cdd:cd05340   68 SENCQQLAQRIAVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLlKSDAGSLVFTSSSVG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 100 YNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKehhqlqrigeSEDCAGIV 179
Cdd:cd05340  148 RQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKLKT----------PADIMPLY 217
                        170
                 ....*....|...
gi 767979509 180 SFLCSPDASYVNG 192
Cdd:cd05340  218 LWLMGDDSRRKTG 230
PRK06123 PRK06123
SDR family oxidoreductase;
6-199 3.04e-13

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 66.34  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGivcHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME 85
Cdd:PRK06123  52 GEALAVAA---DVADEADVLRLFEAVDRELGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  86 NRR----GAVILVSSIAAYnpvvaLGV------YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvFH---G 152
Cdd:PRK06123 129 TRHggrgGAIVNVSSMAAR-----LGSpgeyidYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE----IHasgG 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767979509 153 NESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06123 200 EPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVSG 246
PRK05855 PRK05855
SDR family oxidoreductase;
18-145 3.81e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 67.31  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVN---VKSPALLLSQLLpyMENRRGAVIL- 93
Cdd:PRK05855 373 VSDADAMEAFAEWVRAEHGVPDIVVNNAGIG-MAGGFLDTSAEDWDRVLDVNlwgVIHGCRLFGRQM--VERGTGGHIVn 449
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767979509  94 VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:PRK05855 450 VASAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTN 501
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
38-158 4.18e-13

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: 66.09  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  38 VDFLVCSAGVNPlvgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAA--------------YNP 102
Cdd:cd05327   81 LDILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHragpidfndldlenNKE 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767979509 103 VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWK 158
Cdd:cd05327  158 YSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYK 213
PLN02253 PLN02253
xanthoxin dehydrogenase
16-199 5.78e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 65.61  E-value: 5.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVIL 93
Cdd:PLN02253  73 CDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLtGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMiPLKKGSIVS 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  94 VSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF----HGNESLWKNFK----EHHQ 165
Cdd:PLN02253 153 LCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHlpedERTEDALAGFRafagKNAN 232
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767979509 166 LQRIGES-EDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PLN02253 233 LKGVELTvDDVANAVLFLASDEARYISGLNLMIDG 267
PRK05872 PRK05872
short chain dehydrogenase; Provisional
23-145 5.91e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 65.76  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQL---VAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAA 99
Cdd:PRK05872  68 DLAAMqaaAEEAVERFGGIDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAA 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767979509 100 YNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:PRK05872 147 FAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTD 192
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
16-201 6.73e-13

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 65.54  E-value: 6.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVI 92
Cdd:PRK08415  62 LDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPkeaLEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL-NDGASVL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFHGNESlwknfkeHHQ 165
Cdd:PRK08415 141 TLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTlaasgigDFRMILKWNEI-------NAP 213
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK08415 214 LKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVdAGYN 250
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
16-201 8.44e-13

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 65.12  E-value: 8.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLV-CSAGVNP--LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVI 92
Cdd:PRK07370  66 CDVQDDAQIEETFETIKQKWGKLDILVhCLAFAGKeeLIGDFSATSREGFARALEISAYSLAPLCKAAKPLM-SEGGSIV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGES 172
Cdd:PRK07370 145 TLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGILDMIHHVEEKAPLRRTVTQ 224
                        170       180       190
                 ....*....|....*....|....*....|
gi 767979509 173 EDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK07370 225 TEVGNTAAFLLSDLASGITGQTIYVdAGYC 254
PRK05876 PRK05876
short chain dehydrogenase; Provisional
4-144 1.37e-12

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 64.59  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK05876  50 LRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSNAGI-VVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPR 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979509  84 M--ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK05876 129 LleQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVET 191
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
38-148 2.29e-12

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 64.02  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  38 VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILV-SSIAAYNPVVALGVYNVSKTAL 116
Cdd:cd09806   80 VDVLVCNAGVG-LLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVtSSVGGLQGLPFNDVYCASKFAL 158
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767979509 117 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:cd09806  159 EGLCESLAVQLLPFNVHLSLIECGPVHTAFME 190
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
5-199 2.64e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 63.52  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   5 QGEGLSVaGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGTseqiWDKILSVNVKSPALLLSQLL 81
Cdd:PRK12384  50 YGEGMAY-GFGADATSEQSVLALSRGVDEIFGRVDLLVYNAGIakaAFITDFQLGD----FDRSLQVNLVGYFLCAREFS 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYM--ENRRGAVILVSSIAA-----YNpvvalGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG-IIKtdfSKVFhgn 153
Cdd:PRK12384 125 RLMirDGIQGRIIQINSKSGkvgskHN-----SGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLK---SPMF--- 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509 154 ESLWKNF--------KEHHQ-------LQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK12384 194 QSLLPQYakklgikpDEVEQyyidkvpLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTG 254
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
16-201 3.57e-12

