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Conserved domains on  [gi|530375916|ref|XP_005269409|]
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D-beta-hydroxybutyrate dehydrogenase, mitochondrial isoform X2 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to corticosteroid 11-beta-dehydrogenase isozyme 2 that catalyzes the conversion of cortisol to the inactive metabolite cortisone; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 56-341 4.30e-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: 443.64  E-value: 4.30e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 135
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 294
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530375916 295 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 341
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; ...
 56-341 4.30e-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: 443.64  E-value: 4.30e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 135
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 294
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530375916 295 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 341
Cdd:cd09805  236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYI-PASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
56-262 1.55e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 155.80  E-value: 1.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG-ARVEVVALDVTDPDAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:COG0300   85 ----VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPG----NFIAAT------SLYSPEsiqAIAKKMWE 262
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGpvdtPFTARAgapagrPLLSPE---EVARAILR 215
PRK06182 PRK06182
short chain dehydrogenase; Validated
 54-316 1.86e-44

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 153.58  E-value: 1.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgvkeLDSLNSDRLRTVQLNVCSSeevekvveivrSSLK- 132
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDK-------MEDLASLGVHPLSLDVTDE-----------ASIKa 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 ------DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPAR 205
Cdd:PRK06182  64 avdtiiAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG------NFIAATSL--------YSPESiQAIAKKMweelpevvRKD 271
Cdd:PRK06182 144 AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGgiktewGDIAADHLlktsgngaYAEQA-QAVAASM--------RST 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 530375916 272 YGkkyfdekiakmetycSSGSTDTSPVIDAVTHALTATTPYTRYH 316
Cdd:PRK06182 215 YG---------------SGRLSDPSVIADAISKAVTARRPKTRYA 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 56-241 4.08e-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: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD-- 133
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA-LGGKALFIQGDVTD-----------RAQVKAlv 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  134 ---PEK--GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 207
Cdd:pfam00106  69 eqaVERlgRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 530375916  208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGV 182
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 58-272 3.37e-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: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPEKG 137
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDV--------------SDREDVKAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  138 M------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARS 206
Cdd:TIGR01830  67 VeeieeeLGtidiLVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLrIMIKQRSGRIINISSVVGLMGNAGQA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916  207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRKDY 272
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; ...
 56-341 4.30e-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: 443.64  E-value: 4.30e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDkgHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdPE 135
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKN--GPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGISTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd09805   77 KGLWGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTD 294
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530375916 295 TSPVIDAVTHALTATTPYTRYHPMDYYWWLRMqIMTHLPGAISDMIY 341
Cdd:cd09805  236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYI-PASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 56-322 3.30e-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: 3.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgVKELDSLNSDRLRTVQLNVCSSeevekvveivrSSLK--- 132
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDK----LESLGELLNDNLEVLELDVTDE-----------ESIKaav 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 ----DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP 207
Cdd:cd05374   66 keviERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIakkmweelpevvrkDYGKKYFDEKIAKMETY 287
Cdd:cd05374  146 YCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALED--------------PEISPYAPERKEIKENA 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 530375916 288 CSSGSTDTSP--VIDAVTHALTATTPYTRYHPMDYYW 322
Cdd:cd05374  212 AGVGSNPGDPekVADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
56-262 1.55e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 155.80  E-value: 1.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG-ARVEVVALDVTDPDAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:COG0300   85 ----VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPG----NFIAAT------SLYSPEsiqAIAKKMWE 262
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGpvdtPFTARAgapagrPLLSPE---EVARAILR 215
PRK06182 PRK06182
short chain dehydrogenase; Validated
 54-316 1.86e-44

