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Conserved domains on  [gi|767927354|ref|XP_011511369|]
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D-beta-hydroxybutyrate dehydrogenase, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0051287|GO:0016491
PubMed:  12604210|19011748|19027726|20423462|19011750

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 60-345 3.45e-158

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: 444.03  E-value: 3.45e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 139
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 298
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 767927354 299 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 345
Cdd:cd09805  236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYI-PASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 60-345 3.45e-158

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: 444.03  E-value: 3.45e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 139
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 298
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 767927354 299 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 345
Cdd:cd09805  236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYI-PASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
60-266 7.89e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 156.57  E-value: 7.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG-ARVEVVALDVTDPDAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:COG0300   85 ----VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPG----NFIAAT------SLYSPEsiqAIAKKMWE 266
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGpvdtPFTARAgapagrPLLSPE---EVARAILR 215
PRK06182 PRK06182
short chain dehydrogenase; Validated
 58-320 3.57e-45

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 155.50  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgvkeLDSLNSDRLRTVQLNVCSSeevekvveivrSSLK- 136
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDK-------MEDLASLGVHPLSLDVTDE-----------ASIKa 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 ------DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPAR 209
Cdd:PRK06182  64 avdtiiAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG------NFIAATSL--------YSPESiQAIAKKMweelpevvRKD 275
Cdd:PRK06182 144 AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGgiktewGDIAADHLlktsgngaYAEQA-QAVAASM--------RST 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767927354 276 YGkkyfdekiakmetycSSGSTDTSPVIDAVTHALTATTPYTRYH 320
Cdd:PRK06182 215 YG---------------SGRLSDPSVIADAISKAVTARRPKTRYA 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 60-245 4.52e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 150.07  E-value: 4.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD-- 137
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA-LGGKALFIQGDVTD-----------RAQVKAlv 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  138 ---PEK--GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 211
Cdd:pfam00106  69 eqaVERlgRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767927354  212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGV 182
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 62-276 3.34e-20

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 88.03  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPEKG 141
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDV--------------SDREDVKAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  142 M------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARS 210
Cdd:TIGR01830  67 VeeieeeLGtidiLVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLrIMIKQRSGRIINISSVVGLMGNAGQA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354  211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRKDY 276
Cdd:TIGR01830 147 NYAASKAGVIGFTKSLAKELASRNITVNAVAPG-FIDT--------------DMTDKLSEKVKKKI 197
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 60-345 3.45e-158

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: 444.03  E-value: 3.45e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 139
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 298
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 767927354 299 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 345
Cdd:cd09805  236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYI-PASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 60-326 3.37e-80

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: 244.83  E-value: 3.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgVKELDSLNSDRLRTVQLNVCSSeevekvveivrSSLK--- 136
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDK----LESLGELLNDNLEVLELDVTDE-----------ESIKaav 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 ----DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP 211
Cdd:cd05374   66 keviERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIakkmweelpevvrkDYGKKYFDEKIAKMETY 291
Cdd:cd05374  146 YCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALED--------------PEISPYAPERKEIKENA 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767927354 292 CSSGSTDTSP--VIDAVTHALTATTPYTRYHPMDYYW 326
Cdd:cd05374  212 AGVGSNPGDPekVADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
60-266 7.89e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 156.57  E-value: 7.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG-ARVEVVALDVTDPDAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:COG0300   85 ----VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPG----NFIAAT------SLYSPEsiqAIAKKMWE 266
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGpvdtPFTARAgapagrPLLSPE---EVARAILR 215
PRK06182 PRK06182
short chain dehydrogenase; Validated
 58-320 3.57e-45

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 155.50  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgvkeLDSLNSDRLRTVQLNVCSSeevekvveivrSSLK- 136
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDK-------MEDLASLGVHPLSLDVTDE-----------ASIKa 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 ------DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPAR 209
Cdd:PRK06182  64 avdtiiAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG------NFIAATSL--------YSPESiQAIAKKMweelpevvRKD 275
Cdd:PRK06182 144 AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGgiktewGDIAADHLlktsgngaYAEQA-QAVAASM--------RST 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767927354 276 YGkkyfdekiakmetycSSGSTDTSPVIDAVTHALTATTPYTRYH 320
Cdd:PRK06182 215 YG---------------SGRLSDPSVIADAISKAVTARRPKTRYA 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 60-245 4.52e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 150.07  E-value: 4.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD-- 137
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA-LGGKALFIQGDVTD-----------RAQVKAlv 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  138 ---PEK--GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 211
Cdd:pfam00106  69 eqaVERlgRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767927354  212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGV 182
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 60-245 6.99e-42

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: 146.10  E-value: 6.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslnsDRLRTVQLNVCSseevekvveivRSSLKD-- 137
Cdd:COG4221    6 KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELG----GRALAVPLDVTD-----------EAAVEAav 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 ---PEKgmWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPAR 209
Cdd:COG4221   71 aaaVAE--FGrldvLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGG 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:COG4221  149 AVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAV 184
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 62-243 2.62e-37

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: 133.95  E-value: 2.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKEldSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEkg 141
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAI--EALGGNAVAVQADVSDEEDVEALVEEALEEFGRLD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 142 mwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:cd05233   77 --ILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPhMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALE 154

                        170       180
                 ....*....|....*....|...
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05233  155 GLTRSLALELAPYGIRVNAVAPG 177
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 59-245 8.68e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 131.19  E-value: 8.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDkghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdp 138
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRV-VGTVRSE---AARADFEALHPDRALARLLDVTDFDAIDAVVADAEATF--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekgmwG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYC 213
Cdd:PRK06180  77 -----GpidvLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRaRRRGHIVNITSMGGLITMPGIGYYC 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK06180 152 GSKFALEGISESLAKEVAPFGIHVTAVEPGSF 183
PRK06914 PRK06914
SDR family oxidoreductase;
60-319 5.98e-35

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 128.99  E-value: 5.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLN-SDRLRTVQLNVCSSEEVekvveivrSSLKDP 138
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNlQQNIKVQQLDVTDQNSI--------HNFQLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGmWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 213
Cdd:PRK06914  76 LKE-IGridlLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYSpESIQAIAKKMWEELPevvrkdYgKKYFDekiaKMETYCS 293
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSY--NTNIWE-VGKQLAENQSETTSP------Y-KEYMK----KIQKHIN 220

                        250       260       270
                 ....*....|....*....|....*....|
gi 767927354 294 SGStDTSP----VIDAVTHALTATTPYTRY 319
Cdd:PRK06914 221 SGS-DTFGnpidVANLIVEIAESKRPKLRY 249
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 60-243 7.94e-34

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: 125.39  E-value: 7.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:cd05332    4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDM--------------SDLEDAE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 K----------GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 208
Cdd:cd05332   70 QvveealklfgGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVPF 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05332  150 RTAYAASKHALQGFFDSLRAELSEPNISVTVVCPG 184
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 60-319 3.03e-33

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: 123.72  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHL---HSKGFLVFAgcLMKD--KGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVveivRSS 134
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYA--TMRDlkKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAA----VER 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 135 LKDPEKGMwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYC 213
Cdd:cd09806   75 VTERHVDV--LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPdMKRRGSGRILVTSSVGGLQGLPFNDVYC 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAatslyspesiqAIAKKMWEELPEV----VRKDYGKKYFDEKIAK-M 288
Cdd:cd09806  153 ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT-----------AFMEKVLGSPEEVldrtADDITTFHFFYQYLAHsK 221

                        250       260       270
                 ....*....|....*....|....*....|.
gi 767927354 289 ETYCSSGSTdTSPVIDAVTHALTATTPYTRY 319
Cdd:cd09806  222 QVFREAAQN-PEEVAEVFLTAIRAPKPPLRY 251
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 60-263 1.05e-31

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: 119.51  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAG-GRALAVAADV--------------TDEAAVE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 208
Cdd:COG1028   72 ALVaaavaaFGrldiLVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPhMRERGGGRIVNISSIAGLRGSPG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIA----ATSLYSPESIQAIAKK 263
Cdd:COG1028  152 QAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPG-PIDtpmtRALLGAEEVREALAAR 209
PRK08017 PRK08017
SDR family oxidoreductase;
60-243 2.29e-30

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 115.95  E-value: 2.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCL-------MKDKGHDGVkELDSLNSDRLRTVQLNVcsseevekvveivr 132
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRkpddvarMNSLGFTGI-LLDLDDPESVERAADEV-------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 133 ssLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSP 211
Cdd:PRK08017  68 --IALTDNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGRGA 145

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08017 146 YAASKYALEAWSDALRMELRHSGIKVSLIEPG 177
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 59-272 2.83e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 110.76  E-value: 2.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC--LMKDKGHDGVK--ELDsLNSDRlrTVQLNVcsseevekvveivrSS 134
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSrnPARAAPIPGVEllELD-VTDDA--SVQAAV--------------DE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 135 LKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 213
Cdd:PRK06179  67 VIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG--------NFIAATS---LYSPE---SIQAIAKKMWE-ELPEVV 272
Cdd:PRK06179 147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAytktnfdaNAPEPDSplaEYDREravVSKAVAKAVKKaDAPEVV 220
PRK05693 PRK05693
SDR family oxidoreductase;
60-262 1.34e-26

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 106.41  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkdkghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 139
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATA-------RKAEDVEALAAAGFTAVQLDVNDGAALARLA----EELEAEH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGV 219
Cdd:PRK05693  71 GGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 220 EAFSDCLRYEMYPLGVKVSVVEPG----NF-----------IAATSLYSP--ESIQAIAK 262
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGaiasQFasnasreaeqlLAEQSPWWPlrEHIQARAR 210
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 60-245 3.54e-26

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: 104.26  E-value: 3.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkghdgvkeLDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSS-LKDP 138
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVI---------------IVARSESKLEEAVEEIEAEANASGQKVSYISAdLSDY 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EK--------GMWG-----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRM 204
Cdd:cd08939   67 EEveqafaqaVEKGgppdlVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKeQRPGHIVFVSSQAALV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767927354 205 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:cd08939  147 GIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDT 187
PRK05993 PRK05993
SDR family oxidoreductase;
60-319 2.89e-25

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 102.80  E-value: 2.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDgvkeLDSLNSDRLRTVQLNVCSSEEVEKVVEivrSSLKDPE 139
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATC---RKEED----VAALEAEGLEAFQLDYAEPESIAALVA---QVLELSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:PRK05993  75 GRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRkQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNfIAatSLYSPESIQAIAKkmWEELPEVV-RKDYgkkyfDEKIAKMETYCSSGST 297
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHVSLIEPGP-IE--TRFRANALAAFKR--WIDIENSVhRAAY-----QQQMARLEGGGSKSRF 224

                        250       260
                 ....*....|....*....|....
gi 767927354 298 DTSP--VIDAVTHALTATTPYTRY 319
Cdd:PRK05993 225 KLGPeaVYAVLLHALTAPRPRPHY 248
PRK05650 PRK05650
SDR family oxidoreductase;
143-245 5.81e-25

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 101.66  E-value: 5.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 143 WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK05650  75 WGgidvIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAKA 154

                         90       100
                 ....*....|....*....|....*...
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK05650 155 GVVALSETLLVELADDEIGVHVVCPSFF 182
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 60-274 1.44e-24

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: 100.31  E-value: 1.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdpe 139
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEA-EGGKALVLELDVTDEQQVDAAVERTVEALG--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:cd08934   80 -RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYSPESiQAIAKKMWEELPEVVRK 274
Cdd:cd08934  159 VNAFSEGLRQEVTERGVRVVVIEPG--TVDTELRDHIT-HTITKEAYEERISTIRK 211
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 60-283 4.44e-24