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 63.45  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTLGT-SEQIWDKILSVNVKSPALLLSQLLPYMENRRGAV 91
Cdd:PRK08690  63 CDVASDDEINQVFADLGKHWDGLDGLVHSIGFAPkeaLSGDFLDSiSREAFNTAHEISAYSLPALAKAARPMMRGRNSAI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  92 ILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGE 171
Cdd:PRK08690 143 VALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLGHVAAHNPLRRNVT 222
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767979509 172 SEDCAGIVSFLCSPDASYVNGENIAV-AGYS 201
Cdd:PRK08690 223 IEEVGNTAAFLLSDLSSGITGEITYVdGGYS 253
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
36-156 4.20e-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: 62.70  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  36 GGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEN-RRGAVILVSSIAA------YNPVVAlgv 108
Cdd:cd05325   74 AGLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINISSRVGsigdntSGGWYS--- 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767979509 109 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESL 156
Cdd:cd05325  151 YRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKGP 198
PRK06194 PRK06194
hypothetical protein; Provisional
2-144 4.27e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.50  E-value: 4.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL 81
Cdd:PRK06194  48 AELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHLLFNNAGVGA-GGLVWENSLADWEWVLGVNLWGVIHGVRAFT 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979509  82 PYM-------ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVV--PGIIKT 144
Cdd:PRK06194 127 PLMlaaaekdPAYEGHIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETLYQDLSLVTDQVGASVlcPYFVPT 198
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
7-145 5.22e-12

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: 62.69  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEN 86
Cdd:cd05367   47 PGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKK 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509  87 RR--GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELapKDIRVNCVVPGIIKTD 145
Cdd:cd05367  127 RGlkKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFFRVLAAEE--PDVRVLSYAPGVVDTD 185
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
1-145 1.31e-11

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: 61.55  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQ 79
Cdd:cd05370   42 LAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDILINNAGIQRPIDLRDPASDlDKADTEIDTNLIGPIRLIKA 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979509  80 LLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:cd05370  122 FLPHLKKQpEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
39-185 1.58e-11

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: 60.61  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  39 DFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALL 117
Cdd:cd02266   33 DVVVHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGLGGYAASKAALD 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509 118 GLTRTLALELAPKDIRVNCVVPGIIKTDFskVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSP 185
Cdd:cd02266  112 GLAQQWASEGWGNGLPATAVACGTWAGSG--MAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDR 177
PRK06179 PRK06179
short chain dehydrogenase; Provisional
14-146 2.16e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 61.07  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTS-EQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAV 91
Cdd:PRK06179  50 LELDVTDDASVQAAVDEVIARAGRIDVLVNNAGVG-LAGAAEESSiAQA-QALFDTNVFGILRMTRAVLPHMrAQGSGRI 127
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767979509  92 ILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK06179 128 INISSVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-199 2.67e-11

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 60.74  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGT-----SEQIWDKILSVNVKSP 73
Cdd:PRK08217  47 AECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAGIlrdGLLVKAKDGKvtskmSLEQFQSVIDVNLTGV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  74 ALLLSQLLPYM--ENRRGAVILVSSIA-AYNpvVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF 150
Cdd:PRK08217 127 FLCGREAAAKMieSGSKGVIINISSIArAGN--MGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAM 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 151 HgNESLWKnFKEHHQLQRIGESEDCAGIVSFLCSPDasYVNGENIAVAG 199
Cdd:PRK08217 205 K-PEALER-LEKMIPVGRLGEPEEIAHTVRFIIEND--YVTGRVLEIDG 249
PRK08340 PRK08340
SDR family oxidoreductase;
20-203 3.01e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 60.59  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  20 KAEDREQLVAKALEHCGGVDFLVCSAG---VNPLVGSTLGTSEqiWDKILSVNVKSPALLLSQLLP-YMENR-RGAVILV 94
Cdd:PRK08340  59 DKDDLKNLVKEAWELLGGIDALVWNAGnvrCEPCMLHEAGYSD--WLEAALLHLVAPGYLTTLLIQaWLEKKmKGVLVYL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  95 SSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-----DFSKVFHGN----ESLW-KNFKEHH 164
Cdd:PRK08340 137 SSVSVKEPMPPLVLADVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTpgareNLARIAEERgvsfEETWeREVLERT 216
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 165 QLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYSTR 203
Cdd:PRK08340 217 PLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFDGAMTR 255
PRK06947 PRK06947
SDR family oxidoreductase;
6-199 3.05e-11