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 153.58  E-value: 1.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgvkeLDSLNSDRLRTVQLNVCSSeevekvveivrSSLK- 132
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDK-------MEDLASLGVHPLSLDVTDE-----------ASIKa 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 ------DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPAR 205
Cdd:PRK06182  64 avdtiiAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG------NFIAATSL--------YSPESiQAIAKKMweelpevvRKD 271
Cdd:PRK06182 144 AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGgiktewGDIAADHLlktsgngaYAEQA-QAVAASM--------RST 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 530375916 272 YGkkyfdekiakmetycSSGSTDTSPVIDAVTHALTATTPYTRYH 316
Cdd:PRK06182 215 YG---------------SGRLSDPSVIADAISKAVTARRPKTRYA 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 56-241 4.08e-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: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD-- 133
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA-LGGKALFIQGDVTD-----------RAQVKAlv 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  134 ---PEK--GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 207
Cdd:pfam00106  69 eqaVERlgRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 530375916  208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGV 182
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 56-241 6.33e-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: 6.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslnsDRLRTVQLNVCSseevekvveivRSSLKD-- 133
Cdd:COG4221    6 KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELG----GRALAVPLDVTD-----------EAAVEAav 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 ---PEKgmWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPAR 205
Cdd:COG4221   71 aaaVAE--FGrldvLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGG 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:COG4221  149 AVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAV 184
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 58-239 1.96e-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: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKEldSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEkg 137
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAI--EALGGNAVAVQADVSDEEDVEALVEEALEEFGRLD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 mwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:cd05233   77 --ILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPhMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALE 154

                        170       180
                 ....*....|....*....|...
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05233  155 GLTRSLALELAPYGIRVNAVAPG 177
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 55-241 6.49e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 131.19  E-value: 6.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDkghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLkdp 134
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRV-VGTVRSE---AARADFEALHPDRALARLLDVTDFDAIDAVVADAEATF--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekgmwG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYC 209
Cdd:PRK06180  77 -----GpidvLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRaRRRGHIVNITSMGGLITMPGIGYYC 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK06180 152 GSKFALEGISESLAKEVAPFGIHVTAVEPGSF 183
PRK06914 PRK06914
SDR family oxidoreductase;
56-315 5.36e-35

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 128.99  E-value: 5.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLN-SDRLRTVQLNVCSSEEVekvveivrSSLKDP 134
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNlQQNIKVQQLDVTDQNSI--------HNFQLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGmWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 209
Cdd:PRK06914  76 LKE-IGridlLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYSpESIQAIAKKMWEELPevvrkdYgKKYFDekiaKMETYCS 289
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSY--NTNIWE-VGKQLAENQSETTSP------Y-KEYMK----KIQKHIN 220

                        250       260       270
                 ....*....|....*....|....*....|
gi 530375916 290 SGStDTSP----VIDAVTHALTATTPYTRY 315
Cdd:PRK06914 221 SGS-DTFGnpidVANLIVEIAESKRPKLRY 249
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 56-239 7.43e-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: 7.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPE 135
Cdd:cd05332    4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDM--------------SDLEDAE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 K----------GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 204
Cdd:cd05332   70 QvveealklfgGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVPF 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05332  150 RTAYAASKHALQGFFDSLRAELSEPNISVTVVCPG 184
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 56-315 2.43e-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: 124.11  E-value: 2.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHL---HSKGFLVFAgcLMKD--KGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVveivRSS 130
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYA--TMRDlkKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAA----VER 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 131 LKDPEKGMwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYC 209
Cdd:cd09806   75 VTERHVDV--LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPdMKRRGSGRILVTSSVGGLQGLPFNDVYC 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAatslyspesiqAIAKKMWEELPEV----VRKDYGKKYFDEKIAK-M 284
Cdd:cd09806  153 ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT-----------AFMEKVLGSPEEVldrtADDITTFHFFYQYLAHsK 221

                        250       260       270
                 ....*....|....*....|....*....|.
gi 530375916 285 ETYCSSGSTdTSPVIDAVTHALTATTPYTRY 315
Cdd:cd09806  222 QVFREAAQN-PEEVAEVFLTAIRAPKPPLRY 251
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 56-259 9.64e-32