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: 98.63  E-value: 4.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGF----SLAKHLHSKgflVFAGClmKDKGhdGVKELDSLNSDRLRTVQLNVCSseevEKVVEIVRSSL 135
Cdd:cd05354    4 KTVLVTGANRGIGKafveSLLAHGAKK---VYAAV--RDPG--SAAHLVAKYGDKVVPLRLDVTD----PESIKAAAAQA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 136 KDPEKgmwgLVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYC 213
Cdd:cd05354   73 KDVDV----VINNAGVLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAMGTYS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF-----------IAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFD 282
Cdd:cd05354  149 ASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIdtrmaagaggpKESPETVAEAVLKALKAGEFHVFPDEMAKQVKEAYQS 228


                 .
gi 767927354 283 E 283
Cdd:cd05354  229 F 229
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 60-243 6.49e-24

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: 98.51  E-value: 6.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 139
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAAL----ENLPEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGIS----TFGEVEFTSLETykqVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 214
Cdd:cd05346   77 RDIDILVNNAGLAlgldPAQEADLEDWET---MIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCA 153

                        170       180
                 ....*....|....*....|....*....
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05346  154 TKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 60-243 9.67e-24

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: 97.31  E-value: 9.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFL-VFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVveivRSSLKDP 138
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLRAEGLS-VRFHQLDVTDDASIEAA----ADFVEEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWGLVNNAGISTFG-EVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMAnparSPYCITK 216
Cdd:cd05324   76 YGGLDILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLT----SAYGVSK 151

                        170       180
                 ....*....|....*....|....*..
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05324  152 AALNALTRILAKELKETGIKVNACCPG 178
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
59-243 2.00e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 97.14  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmkdKGHDGVKELDSLN---SDRLRTVQLNVCSSEEVEKVVeivrSSL 135
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEEYgftEDQVRLKELDVTDTEECAEAL----AEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 136 KDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCI 214
Cdd:PRK12824  75 EEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSA 154

                        170       180
                 ....*....|....*....|....*....
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPG 183
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
59-246 3.63e-23

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 96.38  E-value: 3.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD- 137
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRA-AGGEARVLVFDVSD-----------EAAVRAl 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 -----PEKGMW-GLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARS 210
Cdd:PRK05653  73 ieaavEAFGALdILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPpMIKARYGRIVNISSVSGVTGNPGQT 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI 246
Cdd:PRK05653 153 NYSAAKAGVIGFTKALALELASRGITVNAVAPG-FI 187
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 60-274 9.57e-23

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: 94.92  E-value: 9.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGN-AAALEADV--------------SDREAVE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 208
Cdd:cd05333   66 ALVekveaeFGpvdiLVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRaMIKRRSGRIINISSVVGLIGNPG 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRK 274
Cdd:cd05333  146 QANYAASKAGVIGFTKSLAKELASRGITVNAVAPG-FIDT--------------DMTDALPEKVKE 196
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 60-264 1.21e-22

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 94.88  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdpe 139
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:PRK05557  83 -GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARpMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGnFIA--ATSLYSPESIQAIAKKM 264
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPG-FIEtdMTDALPEDVKEAILAQI 208
PRK09291 PRK09291
SDR family oxidoreductase;
59-245 2.48e-22

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 94.29  E-value: 2.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC--------LMKDKGHDGVkeldslnsdRLRTVQLNVCSSEEVEkvvei 130
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVqiapqvtaLRAEAARRGL---------ALRVEKLDLTDAIDRA----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 131 vRSSLKDPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPAR 209
Cdd:PRK09291  68 -QAAEWDVDV----LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFT 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPY 178
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 60-243 2.98e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 94.62  E-value: 2.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslnsdRLRTVQLNVCSseevekvveivRSSLK--- 136
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-----LVVGGPLDVTD-----------PASFAafl 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 211
Cdd:PRK07825  70 DAVEADLGpidvLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAT 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07825 150 YCASKHAVVGFTDAARLELRGTGVHVSVVLPS 181
PRK12826 PRK12826
SDR family oxidoreductase;
59-244 9.41e-22

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 92.67  E-value: 9.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGhDGVKELDSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDP 138
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDA-AATAELVEAAGGKARARQVDVRDRAAL-------KAAVAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKgMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGR-MANPARSPY 212
Cdd:PRK12826  78 VE-DFGrldiLVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPrVGYPGLAHY 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 213 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN 244
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPGG 188
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 57-243 2.67e-21

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: 91.29  E-value: 2.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  57 VGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELdslnSDRLRTVQLNVCSSEEVEKVVEIVRSSLK 136
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL----GDAARFFHLDVTDEDGWTAVVDTAREAFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 dpekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYCIT 215
Cdd:cd05341   79 ----RLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNAS 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 216 KFGVEAFSDCLRYEMYP--LGVKVSVVEPG 243
Cdd:cd05341  155 KGAVRGLTKSAALECATqgYGIRVNSVHPG 184
PRK06482 PRK06482
SDR family oxidoreductase;
59-254 4.44e-21

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 91.33  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkdKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATV----RRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK06482  78 DV----VVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRqGGGRIVQVSSEGGQIAYPGFSLYHATKW 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG----NFIAATSLYSP 254
Cdd:PRK06482 154 GIEGFVEAVAQEVAPFGIEFTIVEPGpartNFGAGLDRGAP 194
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 62-278 6.46e-21

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: 90.05  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKG-FLVFAGClmKDKghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDpeK 140
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATC--RDP--SAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGD--A 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 141 GMWGLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP---YCIT 215
Cdd:cd05325   75 GLDVLINNAGILHsYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGArAKIINISSRVGSIGDNTSGGwysYRAS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPG--------NFIAATSLYSPESiqaIAKKMWEELPEVVRKDYGK 278
Cdd:cd05325  155 KAALNMLTKSLAVELKRDGITVVSLHPGwvrtdmggPFAKNKGPITPEE---SVAGLLKVIDNLNEEDSGK 222
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 58-246 7.11e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 89.97  E-value: 7.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAvLVTGCDSGFGFSLAKHLHSKGFLVfagclmkdkGHDG--VKELDSLNS---DRLRTVQLNVCSSEEVEKVVEIVR 132
Cdd:PRK12936   6 GRKA-LVTGASGGIGEEIARLLHAQGAIV---------GLHGtrVEKLEALAAelgERVKIFPANLSDRDEVKALGQKAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 133 SSLKdpekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARSP 211
Cdd:PRK12936  76 ADLE----GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQAN 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI 246
Cdd:PRK12936 152 YCASKAGMIGFSKSLAQEIATRNVTVNCVAPG-FI 185
PRK07832 PRK07832
SDR family oxidoreductase;
60-243 7.49e-21

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 90.49  E-value: 7.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclMKDKGHDG----VKELDSLNSdrlrTVQLNVCSSEEVEKVVEIVRSSL 135
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF----LTDRDADGlaqtVADARALGG----TVPEHRALDISDYDAVAAFAADI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 136 KDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGR-VVNISSMLGRMANPARSPYC 213
Cdd:PRK07832  73 HAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPWHAAYS 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07832 153 ASKFGLRGLSEVLRFDLARHGIGVSVVVPG 182
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-270 1.33e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 89.13  E-value: 1.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKG-FLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVcsseevekvveivrSSLKDP 138
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEGaKVVIAYDINEEAAQELLEEIKEEGGDAI-AVKADV--------------SSEEDV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKgMWG-----------LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMAN 206
Cdd:PRK05565  71 EN-LVEqivekfgkidiLVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGA 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927354 207 PARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfiaatslyspesiqAIAKKMWEELPE 270
Cdd:PRK05565 150 SCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPG---------------AIDTEMWSSFSE 198
PRK07326 PRK07326
SDR family oxidoreductase;
60-243 1.73e-20

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.91  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslNSDRLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN--NKGNVLGLAADV--------------RDEADVQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPAR 209
Cdd:PRK07326  71 RAVdaivaaFGgldvLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGG 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07326 151 AAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPG 184
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 60-269 2.07e-20

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: 88.90  E-value: 2.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGhdGVKELDSLN-SDRLRTVQLNVCSSEEVekvveivrSSLKDP 138
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINpKVKATFVQCDVTSWEQL--------AAAFKK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWG----LVNNAGISTFGEVEFTSLETY--KQVAEVNLWGTVRMTKSFLPLIRRAK----GRVVNISSMLGRMANPA 208
Cdd:cd05323   71 AIEKFGrvdiLINNAGILDEKSYLFAGKLPPpwEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQ 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEM-YPLGVKVSVVEPGnfIAATSLYspESIQAIAKKMWEELP 269
Cdd:cd05323  151 FPVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPG--FTNTPLL--PDLVAKEAEMLPSAP 208
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 60-269 2.79e-20

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: 87.89  E-value: 2.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgclmKDKGHDGVKELD-SLNSDRLRTVQLNVcsseeveKVVEIVRSSLKD- 137
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGL----YDIDEDGLAALAaELGAENVVAGALDV-------TDRAAWAAALADf 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 -PEKG--MWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYC 213
Cdd:cd08931   70 aAATGgrLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDLAVYS 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAATSLYSPESIQAIAKKMWEELP 269
Cdd:cd08931  150 ATKFAVRGLTEALDVEWARHGIRVADVWPW-FVDTPILTKGETGAAPKKGLGRVLP 204
PRK06181 PRK06181
SDR family oxidoreductase;
145-243 3.06e-20

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 88.50  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI---STFGEVefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK06181  82 LVNNAGItmwSRFDEL--TDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHG 159

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06181 160 FFDSLRIELADDGVAVTVVCPG 181
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 62-276 3.34e-20

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 88.03  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPEKG 141
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDV--------------SDREDVKAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  142 M------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARS 210
Cdd:TIGR01830  67 VeeieeeLGtidiLVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLrIMIKQRSGRIINISSVVGLMGNAGQA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354  211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRKDY 276
Cdd:TIGR01830 147 NYAASKAGVIGFTKSLAKELASRNITVNAVAPG-FIDT--------------DMTDKLSEKVKKKI 197
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 60-243 4.61e-20

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 87.42  E-value: 4.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAG--------CLMKDKGHDGVKELDSLNSDRLRTVQlnvcsseevekvveiv 131
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGlrnpedlaALSASGGDVEAVPYDARDPEDARALV---------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 132 rSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARS 210
Cdd:cd08932   65 -DALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGNA 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08932  144 GYSASKFALRALAHALRQEGWDHGVRVSAVCPG 176
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 60-243 5.81e-20

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: 87.18  E-value: 5.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfaGCLMKDKGhdgvkELDSLNSDRLRTVQLNVCSseevEKVVEIVRSSLKDPE 139
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRV--GICARDEA-----RLAAAAAQELEGVLGLAGD----VRDEADVRRAVDAME 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 K---GMWGLVNNAGISTFGEV-EFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCIT 215
Cdd:cd08929   70 EafgGLDALVNNAGVGVMKPVeELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNAS 149

                        170       180
                 ....*....|....*....|....*...
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08929  150 KFGLLGLSEAAMLDLREANIRVVNVMPG 177
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 146-240 6.77e-20

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: 87.05  E-value: 6.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 146 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 224
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                         90
                 ....*....|....*.
gi 767927354 225 CLRYEMYPLGVKVSVV 240
Cdd:cd05360  162 SLRAELAHDGAPISVT 177
PRK08219 PRK08219
SDR family oxidoreductase;
58-243 7.06e-20