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 60.59  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVAGIVCHvgkAEDREQLVAKALEHCGGVDFLVCSAGV----NPLVGSTLGTSEQIWDkilsVNVKSPALLLSQLL 81
Cdd:PRK06947  52 GRACVVAGDVAN---EADVIAMFDAVQSAFGRLDALVNNAGIvapsMPLADMDAARLRRMFD----TNVLGAYLCAREAA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  82 PYMENRRG----AVILVSSIAAynpvvALGV------YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvFH 151
Cdd:PRK06947 125 RRLSTDRGgrggAIVNVSSIAS-----RLGSpneyvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE----IH 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767979509 152 ---GNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06947 196 asgGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDAASYVTGALLDVGG 246
PRK06182 PRK06182
short chain dehydrogenase; Validated
7-146 3.24e-11

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 60.74  E-value: 3.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVC---HVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvGStLGTSEQI----WDKILSVNVKSPALLLSQ 79
Cdd:PRK06182  41 EDLASLGVHPlslDVTDEASIKAAVDTIIAEEGRIDVLVNNAGY----GS-YGAIEDVpideARRQFEVNLFGAARLTQL 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  80 LLPYM-ENRRGAVILVSSIAA--YNPVVALgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK06182 116 VLPHMrAQRSGRIINISSMGGkiYTPLGAW--YHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEW 183
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
21-199 5.85e-11

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: 59.65  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  21 AEDREQLVAKALEHCGGVDFLVCSAGvnPLVGSTL--GTSEQIWDKILSVNVKSpALLLSQL-LPYMeNRRGAVILVSSI 97
Cdd:cd05334   52 TEQAKQVVASVARLSGKVDALICVAG--GWAGGSAksKSFVKNWDLMWKQNLWT-SFIASHLaTKHL-LSGGLLVLTGAK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  98 AAYNPVVALGVYNVSKTALLGLTRTLALEL--APKDIRVNCVVPGIIKT----------DFSKvfhgneslWKNFkehhq 165
Cdd:cd05334  128 AALEPTPGMIGYGAAKAAVHQLTQSLAAENsgLPAGSTANAILPVTLDTpanrkampdaDFSS--------WTPL----- 194
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767979509 166 lqrigesEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05334  195 -------EFIAELILFWASGAARPKSGSLIPVVT 221
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
16-202 7.30e-11

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 59.57  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVI 92
Cdd:PRK07533  67 LDVREPGQLEAVFARIAEEWGRLDFLLHSIAFAPkedLHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTNG-GSLL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFskvfhgnESLWKNFKEHHQ 165
Cdd:PRK07533 146 TMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTraasgidDF-------DALLEDAAERAP 218
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:PRK07533 219 LRRLVDIDDVGAVAAFLASDAARRLTGNTLYIdGGYHI 256
PRK05693 PRK05693
SDR family oxidoreductase;
7-148 1.32e-10

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 59.03  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   7 EGLSVAGIVC---HVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK05693  39 EALAAAGFTAvqlDVNDGAALARLAEELEAEHGGLDVLINNAGYGAM-GPLLDGGVEAMRRQFETNVFAVVGVTRALFPL 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979509  84 MENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 148
Cdd:PRK05693 118 LRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
16-202 2.14e-10

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 58.29  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTL-GTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAV 91
Cdd:PRK06997  63 CDVASDEQIDALFASLGQHWDGLDGLVHSIGFAPreaIAGDFLdGLSRENFRIAHDISAYSFPALAKAALPML-SDDASL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  92 ILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFhgneslwKNFKEHH 164
Cdd:PRK06997 142 LTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaasgikDFGKIL-------DFVESNA 214
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767979509 165 QLQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:PRK06997 215 PLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVdSGFNA 253
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
8-199 6.40e-10