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: 9.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNsDRLRTVQLNVcsseevekvveivrSSLKDPE 135
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAG-GRALAVAADV--------------TDEAAVE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 204
Cdd:COG1028   72 ALVaaavaaFGrldiLVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPhMRERGGGRIVNISSIAGLRGSPG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIA----ATSLYSPESIQAIAKK 259
Cdd:COG1028  152 QAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPG-PIDtpmtRALLGAEEVREALAAR 209
PRK08017 PRK08017
SDR family oxidoreductase;
56-239 2.80e-30

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 115.57  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCL-------MKDKGHDGVkELDSLNSDRLRTVQLNVcsseevekvveivr 128
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRkpddvarMNSLGFTGI-LLDLDDPESVERAADEV-------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 129 ssLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSP 207
Cdd:PRK08017  68 --IALTDNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGRGA 145

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08017 146 YAASKYALEAWSDALRMELRHSGIKVSLIEPG 177
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 55-268 4.08e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 110.38  E-value: 4.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC--LMKDKGHDGVK--ELDsLNSDRlrTVQLNVcsseevekvveivrSS 130
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSrnPARAAPIPGVEllELD-VTDDA--SVQAAV--------------DE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 131 LKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 209
Cdd:PRK06179  67 VIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG--------NFIAATS---LYSPE---SIQAIAKKMWE-ELPEVV 268
Cdd:PRK06179 147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAytktnfdaNAPEPDSplaEYDREravVSKAVAKAVKKaDAPEVV 220
PRK05693 PRK05693
SDR family oxidoreductase;
56-258 1.15e-26

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 106.41  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkdkghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 135
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATA-------RKAEDVEALAAAGFTAVQLDVNDGAALARLA----EELEAEH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGV 215
Cdd:PRK05693  71 GGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 216 EAFSDCLRYEMYPLGVKVSVVEPG----NF-----------IAATSLYSP--ESIQAIAK 258
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGaiasQFasnasreaeqlLAEQSPWWPlrEHIQARAR 210
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 56-241 1.99e-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: 105.03  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkghdgvkeLDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSS-LKDP 134
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVI---------------IVARSESKLEEAVEEIEAEANASGQKVSYISAdLSDY 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EK--------GMWG-----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRM 200
Cdd:cd08939   67 EEveqafaqaVEKGgppdlVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKeQRPGHIVFVSSQAALV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530375916 201 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:cd08939  147 GIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDT 187
PRK05993 PRK05993
SDR family oxidoreductase;
56-315 2.41e-25

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 102.80  E-value: 2.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDgvkeLDSLNSDRLRTVQLNVCSSEEVEKVVEivrSSLKDPE 135
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATC---RKEED----VAALEAEGLEAFQLDYAEPESIAALVA---QVLELSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:PRK05993  75 GRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRkQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNfIAatSLYSPESIQAIAKkmWEELPEVV-RKDYgkkyfDEKIAKMETYCSSGST 293
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHVSLIEPGP-IE--TRFRANALAAFKR--WIDIENSVhRAAY-----QQQMARLEGGGSKSRF 224

                        250       260
                 ....*....|....*....|....
gi 530375916 294 DTSP--VIDAVTHALTATTPYTRY 315
Cdd:PRK05993 225 KLGPeaVYAVLLHALTAPRPRPHY 248
PRK05650 PRK05650
SDR family oxidoreductase;
58-241 5.27e-25

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 102.04  E-value: 5.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVekvveivrSSLKDPEKG 137
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGF-YQRCDVRDYSQL--------TALAQACEE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 MWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK05650  74 KWGgidvIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAK 153

                        170       180
                 ....*....|....*....|....*....
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK05650 154 AGVVALSETLLVELADDEIGVHVVCPSFF 182
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 56-270 1.07e-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: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdpe 135
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEA-EGGKALVLELDVTDEQQVDAAVERTVEALG--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd08934   80 -RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYSPESiQAIAKKMWEELPEVVRK 270
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 ...
 56-279 3.65e-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: 3.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGF----SLAKHLHSKgflVFAGClmKDKGhdGVKELDSLNSDRLRTVQLNVcsseEVEKVVEIVRSSL 131
Cdd:cd05354    4 KTVLVTGANRGIGKafveSLLAHGAKK---VYAAV--RDPG--SAAHLVAKYGDKVVPLRLDV----TDPESIKAAAAQA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 132 KDPEKgmwgLVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYC 209
Cdd:cd05354   73 KDVDV----VINNAGVLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAMGTYS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF-----------IAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFD 278
Cdd:cd05354  149 ASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIdtrmaagaggpKESPETVAEAVLKALKAGEFHVFPDEMAKQVKEAYQS 228