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 86.91  E-value: 7.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkdkghdgvkeldsLNSDRLRTVQLNVCSSEEVEkvveivrSSLKD 137
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAPTHTLLLGG----------------RPAERLDELAAELPGATPFP-------VDLTD 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKGMWG---------LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPA 208
Cdd:PRK08219  59 PEAIAAAveqlgrldvLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPG 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMyPLGVKVSVVEPG 243
Cdd:PRK08219 139 WGSYAASKFALRALADALREEE-PGNVRVTSVHPG 172
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 59-264 9.99e-20

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 86.72  E-value: 9.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:PRK12937  83 --RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGPYAASKAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNfiAATSLY----SPESIQAIAKKM 264
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGP--VATELFfngkSAEQIDQLAGLA 207
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 51-239 1.85e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 86.95  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  51 ASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVfagCLMkdkGHDGvKELDSL-----NSDRLRTVQLNVCSSEEVE 125
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKL---ALV---DLEE-AELAALaaelgGDDRVLTVVADVTDLAAMQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 126 KVVEIVRSSLKDPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMA 205
Cdd:PRK05872  74 AAAEEAVERFGGIDV----VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAA 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSV 239
Cdd:PRK05872 150 APGMAAYCASKAGVEAFANALRLEVAHHGVTVGS 183
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 146-239 1.92e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 87.67  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 146 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 224
Cdd:PRK07109  90 VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTD 169

                         90
                 ....*....|....*
gi 767927354 225 CLRYEMYPLGVKVSV 239
Cdd:PRK07109 170 SLRCELLHDGSPVSV 184
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 59-254 2.42e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 86.25  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgVKELDSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDP 138
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTAT----LADLAEKYGDRLLPLALDVTDRAAV-------FAAVETA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWGL---VNNAGISTFGEVE-FTSLETYKQVaEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYC 213
Cdd:PRK08263  72 VEHFGRLdivVNNAGYGLFGMIEeVTESEARAQI-DTNFFGALWVTQAVLPYLREqRSGHIIQISSIGGISAFPMSGIYH 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYSP 254
Cdd:PRK08263 151 ASKWALEGMSEALAQEVAEFGIKVTLVEPGGY--STDWAGT 189
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 144-264 3.53e-19

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: 85.17  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  144 GLVNNAGISTFGEVEF--TSLETYKQVAEVNLWGTVRMTKSFLPLIRRaKGRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:pfam13561  74 ILVNNAGFAPKLKGPFldTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767927354  222 FSDCLRYEMYPLGVKVSVVEPGnFI---AATSLYSPESIQAIAKKM 264
Cdd:pfam13561 153 LTRYLAVELGPRGIRVNAISPG-PIktlAASGIPGFDELLAAAEAR 197
PRK09072 PRK09072
SDR family oxidoreductase;
59-242 6.41e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 84.99  E-value: 6.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKG-FLVFAGclmKDKGhdgvkELDSL-----NSDRLRTVQLNVCSSEEVEKVVEIVR 132
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGaRLLLVG---RNAE-----KLEALaarlpYPGRHRWVVADLTSEAGREAVLARAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 133 SslkdpEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSP 211
Cdd:PRK09072  77 E-----MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGYAS 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:PRK09072 152 YCASKFALRGFSEALRRELADTGVRVLYLAP 182
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 145-242 7.76e-19

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 84.36  E-value: 7.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                         90
                 ....*....|....*....
gi 767927354 224 DCLRYEMYPLGVKVSVVEP 242
Cdd:PRK07666 168 ESLMQEVRKHNIRVTALTP 186
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-244 1.04e-18

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 84.15  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDGVKELDSL---NSDRLRTVQLNVCSseevekvVEIVRSSLK 136
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHY---RSDEEAAEELVEAveaLGRRAQAVQADVTD-------KAALEAAVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEK---GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPY 212
Cdd:PRK12825  77 AAVErfgRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNY 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 213 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN 244
Cdd:PRK12825 157 AAAKAGLVGLTKALARELAEYGITVNMVAPGD 188
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 59-243 1.83e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 83.48  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAH-AIAADLADPASVQRFFDAAAAALG-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK12939  84 --GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGrGRIVNLASDTALWGAPKLGAYVASKG 161

                        170       180
                 ....*....|....*....|....*.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPG 187
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 58-243 3.13e-18

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 82.65  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAVlVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivRSSLKD 137
Cdd:cd05356    1 GTWAV-VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERI---EKELEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKGMwgLVNNAGISTFGEVEF--TSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 214
Cdd:cd05356   77 LDIGI--LVNNVGISHSIPEYFleTPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTPLLATYSA 154

                        170       180
                 ....*....|....*....|....*....
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05356  155 SKAFLDFFSRALYEEYKSQGIDVQSLLPY 183
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 145-243 9.69e-18

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 81.13  E-value: 9.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd05339   80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                         90       100
                 ....*....|....*....|...
gi 767927354 224 DCLRYEM---YPLGVKVSVVEPG 243
Cdd:cd05339  160 ESLRLELkayGKPGIKTTLVCPY 182
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 60-244 1.31e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 81.00  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-LDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARG----ARVALIGRGAAPLSQtLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK12828  82 --RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGMGAYAAAKA 159

                        170       180
                 ....*....|....*....|....*..
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPGN 244
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSI 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 60-237 1.31e-17

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 80.43  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlnsdrLRTVQLNVCSSEEVEKVVEIVRSslKDPE 139
Cdd:cd05370    6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-----IHTIVLDVGDAESVEALAEALLS--EYPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMwgLVNNAGISTfgEVEFTSLETYKQVAE----VNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLG---RMANPArsp 211
Cdd:cd05370   79 LDI--LINNAGIQR--PIDLRDPASDLDKADteidTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAfvpMAANPV--- 151

                        170       180
                 ....*....|....*....|....*.
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKV 237
Cdd:cd05370  152 YCATKAALHSYTLALRHQLKDTGVEV 177
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 60-253 1.55e-17

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: 80.92  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAkhlhskgfLVFA--GCLMKDKGHdgvkeldslNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKD 137
Cdd:cd05364    4 KVAIITGSSSGIGAGTA--------ILFArlGARLALTGR---------DAERLEETRQSCLQAGVSEKKILLVVADLTE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEK---------GMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRM 204
Cdd:cd05364   67 EEGqdriisttlAKFGrldiLVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGR 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767927354 205 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYS 253
Cdd:cd05364  147 SFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPG--VIVTGFHR 193
PRK08267 PRK08267
SDR family oxidoreductase;
60-266 1.73e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 80.75  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkDKGHDGVKEL-DSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDP 138
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAY----DINEAGLAALaAELGAGNAWTGALDVTDRAAW-------DAALADF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYC 213
Cdd:PRK08267  71 AAATGGrldvLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAIYGQPGLAVYS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG-----------NFIAATSLYS------PESiqaIAKKMWE 266
Cdd:PRK08267 151 ATKFAVRGLTEALDLEWRRHGIRVADVMPLfvdtamldgtsNEVDAGSTKRlgvrltPED---VAEAVWA 217
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 60-262 7.14e-17

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: 78.86  E-value: 7.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEkvveivrsSLKDPE 139
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVA--------RLFDAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCIT 215
Cdd:cd05362   76 EKAFGgvdiLVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTPNYGAYAGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPGNfiAATSLY----SPESIQAIAK 262
Cdd:cd05362  155 KAAVEAFTRVLAKELGGRGITVNAVAPGP--VDTDMFyagkTEEAVEGYAK 203
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 62-243 1.47e-16

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: 77.71  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPEKG 141
Cdd:cd05367    2 IILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLL----EAIRKLDGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 142 MWGLVNNAG-ISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI--RRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:cd05367   78 RDLLINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                        170       180
                 ....*....|....*....|....*
gi 767927354 219 VEAFSDCLRYEMYplGVKVSVVEPG 243
Cdd:cd05367  158 RDMFFRVLAAEEP--DVRVLSYAPG 180
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 144-270 1.67e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 78.08  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNA-GISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07890  85 ALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAA 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG-----------NFIAATSLYSPESI-QAIAKKM-WEELPE 270
Cdd:PRK07890 165 SQSLATELGPQGIRVNSVAPGyiwgdplkgyfRHQAGKYGVTVEQIyAETAANSdLKRLPT 225
PRK07454 PRK07454
SDR family oxidoreductase;
145-259 1.80e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 77.69  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRaRGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFT 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGNfiAATSLYSPESIQA 259
Cdd:PRK07454 167 KCLAEEERSHGIRVCTITLGA--VNTPLWDTETVQA 200
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 59-243 6.49e-16

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: 76.42  E-value: 6.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFaGClmkdkGHDGVKELDSLnsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:cd08945    3 SEVALVTGATSGIGLAIARRLGKEGLRVF-VC-----ARGEEGLATTV--KELREAGVEADGRTCDVRSVPEIEALVAAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 eKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP---LIRRAKGRVVNISSMLGRMANPARSP 211
Cdd:cd08945   75 -VARYGpidvLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAP 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08945  154 YSASKHGVVGFTKALGLELARTGITVNAVCPG 185
PRK08264 PRK08264
SDR family oxidoreductase;
145-243 1.03e-15

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 75.31  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK08264  77 LVNNAGIfRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSL 156

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08264 157 TQALRAELAPQGTRVLGVHPG 177
PRK06484 PRK06484
short chain dehydrogenase; Validated
 59-243 4.74e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 76.04  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfagcLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRsslkdp 138
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRL----LIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQ------ 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWG----LVNNAGIS-TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYC 213
Cdd:PRK06484 339 --ARWGrldvLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYC 415

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06484 416 ASKAAVTMLSRSLACEWAPAGIRVNTVAPG 445
PRK05855 PRK05855
SDR family oxidoreductase;
145-243 5.61e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 75.79  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAK-GRVVNISSMLGRManPARS--PYCITKFGVE 220
Cdd:PRK05855 396 VVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRqMVERGTgGHIVNVASAAAYA--PSRSlpAYATSKAAVL 473

                         90       100
                 ....*....|....*....|...
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK05855 474 MLSECLRAELAAAGIGVTAICPG 496
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 145-268 6.85e-15

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: 73.72  E-value: 6.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd08933   91 LVNNAGWHPPHQtTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAITAMT 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGNfiaatsLYSPesiqaiakkMWEEL 268
Cdd:cd08933  171 KALAVDESRYGVRVNCISPGN------IWTP---------LWEEL 200
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 62-237 7.82e-15

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: 72.89  E-value: 7.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkdkGHDGVKeLDSLNSDR--LRTVQLNVCSSEEvekvveivRSSLKD-- 137
Cdd:COG3967    8 ILITGGTSGIGLALAKRLHARGNTVIIT------GRREEK-LEEAAAANpgLHTIVLDVADPAS--------IAALAEqv 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 ----PEKGMwgLVNNAGIS---TFGEVEFTsLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRManP-A 208
Cdd:COG3967   73 taefPDLNV--LINNAGIMraeDLLDEAED-LADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFV--PlA 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 209 RSP-YCITKFGVEAFSDCLRYEMYPLGVKV 237
Cdd:COG3967  148 VTPtYSATKAALHSYTQSLRHQLKDTSVKV 177
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 145-292 1.33e-14

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: 71.39  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMkAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGNfiaatslyspesiqaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYC 292
Cdd:cd02266  115 QQWASEGWGNGLPATAVACGT---------------WAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVA 168
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 60-245 1.75e-14