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: 57.09  E-value: 6.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   8 GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGTseqiWDKILSVNVKSPALLLSQLLPYM 84
Cdd:cd05322   51 GEKAYGFGADATNEQSVIALSKGVDEIFKRVDLLVYSAGIaksAKITDFELGD----FDRSLQVNLVGYFLCAREFSKLM 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  85 --ENRRGAVILVSSIAA-----YNpvvalGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG-IIKTD--------FSK 148
Cdd:cd05322  127 irDGIQGRIIQINSKSGkvgskHN-----SGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPmfqsllpqYAK 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767979509 149 VFHGNES-LWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:cd05322  202 KLGIKESeVEQYYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINITG 253
PRK09186 PRK09186
flagellin modification protein A; Provisional
66-197 7.00e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 56.92  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  66 LSVNVKSPALLLSQLLPYMENRR-GAVILVSSI--------------AAYNPVValgvYNVSKTALLGLTRTLALELAPK 130
Cdd:PRK09186 114 LSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIygvvapkfeiyegtSMTSPVE----YAAIKAGIIHLTKYLAKYFKDS 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979509 131 DIRVNCVVPGIIKTdfskvfHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAV 197
Cdd:PRK09186 190 NIRVNCVSPGGILD------NQPEAFLNAYKKCCNGKGMLDPDDICGTLVFLLSDQSKYITGQNIIV 250
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
58-144 8.12e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 56.42  E-value: 8.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  58 SEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNC 136
Cdd:PRK08945 113 DPEVWQDVMQVNVNATFMLTQALLPLLLkSPAASLVFTSSSVGRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNC 192

                 ....*...
gi 767979509 137 VVPGIIKT 144
Cdd:PRK08945 193 INPGGTRT 200
PRK05993 PRK05993
SDR family oxidoreductase;
76-146 9.31e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 56.57  E-value: 9.31e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979509  76 LLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK05993 114 LTRRVIPVMRKQgQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF 185
PRK07041 PRK07041
SDR family oxidoreductase;
88-182 1.37e-09

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 55.81  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  88 RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPkdIRVNCVVPGIIKTD-FSKVF-HGNESLWKNFKEHHQ 165
Cdd:PRK07041 116 GGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALELAP--VRVNTVSPGLVDTPlWSKLAgDAREAMFAAAAERLP 193
                         90
                 ....*....|....*..
gi 767979509 166 LQRIGESEDCAGIVSFL 182
Cdd:PRK07041 194 ARRVGQPEDVANAILFL 210
PRK09072 PRK09072
SDR family oxidoreductase;
21-146 1.99e-09

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 55.72  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  21 AEDREQLVAKALEHcGGVDFLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAA 99
Cdd:PRK09072  65 EAGREAVLARAREM-GGINVLINNAGVNHFALLEDQDPEAI-ERLLALNLTAPMQLTRALLPLLrAQPSAMVVNVGSTFG 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767979509 100 ynpvvALG-----VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK09072 143 -----SIGypgyaSYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
41-158 2.34e-09

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: 55.36  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  41 LVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLT 120
Cdd:cd09805   82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAFS 161
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767979509 121 RTLALELAPKDIRVNCVVPGIIKTdfskVFHGNESLWK 158
Cdd:cd09805  162 DSLRRELQPWGVKVSIIEPGNFKT----GITGNSELWE 195
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
28-197 4.86e-09

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 54.82  E-value: 4.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALE-HCGGVDFLVCSAGVNPLVG-STLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVA 105
Cdd:PRK06300 109 VAEQVKkDFGHIDILVHSLANSPEISkPLLETSRKGYLAALSTSSYSFVSLLSHFGPIM-NPGGSTISLTYLASMRAVPG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 106 LGV-YNVSKTALLGLTRTLALELAPK-DIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLC 183
Cdd:PRK06300 188 YGGgMSSAKAALESDTKVLAWEAGRRwGIRVNTISAGPLASRAGKAIGFIERMVDYYQDWAPLPEPMEAEQVGAAAAFLV 267
                        170
                 ....*....|....
gi 767979509 184 SPDASYVNGENIAV 197
Cdd:PRK06300 268 SPLASAITGETLYV 281
PRK09291 PRK09291
SDR family oxidoreductase;
2-146 5.45e-09