                 .
gi 530375916 279 E 279
Cdd:cd05354  229 F 229
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 56-239 5.85e-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: 5.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 135
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAAL----ENLPEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGIS----TFGEVEFTSLETykqVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 210
Cdd:cd05346   77 RDIDILVNNAGLAlgldPAQEADLEDWET---MIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCA 153

                        170       180
                 ....*....|....*....|....*....
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
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 ...
 56-239 8.03e-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: 97.69  E-value: 8.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFL-VFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVveivRSSLKDP 134
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLRAEGLS-VRFHQLDVTDDASIEAA----ADFVEEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWGLVNNAGISTFG-EVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMAnparSPYCITK 212
Cdd:cd05324   76 YGGLDILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLT----SAYGVSK 151

                        170       180
                 ....*....|....*....|....*..
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05324  152 AALNALTRILAKELKETGIKVNACCPG 178
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
55-239 1.67e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 97.14  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmkdKGHDGVKELDSLN---SDRLRTVQLNVCSSEEVEKVVeivrSSL 131
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEEYgftEDQVRLKELDVTDTEECAEAL----AEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 132 KDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCI 210
Cdd:PRK12824  75 EEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSA 154

                        170       180
                 ....*....|....*....|....*....
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPG 183
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
55-242 3.41e-23

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 96.38  E-value: 3.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlNSDRLRTVQLNVCSseevekvveivRSSLKD- 133
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRA-AGGEARVLVFDVSD-----------EAAVRAl 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 -----PEKGMW-GLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARS 206
Cdd:PRK05653  73 ieaavEAFGALdILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPpMIKARYGRIVNISSVSGVTGNPGQT 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI 242
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; ...
 56-270 9.01e-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: 9.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVcsseevekvveivrSSLKDPE 135
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGN-AAALEADV--------------SDREAVE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 204
Cdd:cd05333   66 ALVekveaeFGpvdiLVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRaMIKRRSGRIINISSVVGLIGNPG 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRK 270
Cdd:cd05333  146 QANYAASKAGVIGFTKSLAKELASRGITVNAVAPG-FIDT--------------DMTDALPEKVKE 196
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 56-260 9.19e-23

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 95.26  E-value: 9.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdpe 135
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:PRK05557  83 -GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARpMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGnFIA--ATSLYSPESIQAIAKKM 260
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPG-FIEtdMTDALPEDVKEAILAQI 208
PRK09291 PRK09291
SDR family oxidoreductase;
55-241 2.20e-22

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 94.29  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC--------LMKDKGHDGVkeldslnsdRLRTVQLNVCSSEEVEkvvei 126
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVqiapqvtaLRAEAARRGL---------ALRVEKLDLTDAIDRA----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 127 vRSSLKDPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPAR 205
Cdd:PRK09291  68 -QAAEWDVDV----LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFT 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPY 178
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 56-239 6.39e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 93.47  E-value: 6.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslnsdRLRTVQLNVCSseevekvveivRSSLK--- 132
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-----LVVGGPLDVTD-----------PASFAafl 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSP 207
Cdd:PRK07825  70 DAVEADLGpidvLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAT 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07825 150 YCASKHAVVGFTDAARLELRGTGVHVSVVLPS 181
PRK12826 PRK12826
SDR family oxidoreductase;
55-240 8.62e-22