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: 72.01  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIV--------INSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMwG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 214
Cdd:cd05347   78 EDF-GkidiLVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLLSELGGPPVPAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYF 187
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 56-279 2.54e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 72.01  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  56 PVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVfAGClmkdkghdGVKElDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSL 135
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGARV-HVC--------DVSE-AALAATAARLPGAKVTATVADVADPAQVERVF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 136 KDPEKGMWGL---VNNAGIS--TFGeVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR--RAKGRVVNISSMLGRMANPA 208
Cdd:PRK12829  78 DTAVERFGGLdvlVNNAGIAgpTGG-IDEITPEQWEQTLAVNLNGQFYFARAAVPLLKasGHGGVIIALSSVAGRLGYPG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNfiaatsLYSPES---IQAIAKKMWEELPEvVRKDYGKK 279
Cdd:PRK12829 157 RTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGI------VRGPRMrrvIEARAQQLGIGLDE-MEQEYLEK 223
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 60-273 3.14e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 68.59  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDkghdgVKELDSLNSDR-LRTVQLNVCSSEEVekvveivRSSLKdp 138
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVA--AARN-----AAALDRLAGETgCEPLRLDVGDDAAI-------RAALA-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMW-GLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA--KGRVVNISSMLGRMANPARSPYCIT 215
Cdd:PRK07060  74 AAGAFdGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLPDHLAYCAS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPG---NFIAATSLYSPES----IQAIAKKMWEELPEVVR 273
Cdd:PRK07060 154 KAALDAITRVLCVELGPHGIRVNSVNPTvtlTPMAAEAWSDPQKsgpmLAAIPLGRFAEVDDVAA 218
PRK06484 PRK06484
short chain dehydrogenase; Validated
 59-243 3.59e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 70.26  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfagcLMKDKGHDGVKEL-DSLNSDRlRTVQLNVcsseevekvveivrSSLKD 137
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQV----VVADRNVERARERaDSLGPDH-HALAMDV--------------SDEAQ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKGMWGL----------VNNAGIS--TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGR 203
Cdd:PRK06484  66 IREGFEQLhrefgridvlVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGL 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767927354 204 MANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06484 146 VALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPG 185
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 56-271 4.48e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 68.21  E-value: 4.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  56 PVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDgvkELDSLNSD------RLRTVQLNVcsseeveKVVE 129
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRA---EADAVAAGieaaggKALGLAFDV-------RDFA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 130 IVRSSLKDPEK---GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIR-RAKGRVVNISSMLGRM 204
Cdd:PRK12827  73 ATRAALDAGVEefgRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRaRRGGRIVNIASVAGVR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 205 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG---NFIAATSLYSPESIQAIAKKMWEELPEV 271
Cdd:PRK12827 153 GNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGainTPMADNAAPTEHLLNPVPVQRLGEPDEV 222
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 60-243 4.71e-13

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: 68.24  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAG----ANIVLNGFGDA--AEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWG---LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCIT 215
Cdd:cd08940   77 RQFGGvdiLVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKkQGWGRIINIASVHGLVASANKSAYVAA 156

                        170       180
                 ....*....|....*....|....*...
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08940  157 KHGVVGLTKVVALETAGTGVTCNAICPG 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 59-287 4.79e-13

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 68.17  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKD 137
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFnIVLADLNLEEAAKSTIQEISEAGYNAV-AVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVN----LWGTVRMTKSFLPLIRraKGRVVNISSMLGRMANPARSPYC 213
Cdd:cd05366   81 FDV----MVNNAGIAPITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFKKLGH--GGKIINASSIAGVQGFPNLGAYS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSlyspesiqaiakkMWEELPEVVRK------DYGKKYFDEKIAK 287
Cdd:cd05366  155 ASKFAVRGLTQTAAQELAPKGITVNAYAPG--IVKTE-------------MWDYIDEEVGEiagkpeGEGFAEFSSSIPL 219
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
59-278 6.42e-13

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 67.83  E-value: 6.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAI-AVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVN----LWGTVRMTKSFLPLirRAKGRVVNISSMLGRMANPARSPYCI 214
Cdd:PRK08643  81 NV----VVNNAGVAPTTPIETITEEQFDKVYNINvggvIWGIQAAQEAFKKL--GHGGKIINATSQAGVVGNPELAVYSS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSlyspesiqaiakkMWEELPEVVRKDYGK 278
Cdd:PRK08643 155 TKFAVRGLTQTAARDLASEGITVNAYAPG--IVKTP-------------MMFDIAHQVGENAGK 203
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 62-243 1.22e-12

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 66.70  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAgclmKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 141
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIA----TGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 142 mwgLVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGV 219
Cdd:PRK10538  78 ---LVNNAGLALGLEpAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154

                        170       180
                 ....*....|....*....|....
gi 767927354 220 EAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK10538 155 RQFSLNLRTDLHGTAVRVTDIEPG 178
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 56-242 1.22e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 66.99  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  56 PVGSKAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLRTVQLNV--CSSEEVEKVVEIVRS 133
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKG----ARVALLDRSEDVAEVAAQLLGGNAKGLVCDVsdSQSVEAAVAAVISAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 134 SLKDPekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPY 212
Cdd:PRK06841  88 GRIDI------LVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHVAY 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 213 CITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:PRK06841 162 CASKAGVVGMTKVLALEWGPYGITVNAISP 191
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 60-243 1.53e-12

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 66.45  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVI--------GFD--QAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmlgrmaNPARSP------Y 212
Cdd:PRK08220  79 V----LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGS------NAAHVPrigmaaY 148

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767927354 213 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08220 149 GASKAALTSLAKCVGLELAPYGVRCNVVSPG 179
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 62-247 1.55e-12

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: 66.20  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 141
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNP-SVEVEILDVTDEERNQLVIAELEAELGGLDL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 142 mwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:cd05350   79 ---VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGrGHLVLISSVAALRGLPGAAAYSASKAALS 155

                        170       180
                 ....*....|....*....|....*..
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPGnFIA 247
Cdd:cd05350  156 SLAESLRYDVKKRGIRVTVINPG-FID 181
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
64-243 2.32e-12

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 66.19  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  64 VTGCDSGFGFSLAKHLHSKGFLVFAGClmkdkGHDGVKELDSLnsDRLRTVQLNVCSSEEVEKVVEIVRSSLkDPEKGMW 143
Cdd:PRK12938   8 VTGGMGGIGTSICQRLHKDGFKVVAGC-----GPNSPRRVKWL--EDQKALGFDFIASEGNVGDWDSTKAAF-DKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 G----LVNNAGISTfgEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITK 216
Cdd:PRK12938  80 GeidvLVNNAGITR--DVVFRKMtrEDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGQTNYSTAK 157

                        170       180
                 ....*....|....*....|....*..
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPG 184
FabG-like PRK07231
SDR family oxidoreductase;
60-243 2.37e-12

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 66.01  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlnSDRLRTVQLNVCSSEEvekvveivRSSLKDPE 139
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--GGRAIAVAADVSDEAD--------VEAAVAAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWG----LVNNAGIS-TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 213
Cdd:PRK07231  76 LERFGsvdiLVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07231 156 ASKGAVITLTKALAAELGPDKIRVNAVAPV 185
PRK06138 PRK06138
SDR family oxidoreductase;
60-243 3.39e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 65.56  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKG-FLVFAgclmkDKGHDG-VKELDSLNSD-RLRTVQLNVCSSEEVekvveivrSSLK 136
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGaRVVVA-----DRDAEAaERVAAAIAAGgRAFARQGDVGSAEAV--------EALV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP 211
Cdd:PRK06138  73 DFVAARWGrldvLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAA 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06138 153 YVASKGAIASLTRAMALDHATDGIRVNAVAPG 184
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-254 4.76e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 65.37  E-value: 4.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEvekvveivRSSLKDP 138
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFdLAINDRPDDEELAATQQELRALGV-EVIFFPADVADLSA--------HEAMLDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWG----LVNNAGISTF--GEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGR------VVNISSMLGRMA 205
Cdd:PRK12745  74 AQAAWGridcLVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKrMLAQPEPEelphrsIVFVSSVNAIMV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYSP 254
Cdd:PRK12745 154 SPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPG--LIKTDMTAP 200
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 63-264 6.85e-12

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: 64.79  E-value: 6.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  63 LVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSseevekvvEIVRSSLKDPEKGM 142
Cdd:cd05337    5 IVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGE--------LSDHEALLDQAWED 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 143 WG----LVNNAGISTFGEVEFTSL--ETYKQVAEVNLWGTVRMTKSF-LPLIRRAK------GRVVNISSMLGRMANPAR 209
Cdd:cd05337   77 FGrldcLVNNAGIAVRPRGDLLDLteDSFDRLIAINLRGPFFLTQAVaRRMVEQPDrfdgphRSIIFVTSINAYLVSPNR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAA--TSLYSPESIQAIAKKM 264
Cdd:cd05337  157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPG-LIHTdmTAPVKEKYDELIAAGL 212
PRK07775 PRK07775
SDR family oxidoreductase;
62-243 7.92e-12

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 64.78  E-value: 7.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 141
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAV-AFPLDVTDPDSVKSFVAQAEEALGEIEV- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 142 mwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:PRK07775  91 ---LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167

                        170       180
                 ....*....|....*....|...
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07775 168 AMVTNLQMELEGTGVRASIVHPG 190
PRK07201 PRK07201
SDR family oxidoreductase;
54-225 8.29e-12

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 66.13  E-value: 8.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  54 AEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdrlrTVQLNVCSseevekvveivrs 133
Cdd:PRK07201 366 RGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG----TAHAYTCD------------- 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 134 sLKDPE------KGMWG-------LVNNAGISTFGEVE--FTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNI 197
Cdd:PRK07201 429 -LTDSAavdhtvKDILAehghvdyLVNNAGRSIRRSVEnsTDRFHDYERTMAVNYFGAVRLILGLLPHMReRRFGHVVNV 507

                        170       180
                 ....*....|....*....|....*....
gi 767927354 198 SSmLGRMANPAR-SPYCITKFGVEAFSDC 225
Cdd:PRK07201 508 SS-IGVQTNAPRfSAYVASKAALDAFSDV 535
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 60-296 1.13e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 63.87  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC-LMKDKGHDGVKELDSlNSDRLRTVQLNVcsseevekVVEIVRSSLKDP 138
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINYnSSKEAAENLVNELGK-EGHDVYAVQADV--------SKVEDANRLVEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 213
Cdd:PRK12935  78 AVNHFGkvdiLVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTNYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAiakKMWEELPevvRKDYGKKyfdEKIAKMETY-C 292
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQ---KIVAKIP---KKRFGQA---DEIAKGVVYlC 228


                 ....
gi 767927354 293 SSGS 296
Cdd:PRK12935 229 RDGA 232
PRK08589 PRK08589
SDR family oxidoreductase;
59-243 1.45e-11

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 64.03  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDP 138
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAYVLAVDI-AEAVSETVDKIKS-NGGKAKAYHVDISDEQQVKDFA----SEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWGLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK08589  80 FGRVDVLFNNAGVDNaAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKG 159

                        170       180
                 ....*....|....*....|....*.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08589 160 AVINFTKSIAIEYGRDGIRANAIAPG 185
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-243 1.65e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 63.44  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKvveivrSSLKDPE 139
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFLAQGAQVY--------GVD--KQDKPDLSGNFHFLQLDLSDDLEPLF------DWVPSVD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KgmwgLVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK06550  70 I----LCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVAGGGGAAYTASKH 145

                        170       180
                 ....*....|....*....|....*.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06550 146 ALAGFTKQLALDYAKDGIQVFGIAPG 171
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 59-243 1.80e-11

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 63.65  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFagcLMKDKGHDGVKELDSLNSDrlrTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVA---VLYNSAENEAKELREKGVF---TIKCDVGNRDQVKKSKEVVEKEFGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGrMANPARSP--YCIT 215
Cdd:PRK06463  81 DV----LVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAG-IGTAAEGTtfYAIT 155

                        170       180
                 ....*....|....*....|....*...
gi 767927354 216 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPG 183
PRK07577 PRK07577
SDR family oxidoreductase;
59-243 2.88e-11