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 54.23  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVagIVCHVGKAEDReqlvAKALEHcgGVDFLVCSAGVnplvgstlGTSEQIWD-------KILSVNVKSPA 74
Cdd:PRK09291  46 AARRGLALRV--EKLDLTDAIDR----AQAAEW--DVDVLLNNAGI--------GEAGAVVDipvelvrELFETNVFGPL 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979509  75 LLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 146
Cdd:PRK09291 110 ELTQGFVRKMvARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGF 182
PRK07775 PRK07775
SDR family oxidoreductase;
28-144 7.07e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 53.99  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVAL 106
Cdd:PRK07775  78 VAQAEEALGEIEVLVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMiERRRGDLIFVGSDVALRQRPHM 156
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767979509 107 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK07775 157 GAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK08267 PRK08267
SDR family oxidoreductase;
23-145 1.64e-08

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 53.02  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQlVAKALEHC-----GGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSS 96
Cdd:PRK08267  59 DRAA-WDAALADFaaatgGRLDVLFNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVInTSS 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:PRK08267 137 ASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTA 185
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
16-145 2.50e-08

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 52.07  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAE--DREQLVAKALEHC----GGVDFLVCSAGVnplvgSTLGTSEQI----WDKILSVNVKSPALLLSQLLPYME 85
Cdd:cd08931   49 VVAGALDvtDRAAWAAALADFAaatgGRLDALFNNAGV-----GRGGPFEDVplaaHDRMVDINVKGVLNGAYAALPYLK 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509  86 NRRGA-VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:cd08931  124 ATPGArVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTP 184
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
18-144 5.75e-08

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 51.48  E-value: 5.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLVCSAGVNPlvGSTLGTS--EQIWD---KILSVNVKSPALLLSQLLPYMeNRRGAVI 92
Cdd:PRK07889  66 VTNEEHLASLADRVREHVDGLDGVVHSIGFAP--QSALGGNflDAPWEdvaTALHVSAYSLKSLAKALLPLM-NEGGSIV 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767979509  93 LVSsiaaYNPVVALGVYN---VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK07889 143 GLD----FDATVAWPAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRT 193
PRK07832 PRK07832
SDR family oxidoreductase;
36-144 7.67e-08

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 51.20  E-value: 7.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  36 GGVDFLVCSAGVnplvgSTLGTSEQI----WDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAynpVVAL--- 106
Cdd:PRK07832  77 GSMDVVMNIAGI-----SAWGTVDRLtheqWRRMVDVNLMGPIHVIETFVPPMvaAGRGGHLVNVSSAAG---LVALpwh 148
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767979509 107 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK07832 149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK08278 PRK08278
SDR family oxidoreductase;
14-139 7.78e-08

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 51.06  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  14 IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGsTLGTSEQIWDKILSVNVKSpALLLSQL-LPYMENRRGAVI 92
Cdd:PRK08278  67 LVGDVRDEDQVAAAVAKAVERFGGIDICVNNASAINLTG-TEDTPMKRFDLMQQINVRG-TFLVSQAcLPHLKKSENPHI 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767979509  93 LVSS---------IAAYNPvvalgvYNVSKTALLGLTRTLALELAPKDIRVNCVVP 139
Cdd:PRK08278 145 LTLSpplnldpkwFAPHTA------YTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK05866 PRK05866
SDR family oxidoreductase;
2-144 9.12e-08

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 50.90  E-value: 9.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNplVGSTLGTSEQIW---DKILSVNVKSPALLLS 78
Cdd:PRK05866  82 DRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAGRS--IRRPLAESLDRWhdvERTMVLNYYAPLRLIR 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979509  79 QLLPYM-ENRRGAVILVSSIAAYNPVVAL-GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK05866 160 GLAPGMlERGDGHIINVATWGVLSEASPLfSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK06914 PRK06914
SDR family oxidoreductase;
36-145 1.10e-07

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 50.79  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  36 GGVDFLVCSAGVnpLVGstlGTSEQI----WDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYN 110
Cdd:PRK06914  80 GRIDLLVNNAGY--ANG---GFVEEIpveeYRKQFETNVFGAISVTQAVLPYMrKQKSGKIINISSISGRVGFPGLSPYV 154
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767979509 111 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 145
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
16-202 1.40e-07

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 50.52  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVI 92
Cdd:PRK08159  67 CDVTDEASIDAVFETLEKKWGKLDFVVHAIGFsdkDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDG-GSIL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFHGNESlwknfkeHHQ 165
Cdd:PRK08159 146 TLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTlaasgigDFRYILKWNEY-------NAP 218
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGENIAV-AGYST 202
Cdd:PRK08159 219 LRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVdSGYHV 256
PRK07023 PRK07023
SDR family oxidoreductase;
66-186 1.69e-07