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 92.67  E-value: 8.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGhDGVKELDSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDP 134
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDA-AATAELVEAAGGKARARQVDVRDRAAL-------KAAVAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKgMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGR-MANPARSPY 208
Cdd:PRK12826  78 VE-DFGrldiLVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPrVGYPGLAHY 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 209 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN 240
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPGG 188
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 53-239 2.23e-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: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  53 VGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELdslnSDRLRTVQLNVCSSEEVEKVVEIVRSSLK 132
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL----GDAARFFHLDVTDEDGWTAVVDTAREAFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 dpekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYCIT 211
Cdd:cd05341   79 ----RLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNAS 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 212 KFGVEAFSDCLRYEMYP--LGVKVSVVEPG 239
Cdd:cd05341  155 KGAVRGLTKSAALECATqgYGIRVNSVHPG 184
PRK06482 PRK06482
SDR family oxidoreductase;
55-250 3.47e-21

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 91.33  E-value: 3.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkdKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATV----RRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK06482  78 DV----VVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRqGGGRIVQVSSEGGQIAYPGFSLYHATKW 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG----NFIAATSLYSP 250
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 ...
 58-274 5.26e-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: 5.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKG-FLVFAGClmKDKghDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDpeK 136
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATC--RDP--SAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGD--A 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 137 GMWGLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP---YCIT 211
Cdd:cd05325   75 GLDVLINNAGILHsYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGArAKIINISSRVGSIGDNTSGGwysYRAS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375916 212 KFGVEAFSDCLRYEMYPLGVKVSVVEPG--------NFIAATSLYSPESiqaIAKKMWEELPEVVRKDYGK 274
Cdd:cd05325  155 KAALNMLTKSLAVELKRDGITVVSLHPGwvrtdmggPFAKNKGPITPEE---SVAGLLKVIDNLNEEDSGK 222
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 54-242 5.79e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 90.36  E-value: 5.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAvLVTGCDSGFGFSLAKHLHSKGFLVfagclmkdkGHDG--VKELDSLNS---DRLRTVQLNVCSSEEVEKVVEIVR 128
Cdd:PRK12936   6 GRKA-LVTGASGGIGEEIARLLHAQGAIV---------GLHGtrVEKLEALAAelgERVKIFPANLSDRDEVKALGQKAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 129 SSLKdpekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARSP 207
Cdd:PRK12936  76 ADLE----GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQAN 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI 242
Cdd:PRK12936 152 YCASKAGMIGFSKSLAQEIATRNVTVNCVAPG-FI 185
PRK07832 PRK07832
SDR family oxidoreductase;
56-239 9.36e-21

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 90.10  E-value: 9.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclMKDKGHDG----VKELDSLNSdrlrTVQLNVCSSEEVEKVVEIVRSSL 131
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF----LTDRDADGlaqtVADARALGG----TVPEHRALDISDYDAVAAFAADI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 132 KDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGR-VVNISSMLGRMANPARSPYC 209
Cdd:PRK07832  73 HAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPWHAAYS 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07832 153 ASKFGLRGLSEVLRFDLARHGIGVSVVVPG 182
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 56-265 1.49e-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: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGhdGVKELDSLN-SDRLRTVQLNVCSSEEVekvveivrSSLKDP 134
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINpKVKATFVQCDVTSWEQL--------AAAFKK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWG----LVNNAGISTFGEVEFTSLETY--KQVAEVNLWGTVRMTKSFLPLIRRAK----GRVVNISSMLGRMANPA 204
Cdd:cd05323   71 AIEKFGrvdiLINNAGILDEKSYLFAGKLPPpwEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQ 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEM-YPLGVKVSVVEPGnfIAATSLYspESIQAIAKKMWEELP 265
Cdd:cd05323  151 FPVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPG--FTNTPLL--PDLVAKEAEMLPSAP 208
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-266 1.54e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 89.13  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKG-FLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVcsseevekvveivrSSLKDP 134
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEGaKVVIAYDINEEAAQELLEEIKEEGGDAI-AVKADV--------------SSEEDV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKgMWG-----------LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMAN 202
Cdd:PRK05565  71 EN-LVEqivekfgkidiLVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGA 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916 203 PARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfiaatslyspesiqAIAKKMWEELPE 266
Cdd:PRK05565 150 SCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPG---------------AIDTEMWSSFSE 198
PRK07326 PRK07326
SDR family oxidoreductase;
56-239 1.64e-20