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 62.44  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDKGHDGVKELDSLN-SDRLRTvqlnvcsseevekvveivRSSLKD 137
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDFPGELFACDlADIEQT------------------AATLAQ 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 --PEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmLGRMANPARSPYCI 214
Cdd:PRK07577  63 inEIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEgMKLREQGRIVNICS-RAIFGALDRTSYSA 141

                        170       180
                 ....*....|....*....|....*....
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07577 142 AKSALVGCTRTWALELAEYGITVNAVAPG 170
PRK07831 PRK07831
SDR family oxidoreductase;
145-242 5.34e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 62.36  E-value: 5.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07831 101 LVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhgGVIVNNASVLGWRAQHGQAHYAAAKAGVMAL 180

                         90       100
                 ....*....|....*....|
gi 767927354 223 SDCLRYEMYPLGVKVSVVEP 242
Cdd:PRK07831 181 TRCSALEAAEYGVRINAVAP 200
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 60-274 6.07e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 62.22  E-value: 6.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-LDSLNSDRLRTVQL--NVCSSEEVEKVVEIVRSSLK 136
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAG----AAVAIADLNQDGANAvADEINKAGGKAIGVamDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCI 214
Cdd:PRK13394  84 SVDI----LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYVT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIaATSLYSPEsIQAIAKKMWEELPEVVRK 274
Cdd:PRK13394 160 AKHGLLGLARVLAKEGAKHNVRSHVVCPG-FV-RTPLVDKQ-IPEQAKELGISEEEVVKK 216
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 60-269 9.09e-11

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: 61.19  E-value: 9.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:cd05352    9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSF-LPLIRRAKGRVVNISSMLGRMAN-PA-RSPYCITK 216
Cdd:cd05352   89 ----ILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAaKIFKKQGKGSLIITASMSGTIVNrPQpQAAYNASK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaiaKKMWEELP 269
Cdd:cd05352  165 AAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELR---KKWESYIP 214
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 62-243 9.49e-11

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 61.33  E-value: 9.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLVFA-----GCLMKDKGHDGVKELDSLNSDRLRTVQlnvcsseevekvveivrSSLK 136
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIAldlpfVLLLEYGDPLRLTPLDVADAAAVREVC-----------------SRLL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmlgrmaNPARSP---- 211
Cdd:cd05331   64 AEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRRTGAIVTVAS------NAAHVPrism 137

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767927354 212 --YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05331  138 aaYGASKAALASLSKCLGLELAPYGVRCNVVSPG 171
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 60-243 9.93e-11

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: 61.14  E-value: 9.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDKGHDGVKELDSLNSDRLRTVQlnvcsseevekvveivrSSLKDPE 139
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARV-AICARNRENLERAASELRAGGAGVLAVV-----------------ADLTDPE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 ---------KGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMA 205
Cdd:cd05344   64 didrlvekaGDAFGrvdiLVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPgMKERGWGRIVNISSLTVKEP 143

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05344  144 EPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPG 181
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 144-243 1.07e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.04  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK08945  95 GVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQGRANWGAYAVSKFATEG 174

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08945 175 MMQVLADEYQGTNLRVNCINPG 196
PRK12746 PRK12746
SDR family oxidoreductase;
60-243 1.35e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 60.82  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLV-FAGCLMKDKGHDGVKELDSlNSDR--LRTVQLNVCSSEEVEKVVEIVRSSLK 136
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIES-NGGKafLIEADLNSIDGVKKLVEQLKNELQIR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIrRAKGRVVNISSMLGRMANPARSPYCITK 216
Cdd:PRK12746  86 VGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL-RAEGRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180
                 ....*....|....*....|....*..
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12746 165 GALNTMTLPLAKHLGERGITVNTIMPG 191
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 59-247 2.19e-10

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: 60.04  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EkgmwGLVNNAGISTFGEVE-FT--SLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMA-------NP 207
Cdd:cd08930   82 D----ILINNAYPSPKVWGSrFEefPYEQWNEVLNVNLGGAFLCSQAFIKLFkKQGKGSIINIASIYGVIApdfriyeNT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767927354 208 AR-SP--YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIA 247
Cdd:cd08930  158 QMySPveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILN 200
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 145-272 2.80e-10

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: 59.71  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd05338   96 LVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSLRPARGDVAYAAGKAGMSRLT 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGNFI--AATSLYSPESIQAIAKKmweelPEVV 272
Cdd:cd05338  176 LGLAAELRRHGIAVNSLWPSTAIetPAATELSGGSDPARARS-----PEIL 221
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
60-243 3.33e-10

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 59.81  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLR--TVQLNVCSSEEVekvveivRSSLKD 137
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHG----ANLILLDISPEIEKLADELCGRGHRctAVVADVRDPASV-------AAAIKR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKgMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM-ANPARSP 211
Cdd:PRK08226  76 AKE-KEGridiLVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMvADPGETA 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08226 155 YALTKAAIVGLTKSLAVEYAQSGIRVNAICPG 186
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 145-243 4.38e-10

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: 59.43  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:cd08944   81 LVNNAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08944  161 TRTLAAELRHAGIRCNALAPG 181
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 60-243 7.80e-10

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 58.74  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGcLMKDKGHDGVKELDSLNSDRLrTVQLNVcsseevekvveivrSSLKDP 138
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAkVVIAD-LNDEAAAAAAEALQKAGGKAI-GVAMDV--------------TDEEAI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANP 207
Cdd:PRK12429  69 NAGIdyavetFGgvdiLVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSA 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767927354 208 ARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12429 149 GKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPG 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
 145-242 8.35e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.57  E-value: 8.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKAAVASLT 162

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767927354 224 -----DCLRYEM-------YPLGVKVSVVEP 242
Cdd:PRK07069 163 ksialDCARRGLdvrcnsiHPTFIRTGIVDP 193
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 145-243 9.33e-10

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: 58.31  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANpaRSPYCITKFGVEAF 222
Cdd:cd08937   84 LINNVGGTIWAKpYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATRGIY--RIPYSAAKGGVNAL 161

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08937  162 TASLAFEHARDGIRVNAVAPG 182
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 145-254 1.04e-09

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: 58.23  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd05329   88 LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAsGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLT 167

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGnfIAATSLYSP 254
Cdd:cd05329  168 RSLACEWAKDNIRVNAVAPW--VIATPLVEP 196
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 145-263 1.17e-09

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: 58.16  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTV--------RMTKSflplirRAKGRVVNISSMLGRMANPARSPYCITK 216
Cdd:cd05358   85 LVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFlcareaikRFRKS------KIKGKIINMSSVHEKIPWPGHVNYAASK 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPGNF---IAATSLYSPESIQAIAKK 263
Cdd:cd05358  159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAIntpINAEAWDDPEQRADLLSL 208
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
60-264 1.50e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 59.09  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslNSDRLRTVQLNVCSseevekvveivRSSLKDP- 138
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELG--GPDRALGVACDVTD-----------EAAVQAAf 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKG--MWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARS 210
Cdd:PRK08324 490 EEAalAFGgvdiVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIASKNAVNPGPNFG 569

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKM 264
Cdd:PRK08324 570 AYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVRGSGIWTGEWIEARAAAY 623
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 60-269 1.93e-09

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: 57.21  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfagCLM---KDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrsslK 136
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFAELGASV---AIAgrkPEVLEAAAEEISSATGGRAHPIQCDV-----------------R 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPE------KGMW-------GLVNNAG---ISTFGEVeftSLETYKQVAEVNLWGTVRMTKSFLP-LIRR-AKGRVVNIS 198
Cdd:cd05369   64 DPEaveaavDETLkefgkidILINNAAgnfLAPAESL---SPNGFKTVIDIDLNGTFNTTKAVGKrLIEAkHGGSILNIS 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927354 199 SMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKMWEELP 269
Cdd:cd05369  141 ATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVP 211
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 60-267 2.37e-09

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: 57.02  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDKGHDGVKElDSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDPE 139
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAV-VVADIDPEIAEKVAE-AAQGGPRALGVQCDVTSEAQV-------QSAFEQAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGL---VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCI 214
Cdd:cd08943   73 LEFGGLdivVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 215 TKFGVEAFSDCLRYEMYPLGVKVSVVEPgNFIAATSLYSPESIQ---AIAKKMWEE 267
Cdd:cd08943  153 AKAAEAHLARCLALEGGEDGIRVNTVNP-DAVFRGSKIWEGVWRaarAKAYGLLEE 207
PRK06398 PRK06398
aldose dehydrogenase; Validated
 60-289 2.83e-09

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 57.15  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmKDKGHDGVK--ELDSLNSDRLRTVQLNVCSSEEvekvveivRSSLkd 137
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI-KEPSYNDVDyfKVDVSNKEQVIKGIDYVISKYG--------RIDI-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 pekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITK 216
Cdd:PRK06398  76 -------LVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRNAAAYVTSK 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927354 217 FGVEAFSDCLRYEMYPLgVKVSVVEPGnfiaatSLYSPESIQAIAKKMWEELPEVVRK--DYGKKYFDEKIAKME 289
Cdd:PRK06398 149 HAVLGLTRSIAVDYAPT-IRCVAVCPG------SIRTPLLEWAAELEVGKDPEHVERKirEWGEMHPMKRVGKPE 216
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 147-253 3.69e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 56.89  E-value: 3.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 147 NNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP--LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 224
Cdd:PRK05876  89 SNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAE 168

                         90       100
                 ....*....|....*....|....*....
gi 767927354 225 CLRYEMYPLGVKVSVVEPgnFIAATSLYS 253
Cdd:PRK05876 169 TLAREVTADGIGVSVLCP--MVVETNLVA 195
PRK07774 PRK07774
SDR family oxidoreductase;
59-243 4.25e-09

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 56.29  E-value: 4.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELdSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQI-VADGGTAIAVQVDVSDPDSAKAMADATVSAFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGIstFGEVEFTSLET-----YKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMlgrMANPARSPY 212
Cdd:PRK07774  83 --GIDYLVNNAAI--YGGMKLDLLITvpwdyYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSST---AAWLYSNFY 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767927354 213 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPG 186
PRK07063 PRK07063
SDR family oxidoreductase;
60-243 7.65e-09

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 55.83  E-value: 7.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKEL-DSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIaRDVAGARVLAVPADVTDAASVAAAVAAAEEAFG-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK07063  86 --PLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180
                 ....*....|....*....|....*.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPG 189
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 60-261 8.65e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 55.79  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDgvkeldslnsDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 139
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH----------ENYQFVPTDVSSAEEVNHTV----AEIIEKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGIS----------TFGEVEFTSlETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 208
Cdd:PRK06171  76 GRIDGLVNNAGINiprllvdekdPAGKYELNE-AAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAATSLYSPESIQAIA 261
Cdd:PRK06171 155 QSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPG-ILEATGLRTPEYEEALA 206
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 60-242 9.78e-09

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: 55.17  E-value: 9.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDKghdgvKELDSLNSD--RLRTVQLNVcsseevekvveivrSSLKD 137
Cdd:cd05351    8 KRALVTGAGKGIGRATVKALAKAGARVVA--VSRTQ-----ADLDSLVREcpGIEPVCVDL--------------SDWDA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEKGMW------GLVNNAGIST---FGEVeftSLETYKQVAEVNLWGTVRMTKSFLP-LI-RRAKGRVVNISSMLGRMAN 206
Cdd:cd05351   67 TEEALGsvgpvdLLVNNAAVAIlqpFLEV---TKEAFDRSFDVNVRAVIHVSQIVARgMIaRGVPGSIVNVSSQASQRAL 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767927354 207 PARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:cd05351  144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNP 179
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 145-245 1.26e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 54.95  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSF--LPLIRRAKGRVVNISSMLGRMANPARSP----YCITKFG 218
Cdd:PRK08213  93 LVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVakRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNTSKGA 172