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 50.01  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  66 LSVNVKSPALLLSQLLPYMEN---RRgaVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALElAPKDIRVNCVVPGII 142
Cdd:PRK07023 106 VGLNVAAPLMLTAALAQAASDaaeRR--ILHISSGAARNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVV 182
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 143 KTDFSKVFHGNES----LWKNFKEHHQLQRIGESEDCAG-IVSFLCSPD 186
Cdd:PRK07023 183 DTGMQATIRATDEerfpMRERFRELKASGALSTPEDAARrLIAYLLSDD 231
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
28-197 2.13e-07

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 49.77  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEH-CGGVDFLVCSAGVNPLVG-STLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVA 105
Cdd:PLN02730 110 VAESVKAdFGSIDILVHSLANGPEVTkPLLETSRKGYLAAISASSYSFVSLLQHFGPIM-NPGGASISLTYIASERIIPG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 106 LGVYNVS-KTALLGLTRTLALELAPK-DIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLC 183
Cdd:PLN02730 189 YGGGMSSaKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAIGFIDDMIEYSYANAPLQKELTADEVGNAAAFLA 268
                        170
                 ....*....|....
gi 767979509 184 SPDASYVNGENIAV 197
Cdd:PLN02730 269 SPLASAITGATIYV 282
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
18-193 4.17e-07

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 48.85  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  18 VGKAEDREQLVAKALEHCGGVDFLV---CSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYMENRRGAVILV 94
Cdd:PRK06603  67 VTNPKSISNLFDDIKEKWGSFDFLLhgmAFADKNELKGRYVDTSLENFHNSLHISCYS-LLELSRSAEALMHDGGSIVTL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  95 SSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESED 174
Cdd:PRK06603 146 TYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDFSTMLKSHAATAPLKRNTTQED 225
                        170
                 ....*....|....*....
gi 767979509 175 CAGIVSFLCSPDASYVNGE 193
Cdd:PRK06603 226 VGGAAVYLFSELSKGVTGE 244
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
2-146 4.62e-07

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: 48.53  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNvkspalLLSQL- 80
Cdd:cd05360   42 REVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVA-VFGRFEDVTPEEFRRVFDVN------YLGHVy 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979509  81 -----LPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAP--KDIRVNCVVPGIIKTDF 146
Cdd:cd05360  115 gtlaaLPHLRRRGgGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHdgAPISVTLVQPTAMNTPF 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
6-192 5.28e-07

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: 48.60  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   6 GEGLSVagiVCHVGKAEDREQLVAK-ALEHCGGVDFLVCSA-GVNPLVGSTLGT-----SEQIWDKILSVNVKSPALLLS 78
Cdd:cd09763   53 GKCIPV---RCDHSDDDEVEALFERvAREQQGRLDILVNNAyAAVQLILVGVAKpfweePPTIWDDINNVGLRAHYACSV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  79 QLLPYM-ENRRGAVILVSSIAA----YNPVvalgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGN 153
Cdd:cd09763  130 YAAPLMvKAGKGLIVIISSTGGleylFNVA-----YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPED 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767979509 154 ESLWKNFKEHHQLQRiGESEDCAG--IVSFLCSPDASYVNG 192
Cdd:cd09763  205 DEGSWHAKERDAFLN-GETTEYSGrcVVALAADPDLMELSG 244
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
97-200 1.10e-06

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 47.80  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  97 IAAYNpvvalgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCA 176
Cdd:PRK08594 155 VQNYN------VMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGFNSILKEIEERAPLRRTTTQEEVG 228
                         90       100
                 ....*....|....*....|....*
gi 767979509 177 GIVSFLCSPDASYVNGENIAV-AGY 200
Cdd:PRK08594 229 DTAAFLFSDLSRGVTGENIHVdSGY 253
PRK06940 PRK06940
short chain dehydrogenase; Provisional
4-199 1.75e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 47.32  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   4 LQGEGLSVAGIVCHVGKAEDREQLVAKALEHcGGVDFLVCSAGVNPLVGSTlgtseqiwDKILSVNVKSPALLLSQLLPY 83
Cdd:PRK06940  44 LREAGFDVSTQEVDVSSRESVKALAATAQTL-GPVTGLVHTAGVSPSQASP--------EAILKVDLYGTALVLEEFGKV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MEnRRGAVILVSSIAAYNP------------------------------VVALGVYNVSKTALLGLTRTLALELAPKDIR 133
Cdd:PRK06940 115 IA-PGGAGVVIASQSGHRLpaltaeqeralattpteellslpflqpdaiEDSLHAYQIAKRANALRVMAEAVKWGERGAR 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979509 134 VNCVVPGIIKTDFskvfhGNESL-------WKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK06940 194 INSISPGIISTPL-----AQDELngprgdgYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDG 261
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
3-146 1.83e-06