                         90       100
                 ....*....|....*....|....*..
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK08213 173 VINFTRALAAEWGPHGIRVNAIAPGFF 199
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
60-287 1.38e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 55.07  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKG--------HDG----------VKELDSLNSDRLRTVQLNVCSS 121
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKEltklaeqyNSNltfhsldlqdVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 122 EEvekvveivrsslkdpekgmwgLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG--RVVNIS 198
Cdd:PRK06924  82 IH---------------------LINNAGMVApIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINIS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 199 SMLGRMANPARSPYCITKFGVEAFSDCLRYEM----YPlgVKVSVVEPGnfIAATSLysPESIQAIAKKMWEELPEVVR- 273
Cdd:PRK06924 141 SGAAKNPYFGWSAYCSSKAGLDMFTQTVATEQeeeeYP--VKIVAFSPG--VMDTNM--QAQIRSSSKEDFTNLDRFITl 214

                        250
                 ....*....|....
gi 767927354 274 KDYGKKYFDEKIAK 287
Cdd:PRK06924 215 KEEGKLLSPEYVAK 228
PRK07024 PRK07024
SDR family oxidoreductase;
148-243 1.52e-08

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 54.94  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 148 NAGIS--TFGEvEFTSLETYKQVAEVNLWGTVrmtKSFLPLI----RRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK07024  85 NAGISvgTLTE-EREDLAVFREVMDTNYFGMV---ATFQPFIapmrAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIK 160

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07024 161 YLESLRVELRPAGVRVVTIAPG 182
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 60-273 1.66e-08

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: 54.59  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDGVKEL-DSLNSDRLR--TVQLNVCSSEEVEKvveivrssLK 136
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHY---NRSEAEAQRLkDELNALRNSavLVQADLSDFAACAD--------LV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNIS-SMLGRmANPARS 210
Cdd:cd05357   70 AAAFRAFGrcdvLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAgSRNGSIINIIdAMTDR-PLTGYF 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLgVKVSVVEPGNFIAATSLYSPESIQAIAK---KMWEELPEVVR 273
Cdd:cd05357  149 AYCMSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEDMDAEYRENALRKvplKRRPSAEEIAD 213
PRK12743 PRK12743
SDR family oxidoreductase;
145-243 2.38e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 54.27  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGtvrmtkSFLPLIRRAK--------GRVVNISSMLGRMANPARSPYCITK 216
Cdd:PRK12743  84 LVNNAGAMTKAPFLDMDFDEWRKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEHTPLPGASAYTAAK 157

                         90       100
                 ....*....|....*....|....*..
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12743 158 HALGGLTKAMALELVEHGILVNAVAPG 184
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-262 2.45e-08

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 54.20  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVEIVRSSLkdpe 139
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTE-VRGYAANVTDEEDVEATFAQIAEDF---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWGLVNNAGI--------STFGEVEFT-SLETYKQVAEVNLWGT--------VRMTKSflplirRAKGRVVNISSmLG 202
Cdd:PRK08217  81 GQLNGLINNAGIlrdgllvkAKDGKVTSKmSLEQFQSVIDVNLTGVflcgreaaAKMIES------GSKGVIINISS-IA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927354 203 RMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI--AATSLYSPESIQAIAK 262
Cdd:PRK08217 154 RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPG-VIetEMTAAMKPEALERLEK 214
PRK06194 PRK06194
hypothetical protein; Provisional
 145-226 4.37e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 53.87  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPL-IRRAK------GRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLmLAAAEkdpayeGHIVNTASMAGLLAPPAMGIYNVSKH 166


                 ....*....
gi 767927354 218 GVEAFSDCL 226
Cdd:PRK06194 167 AVVSLTETL 175
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 60-255 4.52e-08

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: 53.62  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRtVQLNVcsseevekvveIVRSSL---K 136
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIA-LAADV-----------LDRASLeraR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAG--------ISTFGEVEFT------SLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNI 197
Cdd:cd08935   74 EEIVAQFGtvdiLINGAGgnhpdattDPEHYEPETEqnffdlDEEGWEFVFDLNLNGSFLPSQVFGkDMLEQKGGSIINI 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767927354 198 SSM-----LGRManPArspYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATS---LYSPE 255
Cdd:cd08935  154 SSMnafspLTKV--PA---YSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNrklLINPD 214
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 60-243 4.83e-08

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 53.23  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmkdKGHDGVKELDSLNSDRLRTVQLNVCSSEEVekvveivrSSLKDPE 139
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY---RSTESAEAVAAEAGERAIAIQADVRDRDQV--------QAMIEEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWG----LVNNAGI---------STFGEVEFtslETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMA 205
Cdd:cd05349   70 KNHFGpvdtIVNNALIdfpfdpdqrKTFDTIDW---EDYQQQLEGAVKGALNLLQAVLPdFKERGSGRVINIGTNLFQNP 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05349  147 VVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGG 184
PRK07062 PRK07062
SDR family oxidoreductase;
144-243 6.21e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 53.12  E-value: 6.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAG---ISTFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANP-------ARSpy 212
Cdd:PRK07062  90 MLVNNAGqgrVSTFAD---TTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPhmvatsaARA-- 164

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767927354 213 citkfGVEAFSDCLRYEMYPLGVKVS-----VVEPG 243
Cdd:PRK07062 165 -----GLLNLVKSLATELAPKGVRVNsillgLVESG 195
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 55-243 6.83e-08

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: 52.93  E-value: 6.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  55 EPVGSKAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGV-KELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRS 133
Cdd:cd08936    6 DPLANKVALVTASTDGIGLAIARRLAQDG----AHVVVSSRKQQNVdRAVATLQGEGL-SVTGTVCHVGKAEDRERLVAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 134 SLKDpEKGMWGLVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMANPARSP 211
Cdd:cd08936   81 AVNL-HGGVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMeKRGGGSVVIVSSVAAFHPFPGLGP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 212 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPG 191
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 144-243 6.94e-08

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: 52.58  E-value: 6.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd09761   78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVALT 157

                         90       100
                 ....*....|....*....|
gi 767927354 224 DCLRYEMYPlGVKVSVVEPG 243
Cdd:cd09761  158 HALAMSLGP-DIRVNCISPG 176
PRK06139 PRK06139
SDR family oxidoreductase;
146-232 7.12e-08

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 53.19  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 146 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPlIRRAKGR--VVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK06139  89 VNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALP-IFKKQGHgiFINMISLGGFAAQPYAAAYSASKFGLRGFS 167


                 ....*....
gi 767927354 224 DCLRYEMYP 232
Cdd:PRK06139 168 EALRGELAD 176
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-243 1.04e-07

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 52.38  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCD--SGFGFSLAKHLHSKGFLVFA----------GCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKV 127
Cdd:PRK12748   6 KIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmPWGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYAPNRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 128 VEIVRSSLKDPEKgmwgLVNNAGIST---FGEVEFTSL-ETYKqvaeVNLWGTVRMTKSFlplIR----RAKGRVVNISS 199
Cdd:PRK12748  86 FYAVSERLGDPSI----LINNAAYSThtrLEELTAEQLdKHYA----VNVRATMLLSSAF---AKqydgKAGGRIINLTS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767927354 200 --MLGRManPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12748 155 gqSLGPM--PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 145-304 1.14e-07

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: 52.09  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM-ANPARSPYCITKFGVEAF 222
Cdd:cd05368   74 LFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPGnfiaatSLYSPeSIQAIAKKmwEELPEVVRKDY------GKKYFDEKIAKMETYCSSGS 296
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPG------TVDTP-SLEERIQA--QPDPEEALKAFaarqplGRLATPEEVAALAVYLASDE 224

                        170
                 ....*....|..
gi 767927354 297 ----TDTSPVID 304
Cdd:cd05368  225 sayvTGTAVVID 236
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 60-243 1.23e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.00  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC-LMKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 138
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYgNRKEEAEETVYEIQS-NGGSAFSIGANLESLHGVEALYSSLDNELQNR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 --EKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRaKGRVVNISSMLGRMANPARSPYCITK 216
Cdd:PRK12747  84 tgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRISLPDFIAYSMTK 162

                        170       180
                 ....*....|....*....|....*..
gi 767927354 217 FGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPG 189
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 57-262 1.66e-07

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: 51.71  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  57 VGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLK 136
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERSDRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-----GRVVNISSMLGRMANPARS- 210
Cdd:cd08942   84 DV------LVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVVSGLENy 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF---IAATSLYSPESIQAIAK 262
Cdd:cd08942  158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFpskMTAFLLNDPAALEAEEK 212
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 58-242 1.95e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 51.79  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAvLVTGCDSGFGFSLAKHLHSKGF-LVFAGclmkdKGHDGVKEL-DSLNSDRLRTVQLNVCS--SEEVEKVVEIVRS 133
Cdd:PLN02780  53 GSWA-LVTGPTDGIGKGFAFQLARKGLnLVLVA-----RNPDKLKDVsDSIQSKYSKTQIKTVVVdfSGDIDEGVKRIKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 134 SLKDPEKGMwgLVNNAGIST-----FGEVEftsLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM--A 205
Cdd:PLN02780 127 TIEGLDVGV--LINNVGVSYpyarfFHEVD---EELLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIVipS 201

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:PLN02780 202 DPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVP 238
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 145-244 2.53e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 51.06  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANP-ARSPYCITKFGVE 220
Cdd:PRK06523  81 LVHVLGGSSAPAGGFAALtdEEWQDELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPeSTTAYAAAKAALS 160

                         90       100
                 ....*....|....*....|....
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPGN 244
Cdd:PRK06523 161 TYSKSLSKEVAPKGVRVNTVSPGW 184
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 63-264 2.74e-07

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: 51.14  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  63 LVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKeldslNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPEKGM 142
Cdd:cd05371    6 VVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-----LGDNCRFVPVDVTSEKDVKAAL----ALAKAKFGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 143 WGLVNNAGISTF-------GEVEFtSLETYKQVAEVNLWGTVRMTKSFLPLIRR-------AKGRVVNISSMLGRMANPA 208
Cdd:cd05371   77 DIVVNCAGIAVAaktynkkGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKnepdqggERGVIINTASVAAFEGQIG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYS--PESIQAIAKKM 264
Cdd:cd05371  156 QAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLF--DTPLLAglPEKVRDFLAKQ 211
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 145-243 2.82e-07

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 51.10  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGiSTFGEVEFTSLETYKQVAEVN--LWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANpaRSPYCITKFGVEA 221
Cdd:PRK12823  88 LINNVG-GTIWAKPFEEYEEEQIEAEIRrsLFPTLWCCRAVLPhMLAQGGGAIVNVSSIATRGIN--RVPYSAAKGGVNA 164

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12823 165 LTASLAFEYAEHGIRVNAVAPG 186
PRK09242 PRK09242
SDR family oxidoreductase;
132-242 3.77e-07

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 50.52  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 132 RSSLKDPEKGMWG----LVNNAGIS-TFGEVEFTSLEtYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMA 205
Cdd:PRK09242  75 RRAILDWVEDHWDglhiLVNNAGGNiRKAAIDYTEDE-WRGIFETNLFSAFELSRYAHPLLkQHASSAIVNIGSVSGLTH 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767927354 206 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:PRK09242 154 VRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190
PRK08251 PRK08251
SDR family oxidoreductase;
148-247 4.81e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 50.32  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 148 NAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANP-ARSPYCITKFGVEAFSDC 225
Cdd:PRK08251  88 NAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQgSGHLVLISSVSAVRGLPgVKAAYAASKAGVASLGEG 167