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: 46.99  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   3 KLQGEGLSVAG-----IVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLL 77
Cdd:cd05373   38 ALLVDIIRDAGgsakaVPTDARDEDEVIALFDLIEEEIGPLEVLVYNAGAN-VWFPILETTPRVFEKVWEMAAFGGFLAA 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509  78 SQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRV-NCVVPGIIKTDF 146
Cdd:cd05373  117 REAAKRMlARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHVaHVIIDGGIDTDF 187
PRK06482 PRK06482
SDR family oxidoreductase;
28-147 1.88e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 47.03  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNpLVGSTLG-TSEQIWDKIlSVNVKSPALLLSQLLPYMENRRGAVIL-VSSI---AAYnP 102
Cdd:PRK06482  67 VDRAFAALGRIDVVVSNAGYG-LFGAAEElSDAQIRRQI-DTNLIGSIQVIRAALPHLRRQGGGRIVqVSSEggqIAY-P 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767979509 103 vvALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:PRK06482 144 --GFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFG 186
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
2-199 3.37e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 46.30  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   2 AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVN---PLvgstlgtsEQI----WDKILSVNVKSpA 74
Cdd:PRK07523  52 ESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQfrtPL--------EDFpadaFERLLRTNISS-V 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  75 LLLSQLL--PYMENRRGAVILVSSI--AAYNPVVAlgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF 150
Cdd:PRK07523 123 FYVGQAVarHMIARGAGKIINIASVqsALARPGIA--PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAAL 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767979509 151 HGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07523 201 VADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLYVDG 249
PRK06101 PRK06101
SDR family oxidoreductase;
60-144 3.57e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 46.02  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  60 QIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVP 139
Cdd:PRK06101  93 TLMARVFNVNVLGVANCIEGIQPHLS-CGHRVVIVGSIASELALPRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFP 171

                 ....*
gi 767979509 140 GIIKT 144
Cdd:PRK06101 172 GFVAT 176
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
25-154 3.69e-06

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 45.90  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  25 EQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPV 103
Cdd:PRK10538  62 EEMLASLPAEWRNIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMvERNHGHIINIGSTAGSWPY 141
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767979509 104 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK-TDFSKV-FHGNE 154
Cdd:PRK10538 142 AGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVrFKGDD 194
PRK08017 PRK08017
SDR family oxidoreductase;
1-147 6.42e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 45.46  E-value: 6.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSvaGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNV----KSPALL 76
Cdd:PRK08017  39 VARMNSLGFT--GILLDLDDPESVERAADEVIALTDNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFfgthQLTMLL 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979509  77 LSQLLPYMENRrgaVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 147
Cdd:PRK08017 117 LPAMLPHGEGR---IVMTSSVMGLISTPGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFT 184
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
41-200 9.37e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.06  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  41 LVCSAG-VNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYMENRRGA--VILVSSIAAYNPVVALGVYNVSKTALL 117
Cdd:PRK06924  84 LINNAGmVAPIKPIEKAESEEL-ITNVHLNLLAPMILTSTFMKHTKDWKVDkrVINISSGAAKNPYFGWSAYCSSKAGLD 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509 118 GLTRTLALELAPKDIRVNCVV--PGIIKTDFSKV--------FHGNESlWKNFKEHHQLQrigESEDCAGIVSFLCSpDA 187
Cdd:PRK06924 163 MFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQirssskedFTNLDR-FITLKEEGKLL---SPEYVAKALRNLLE-TE 237
                        170
                 ....*....|...
gi 767979509 188 SYVNGENIAVAGY 200
Cdd:PRK06924 238 DFPNGEVIDIDEY 250
PRK07024 PRK07024
SDR family oxidoreductase;
23-144 9.62e-06

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 44.92  E-value: 9.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  23 DREQLVAKA---LEHCGGVDFLVCSAGVNplVGSTLGTSEQI--WDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSS 96
Cdd:PRK07024  61 DADALAAAAadfIAAHGLPDVVIANAGIS--VGTLTEEREDLavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVgIAS 138
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767979509  97 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 144
Cdd:PRK07024 139 VAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-146 1.05e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.91  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVnplvgSTLGTSEQI----WDKILSVNvkspalL 76
Cdd:PRK07109  49 AAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMV-----TVFGPFEDVtpeeFRRVTEVT------Y 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  77 LSQL------LPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALEL----APkdIRVNCVVPGIIKTD 145
Cdd:PRK07109 118 LGVVhgtlaaLRHMRPRdRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCELlhdgSP--VSVTMVQPPAVNTP 195

                 .
gi 767979509 146 F 146
Cdd:PRK07109 196 Q 196
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-197 1.36e-05

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 44.33  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509   1 MAKLQGEglSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCS---AGVNPLVGSTLGTSEQIWDkiLSVNVKSPALLL 77
Cdd:PRK06079  49 LQKLVDE--EDLLVECDVASDESIERAFATIKERVGKIDGIVHAiayAKKEELGGNVTDTSRDGYA--LAQDISAYSLIA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  78 SQLL--PYMENRRGAVIL-----VSSIAAYNpvvalgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVF 150
Cdd:PRK06079 125 VAKYarPLLNPGASIVTLtyfgsERAIPNYN------VMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGI 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767979509 151 HGNESLwknFKEHHQLQRIGES---EDCAGIVSFLCSPDASYVNGENIAV 197
Cdd:PRK06079 199 KGHKDL---LKESDSRTVDGVGvtiEEVGNTAAFLLSDLSTGVTGDIIYV 245
PRK07984 PRK07984
enoyl-ACP reductase FabI;
84-199 2.19e-05

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 43.74  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  84 MENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFHGNESL 156
Cdd:PRK07984 134 MLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTlaasgikDFRKMLAHCEAV 213
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767979509 157 wknfkehHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAG 199
Cdd:PRK07984 214 -------TPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDG 249
PRK06953 PRK06953
SDR family oxidoreductase;
52-145 1.06e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 38.51  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  52 GSTLGTSEQiWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSS----IAAYnPVVALGVYNVSKTALlgltrTLALEL 127
Cdd:PRK06953  87 GVEPITRED-FDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrmgsIGDA-TGTTGWLYRASKAAL-----NDALRA 159
                         90       100
                 ....*....|....*....|.
gi 767979509 128 APKDIR-VNCVV--PGIIKTD 145
Cdd:PRK06953 160 ASLQARhATCIAlhPGWVRTD 180
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
28-139 1.37e-03

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: 38.58  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  28 VAKALEHCGGVDFLVCSAGVNPLVGsTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPV--- 103
Cdd:cd09762   78 VEKAVEKFGGIDILVNNASAISLTG-TLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILnLSPPLNLNPKwfk 156
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767979509 104 --VAlgvYNVSKTALLGLTRTLALELAPKDIRVNCVVP 139
Cdd:cd09762  157 nhTA---YTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK07578 PRK07578
short chain dehydrogenase; Provisional
36-143 3.07e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 37.10  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  36 GGVDFLVCSAGV---NPLVGSTlgtSEQIWdkiLSVNVKspalLLSQL------LPYMeNRRGAVILVSSIAAYNPVVAL 106
Cdd:PRK07578  54 GKVDAVVSAAGKvhfAPLAEMT---DEDFN---VGLQSK----LMGQVnlvligQHYL-NDGGSFTLTSGILSDEPIPGG 122
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767979509 107 GVYNVSKTALLGLTRTLALELaPKDIRVNCVVPGIIK 143
Cdd:PRK07578 123 ASAATVNGALEGFVKAAALEL-PRGIRINVVSPTVLT 158
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
16-193 4.44e-03

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 37.03  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  16 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGV---NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVI 92
Cdd:PRK06505  64 CDVEDIASVDAVFEALEKKWGKLDFVVHAIGFsdkNELKGRYADTTRENFSRTMVISCFSFTEIAKRAAKLMPDG-GSML 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979509  93 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVFHGNeslwknfKEHHQ 165
Cdd:PRK06505 143 TLTYGGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTlagagigDARAIFSYQ-------QRNSP 215
                        170       180
                 ....*....|....*....|....*...
gi 767979509 166 LQRIGESEDCAGIVSFLCSPDASYVNGE 193
Cdd:PRK06505 216 LRRTVTIDEVGGSALYLLSDLSSGVTGE 243
 
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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