                         90       100
                 ....*....|....*....|..
gi 767927354 226 LRYEMYPLGVKVSVVEPGnFIA 247
Cdd:PRK08251 168 LRAELAKTPIKVSTIEPG-YIR 188
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 60-267 5.69e-07

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: 50.21  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-----LDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSS 134
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEG----AKLSLVDLNEEGLEAakaalLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 135 LKDPEkgmwGLVNNAGIStfGEVEFT---SLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARS 210
Cdd:cd05330   80 FGRID----GFFNNAGIE--GKQNLTedfGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767927354 211 PYCITKFGVEAFS--DCLRYEMYplGVKVSVVEPGnfiAATSLYSPESIQAIAKKMWEE 267
Cdd:cd05330  154 GYAAAKHGVVGLTrnSAVEYGQY--GIRINAIAPG---AILTPMVEGSLKQLGPENPEE 207
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 60-242 6.34e-07

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: 49.70  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSseevekvveivRSSLK--- 136
Cdd:cd05345    6 KVAIVTGAGSGFGEGIARRFAQEG----ARVVIADINADGAERVAADIGEAAIAIQADVTK-----------RADVEamv 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARS 210
Cdd:cd05345   71 EAALSKFGrldiLVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPhMEEQGGGVIINIASTAGLRPRPGLT 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 242
Cdd:cd05345  151 WYNASKGWVVTATKAMAVELAPRNIRVNCLCP 182
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 60-203 6.36e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 50.06  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGcLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVEIVRSslkdp 138
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGAtIVFND-INQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEK----- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWG-LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSM---LGR 203
Cdd:PRK07097  84 EVGVIDiLVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMmseLGR 153
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 60-206 6.58e-07

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 49.92  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDS-LNSDRLRTVQLNVCSseevekvveiVRS----- 133
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKeTGNAKVEVIQLDLSS----------LASvrqfa 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927354 134 -SLKDPEKGMWGLVNNAGI--STFGEVEfTSLEtyKQVAeVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMAN 206
Cdd:cd05327   72 eEFLARFPRLDILINNAGImaPPRRLTK-DGFE--LQFA-VNYLGHFLLTNLLLPVLKAsAPSRIVNVSSIAHRAGP 144
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 62-211 7.47e-07

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: 49.80  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCDSGFGFSLAKHLHSKGFLV--------FAGCLMKDKGhdGVKELdslnsdrlrTVQLnvcsseevekvveivrs 133
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVigidlreaDVIADLSTPE--GRAAA---------IADV----------------- 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927354 134 sLKDPEKGMWGLVNNAGISTFGEVEFtsletykqVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSP 211
Cdd:cd05328   54 -LARCSGVLDGLVNCAGVGGTTVAGL--------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGAGWAQDKLE 123
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
145-243 7.78e-07

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 49.64  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKG-RVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07067  84 LFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARhMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAVISY 163

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07067 164 TQSAALALIRHGINVNAIAPG 184
PRK06500 PRK06500
SDR family oxidoreductase;
148-269 7.86e-07

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 49.57  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 148 NAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVN--ISSMLGRmanPARSPYCITKFGVEAFSDC 225
Cdd:PRK06500  87 NAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNgsINAHIGM---PNSSVYAASKAALLSLAKT 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767927354 226 LRYEMYPLGVKVSVVEPGNfiAATSLY-----SPESIQAIAKKMWEELP 269
Cdd:PRK06500 164 LSGELLPRGIRVNAVSPGP--VQTPLYgklglPEATLDAVAAQIQALVP 210
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 145-255 9.41e-07

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: 49.27  E-value: 9.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:cd05359   80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGnFI---AATSLYSPE 255
Cdd:cd05359  160 RYLAVELGPRGIRVNAVSPG-VIdtdALAHFPNRE 193
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 145-243 1.04e-06

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 49.40  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTfgEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK12859 100 LVNNAAYST--NNDFSNLtaEELDKHYMVNVRATTLLSSQFARGFDKKSGgRIINMTSGQFQGPMVGELAYAATKGAIDA 177

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK12859 178 LTSSLAAEVAHLGITVNAINPG 199
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 145-251 1.30e-06

(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: 48.86  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI---STFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:cd05353   92 LVNNAGIlrdRSFAK---MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGQANYSAAKLGLL 168

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPgnfIAATSL 251
Cdd:cd05353  169 GLSNTLAIEGAKYNITCNTIAP---AAGSRM 196
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 144-243 1.43e-06

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 48.73  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAG-ISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:cd05340   87 GVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAVSKFATEG 166

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05340  167 L*QVLADEYQQRNLRVNCINPG 188
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
62-246 2.53e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.44  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  62 VLVTGCdSGF-GFSLAKHLHSKGFLVFAGclmkDKGHDGVKELDSLnsDRLRTVQLNVCSseevekvVEIVRSSLKDPEk 140
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGL----DRSPPGAANLAAL--PGVEFVRGDLRD-------PEALAAALAGVD- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 141 gmwGLVNNAGISTFGEveftslETYKQVAEVNLWGTVRMtksfLPLIRRAK-GRVVNISSM--LGRMANP--------AR 209
Cdd:COG0451   67 ---AVVHLAAPAGVGE------EDPDETLEVNVEGTLNL----LEAARAAGvKRFVYASSSsvYGDGEGPidedtplrPV 133

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767927354 210 SPYCITKFGVEAFsdcLRYEMYPLGVKVSVVEPGNFI 246
Cdd:COG0451  134 SPYGASKLAAELL---ARAYARRYGLPVTILRPGNVY 167
PRK06124 PRK06124
SDR family oxidoreductase;
145-250 2.60e-06

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 48.17  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI---STFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:PRK06124  92 LVNNVGArdrRPLAE---LDDAAIRALLETDLVAPILLSRLAAQRMKRqGYGRIIAITSIAGQVARAGDAVYPAAKQGLT 168

                         90       100       110
                 ....*....|....*....|....*....|
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPGNFiaATS 250
Cdd:PRK06124 169 GLMRALAAEFGPHGITSNAIAPGYF--ATE 196
PRK06114 PRK06114
SDR family oxidoreductase;
63-243 3.73e-06

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 47.47  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  63 LVTGCDSGFGFSLAKHLHSKGFLVfagCLMKDKGHDGVKE-LDSLNSDRLRTVQL--NVCSSEEVEKVVEIVRSSLkdpe 139
Cdd:PRK06114  12 FVTGAGSGIGQRIAIGLAQAGADV---ALFDLRTDDGLAEtAEHIEAAGRRAIQIaaDVTSKADLRAAVARTEAEL---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 kGMWGL-VNNAGISTFGEVEFTSLETYKQVAEVNLWGTvrmtksFLP-------LIRRAKGRVVNISSMLGRMANPA--R 209
Cdd:PRK06114  85 -GALTLaVNAAGIANANPAEEMEEEQWQTVMDINLTGV------FLScqaearaMLENGGGSIVNIASMSGIIVNRGllQ 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPG 191
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 165-294 3.79e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 47.64  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 165 YKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGn 244
Cdd:PRK07576 110 FKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG- 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767927354 245 FIAATSLY-----SPESIQAIAKKmweelpeVVRKDYGKKyfdEKIAKMETYCSS 294
Cdd:PRK07576 189 PIAGTEGMarlapSPELQAAVAQS-------VPLKRNGTK---QDIANAALFLAS 233
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 60-322 5.11e-06

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: 47.12  E-value: 5.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMK-DKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDP 138
Cdd:cd05343    7 RVALVTGASVGIGAAVARALVQHGMKV-VGCARRvDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMF----SAIRTQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 EKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK---GRVVNISSMLGRMANPARSP--YC 213
Cdd:cd05343   82 HQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGHRVPPVSVFhfYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 214 ITKFGVEAFSDCLRYEMYPL--GVKVSVVEPGnfiaatslyspesiqaiakkmweelpeVVRKDYGKKYFDEKIAKME-T 290
Cdd:cd05343  162 ATKHAVTALTEGLRQELREAktHIRATSISPG---------------------------LVETEFAFKLHDNDPEKAAaT 214

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767927354 291 YCSSGSTDTSPVIDAVTHALTaTTPYTRYHPM 322
Cdd:cd05343  215 YESIPCLKPEDVANAVLYVLS-TPPHVQIHDI 245
PRK07035 PRK07035
SDR family oxidoreductase;
145-243 5.29e-06

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 47.32  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07035  89 LVNNAAANPyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGVSPGDFQGIYSITKAAVISM 168

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07035 169 TKAFAKECAPFGIRVNALLPG 189
PRK06947 PRK06947
SDR family oxidoreductase;
59-243 6.41e-06

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 46.72  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 138
Cdd:PRK06947   2 RKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 139 ekGMWGLVNNAGI----STFGEVEFTSLetyKQVAEVNLWGTV--------RMTKSflplirR--AKGRVVNISSMLGRM 204
Cdd:PRK06947  80 --RLDALVNNAGIvapsMPLADMDAARL---RRMFDTNVLGAYlcareaarRLSTD------RggRGGAIVNVSSIASRL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767927354 205 ANPAR-SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06947 149 GSPNEyVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPG 188
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 60-251 6.46e-06

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


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 46.68  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLR---TVQLNVcsseevekvveivrSSLK 136
Cdd:cd05326    5 KVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVHcdvTVEADV--------------RAAV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 137 DPEKGMWG----LVNNAGIS--TFGEVEFTSLETYKQVAEVNLWGTVRMTK-SFLPLIRRAKGRVVNISSMLGRMANPAR 209
Cdd:cd05326   71 DTAVARFGrldiMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVGGLGP 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767927354 210 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSL 251
Cdd:cd05326  151 HAYTASKHAVLGLTRSAATELGEHGIRVNCVSPY--GVATPL 190
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 145-243 7.39e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 46.95  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAG----ISTFGEVEFTSLE-TYKqvaeVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFGV 219
Cdd:PRK06701 128 LVNNAAfqypQQSLEDITAEQLDkTFK----TNIYSYFHMTKAALPHLKQG-SAIINTGSITGYEGNETLIDYSATKGAI 202

                         90       100
                 ....*....|....*....|....
gi 767927354 220 EAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06701 203 HAFTRSLAQSLVQKGIRVNAVAPG 226
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 145-262 1.15e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 45.99  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGIStfGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVV-NISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK06113  92 LVNNAGGG--GPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAENKNINMTSYASSKAAASHL 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPGNFI--AATSLYSPESIQAIAK 262
Cdd:PRK06113 170 VRNMAFDLGEKNIRVNGIAPGAILtdALKSVITPEIEQKMLQ 211
PRK05717 PRK05717
SDR family oxidoreductase;
144-243 1.17e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 46.04  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAGISTFGEVEFTSLET--YKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK05717  87 ALVCNAAIADPHNTTLESLSLahWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLA 166

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPlGVKVSVVEPG 243
Cdd:PRK05717 167 LTHALAISLGP-EIRVNAVSPG 187
PRK06949 PRK06949
SDR family oxidoreductase;
60-278 1.38e-05

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 45.91  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKEL----DSLNSDRlRTVQLNVCSSEEVekvveivRSSL 135
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAG----AKVVLASRRVERLKELraeiEAEGGAA-HVVSLDVTDYQSI-------KAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 136 KDPEKGMWG---LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTV--------RMtksflplIRRAKG--------RVVN 196
Cdd:PRK06949  78 AHAETEAGTidiLVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFfvaqevakRM-------IARAKGagntkpggRIIN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 197 ISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaiAKKMWEELPevvRKDY 276
Cdd:PRK06949 151 IASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQ--GQKLVSMLP---RKRV 225


                 ..
gi 767927354 277 GK 278
Cdd:PRK06949 226 GK 227
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 145-279 1.38e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 45.80  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI--RRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK12384  85 LVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMirDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPGNFiaatsLYSPesiqaiakkMWEEL-----------PEVVRKDYGKK 279
Cdd:PRK12384 165 TQSLALDLAEYGITVHSLMLGNL-----LKSP---------MFQSLlpqyakklgikPDEVEQYYIDK 218
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 60-220 2.02e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 45.38  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKG--FLVFAGcLMKDKGHDGVKELDSLNSDrLRTVQLNVcsseevekvveivrSSLKD 137
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAERGaaGLVICG-RNAEKGEAQAAELEALGAK-AVFVQADL--------------SDVED 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEK----------GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNL-------WGTVRMtksflpLIRR-AKGRVVNISS 199
Cdd:PRK06198  71 CRRvvaaadeafgRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVrapfflmQEAIKL------MRRRkAEGTIVNIGS 144

                        170       180
                 ....*....|....*....|.
gi 767927354 200 MLGRMANPARSPYCITKFGVE 220
Cdd:PRK06198 145 MSAHGGQPFLAAYCASKGALA 165
PRK08628 PRK08628
SDR family oxidoreductase;
144-263 2.92e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.95  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 144 GLVNNAGISTFGEVEfTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK08628  86 GLVNNAGVNDGVGLE-AGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767927354 224 DCLRYEMYPLGVKVSVVEPGNfiAATSLYS--------PES-IQAIAKK 263
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAE--VMTPLYEnwiatfddPEAkLAAITAK 211
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 60-285 4.70e-05

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: 44.38  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR--AKGRVVNISSMLGRMANPARSPYCITKF 217
Cdd:cd05322   83 L----LVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRdgIQGRIIQINSKSGKVGSKHNSGYSAAKF 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPGNFiaatsLYSP--ES-IQAIAKKMWEELPEVvrkdygKKYFDEKI 285
Cdd:cd05322  159 GGVGLTQSLALDLAEHGITVNSLMLGNL-----LKSPmfQSlLPQYAKKLGIKESEV------EQYYIDKV 218
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 145-243 5.38e-05

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 44.33  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP--LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK08936  89 MINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKyfVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLM 168

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08936 169 TETLAMEYAPKGIRVNNIGPG 189
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 63-245 6.96e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 43.60  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  63 LVTGCDSGFGFSLAKHLHSKGFLVFAgclmkdKGHDGVKeLDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLK--DPEK 140
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLAQAGAEVIL------NGRDPAK-LAA-AAESLKGQGLSAHALAFDVTDHDAVRAAIDafEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 141 GMWG-LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 218
Cdd:PRK07523  86 GPIDiLVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGIAPYTATKGA 165

                        170       180
                 ....*....|....*....|....*..
gi 767927354 219 VEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK07523 166 VGNLTKGMATDWAKHGLQCNAIAPGYF 192
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
145-243 8.59e-05

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 43.57  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWG----TVRMTKSFlplIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 220
Cdd:PRK06935  95 LVNNAGTIRRAPLLEYKDEDWNAVMDINLNSvyhlSQAVAKVM---AKQGSGKIINIASMLSFQGGKFVPAYTASKHGVA 171

                         90       100
                 ....*....|....*....|...
gi 767927354 221 AFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06935 172 GLTKAFANELAAYNIQVNAIAPG 194
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 61-243 1.21e-04

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: 42.99  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   61 AVLVTGCDSGFGFSLAKHLHSKGFLVfagCL-MKDKGHDGVKELDSLNSDRLRTVQlnVCSSEEVEKVVEIVR-SSLKDP 138
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRV---VLhYHRSAAAASTLAAELNARRPNSAV--TCQADLSNSATLFSRcEAIIDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  139 EKGMWG----LVNNA----------GISTFGEVEFTSLETykQVAEvnLWGTVRMTKSFL--PLIRRAKGR--------- 193
Cdd:TIGR02685  78 CFRAFGrcdvLVNNAsafyptpllrGDAGEGVGDKKSLEV--QVAE--LFGSNAIAPYFLikAFAQRQAGTraeqrstnl 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767927354  194 -VVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:TIGR02685 154 sIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG 204
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 145-243 2.02e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 42.30  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAgiSTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 223
Cdd:PRK08265  84 LVNLA--CTYLDDGLaSSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLT 161

                         90       100
                 ....*....|....*....|
gi 767927354 224 DCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK08265 162 RSMAMDLAPDGIRVNSVSPG 181
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 60-243 2.38e-04

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: 42.22  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDkghdgvkeldsLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 139
Cdd:cd05363    4 KTALITGSARGIGRAFAQAYVREG----ARVAIAD-----------INLEAARATAAEIGPAACAISLDVTDQASIDRCV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGM---WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKG-RVVNISSMLGRMANPARS 210
Cdd:cd05363   69 AALvdrWGsidiLVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVArAMIAQGRGgKIINMASQAGRRGEALVG 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767927354 211 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:cd05363  149 VYCATKAAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK07074 PRK07074
SDR family oxidoreductase;
145-243 3.11e-04

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 41.68  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMA--NPArspYCITKFGVEA 221
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLeGMLKRSRGAVVNIGSVNGMAAlgHPA---YSAAKAGLIH 157

                         90       100
                 ....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK07074 158 YTKLLAVEYGRFGIRANAVAPG 179
PRK07023 PRK07023
SDR family oxidoreductase;
145-243 3.38e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.54  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07023  81 LINNAGTvEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGWSVYCATKAALDHH 160

                         90       100
                 ....*....|....*....|.
gi 767927354 223 SDCLRYEmYPLGVKVSVVEPG 243
Cdd:PRK07023 161 ARAVALD-ANRALRIVSLAPG 180
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 145-280 3.94e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 41.63  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGI---STFGEVEFTSLEtyKQVaEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFGVEA 221
Cdd:PRK06077  88 LVNNAGLglfSPFLNVDDKLID--KHI-STDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGLSIYGAMKAAVIN 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927354 222 FSDCLRYEMYPlGVKVSVVEPGnfiaatslyspesiqAIAKKMWEELPEVV---RKDYGKKY 280
Cdd:PRK06077 164 LTKYLALELAP-KIRVNAIAPG---------------FVKTKLGESLFKVLgmsEKEFAEKF 209
PRK06101 PRK06101
SDR family oxidoreductase;
59-243 5.72e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 41.01  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  59 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAgClmkDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVeivrSSLK-D 137
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIA-C---GRNQSVLDELHTQSAN-IFTLAFDVTDHPGTKAAL----SQLPfI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 138 PEkgMWglVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKgRVVNISSMLGRMANPARSPYCITKF 217
Cdd:PRK06101  72 PE--LW--IFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPRAEAYGASKA 146

                        170       180
                 ....*....|....*....|....*.
gi 767927354 218 GVEAFSDCLRYEMYPLGVKVSVVEPG 243
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPG 172
PRK07856 PRK07856
SDR family oxidoreductase;
145-262 8.37e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 40.30  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 145 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR--AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 222
Cdd:PRK07856  79 LVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNL 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767927354 223 SDCLRYEMYPlGVKVSVVEPGNFI--AATSLY-SPESIQAIAK 262
Cdd:PRK07856 159 TRSLAVEWAP-KVRVNAVVVGLVRteQSELHYgDAEGIAAVAA 200
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 60-257 1.84e-03

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: 39.26  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfaGCLmkDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:cd05348    5 EVALITGGGSGLGRALVERFVAEGAKV--AVL--DRSAEKVAELRADFGDAVVGVEGDV--------------RSLADNE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGM------WG----LVNNAGISTFgeveFTSL---------ETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSM 200
Cdd:cd05348   67 RAVarcverFGkldcFIGNAGIWDY----STSLvdipeekldEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSN 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767927354 201 LGRMANPARSPYCITKFGVEAFSDCLRYEMYPLgVKVSVVEPGNFiaATSLYSPESI 257
Cdd:cd05348  143 AGFYPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGM--VTDLRGPASL 196
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 63-270 2.37e-03

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 39.13  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354   63 LVTGCDSGFGFS----LAKHLHSKGFLVfagcLMKDKGHDGVKELDS-----LNSDRLRTVQLNVCSSEEVEKVVEIVRS 133
Cdd:TIGR01500   4 LVTGASRGFGRTiaqeLAKCLKSPGSVL----VLSARNDEALRQLKAeigaeRSGLRVVRVSLDLGAEAGLEQLLKALRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  134 SLKDPEKGMWGLVNNAGI---STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG---RVVNISSMLGRMANP 207
Cdd:TIGR01500  80 LPRPKGLQRLLLINNAGTlgdVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927354  208 ARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF-IAATSLYSPESIQAIAKKMWEELPE 270
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLdTDMQQQVREESVDPDMRKGLQELKA 223
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 60-245 2.74e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 38.97  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEVekvveivRSSLKDPE 139
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGI-KAHAAPFNVTHKQEV-------EAAIEHIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 KGMWG---LVNNAGI------STFGEVEFTSLETYKQVAEVNLWGTV--RMtksflplIRRAKGRVVNISSMLGRMANPA 208
Cdd:PRK08085  82 KDIGPidvLINNAGIqrrhpfTEFPEQEWNDVIAVNQTAVFLVSQAVarYM-------VKRQAGKIINICSMQSELGRDT 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767927354 209 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 245
Cdd:PRK08085 155 ITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYF 191
PRK05867 PRK05867
SDR family oxidoreductase;
146-305 3.59e-03

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 38.48  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 146 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKG-RVVNISSMLGRMAN-PAR-SPYCITKFGVEA 221
Cdd:PRK05867  91 VCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAkAMVKQGQGgVIINTASMSGHIINvPQQvSHYCASKAAVIH 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 222 FSDCLRYEMYPLGVKVSVVEPGnFIaATSLYSPesiQAIAKKMWEelPEVVRKDYGKKyfdEKIAKMETYCSSGS----T 297
Cdd:PRK05867 171 LTKAMAVELAPHKIRVNSVSPG-YI-LTELVEP---YTEYQPLWE--PKIPLGRLGRP---EELAGLYLYLASEAssymT 240


                 ....*...
gi 767927354 298 DTSPVIDA 305
Cdd:PRK05867 241 GSDIVIDG 248
PRK05854 PRK05854
SDR family oxidoreductase;
58-203 7.17e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 37.74  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  58 GSKAVlVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSD-RLRTVQLNVCSseevEKVVEIVRSSLK 136
Cdd:PRK05854  14 GKRAV-VTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDaKLSLRALDLSS----LASVAALGEQLR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927354 137 DPEKGMWGLVNNAGIST----------FgEVEFTSletykqvaevNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGR 203
Cdd:PRK05854  89 AEGRPIHLLINNAGVMTpperqttadgF-ELQFGT----------NHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 60-257 7.45e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 37.63  E-value: 7.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354  60 KAVLVTGCDSGFGFSLAKHLHSKGFLVfaGCLMKDKghDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPE 139
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEGARV--AVLERSA--EKLASLRQRFGDHVLVVEGDV--------------TSYADNQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927354 140 K----------GMWGLVNNAGISTFgeveFTSLE---------TYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSM 200
Cdd:PRK06200  69 RavdqtvdafgKLDCFVGNAGIWDY----NTSLVdipaetldtAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSN 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767927354 201 LGRMANPARSPYCITKFGVEAFSDCLRYEMYPlGVKVSVVEPGNfiAATSLYSPESI 257
Cdd:PRK06200 145 SSFYPGGGGPLYTASKHAVVGLVRQLAYELAP-KIRVNGVAPGG--TVTDLRGPASL 198
 
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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