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.91  E-value: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslNSDRLRTVQLNVcsseevekvveivrSSLKDPE 135
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN--NKGNVLGLAADV--------------RDEADVQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPAR 205
Cdd:PRK07326  71 RAVdaivaaFGgldvLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGG 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07326 151 AAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPG 184
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 56-265 2.27e-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: 88.28  E-value: 2.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgclmKDKGHDGVKELD-SLNSDRLRTVQLNVcsseeveKVVEIVRSSLKD- 133
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGL----YDIDEDGLAALAaELGAENVVAGALDV-------TDRAAWAAALADf 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 -PEKG--MWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYC 209
Cdd:cd08931   70 aAATGgrLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDLAVYS 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAATSLYSPESIQAIAKKMWEELP 265
Cdd:cd08931  150 ATKFAVRGLTEALDVEWARHGIRVADVWPW-FVDTPILTKGETGAAPKKGLGRVLP 204
PRK06181 PRK06181
SDR family oxidoreductase;
141-239 3.33e-20

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 88.50  E-value: 3.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI---STFGEVefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK06181  82 LVNNAGItmwSRFDEL--TDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHG 159

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06181 160 FFDSLRIELADDGVAVTVVCPG 181
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 58-272 3.37e-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: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPEKG 137
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDV--------------SDREDVKAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  138 M------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARS 206
Cdd:TIGR01830  67 VeeieeeLGtidiLVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLrIMIKQRSGRIINISSVVGLMGNAGQA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916  207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAAtslyspesiqaiakKMWEELPEVVRKDY 272
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 ...
 56-239 4.38e-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: 4.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAG--------CLMKDKGHDGVKELDSLNSDRLRTVQlnvcsseevekvveiv 127
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGlrnpedlaALSASGGDVEAVPYDARDPEDARALV---------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 128 rSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARS 206
Cdd:cd08932   65 -DALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGNA 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08932  144 GYSASKFALRALAHALRQEGWDHGVRVSAVCPG 176
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 56-239 4.99e-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: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfaGCLMKDKGhdgvkELDSLNSDRLRTVQLNVCSseevEKVVEIVRSSLKDPE 135
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRV--GICARDEA-----RLAAAAAQELEGVLGLAGD----VRDEADVRRAVDAME 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 K---GMWGLVNNAGISTFGEV-EFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCIT 211
Cdd:cd08929   70 EafgGLDALVNNAGVGVMKPVeELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNAS 149

                        170       180
                 ....*....|....*....|....*...
gi 530375916 212 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08929  150 KFGLLGLSEAAMLDLREANIRVVNVMPG 177
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 142-236 6.43e-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: 6.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 142 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 220
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                         90
                 ....*....|....*.
gi 530375916 221 CLRYEMYPLGVKVSVV 236
Cdd:cd05360  162 SLRAELAHDGAPISVT 177
PRK08219 PRK08219
SDR family oxidoreductase;
54-239 6.77e-20

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 86.91  E-value: 6.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkdkghdgvkeldsLNSDRLRTVQLNVCSSEEVEkvveivrSSLKD 133
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAPTHTLLLGG----------------RPAERLDELAAELPGATPFP-------VDLTD 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKGMWG---------LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPA 204
Cdd:PRK08219  59 PEAIAAAveqlgrldvLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPG 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMyPLGVKVSVVEPG 239
Cdd:PRK08219 139 WGSYAASKFALRALADALREEE-PGNVRVTSVHPG 172
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 55-260 7.92e-20

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 87.10  E-value: 7.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:PRK12937  83 --RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGPYAASKAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNfiAATSLY----SPESIQAIAKKM 260
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGP--VATELFfngkSAEQIDQLAGLA 207
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 55-250 2.07e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 86.63  E-value: 2.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKghdgVKELDSLNSDRLRTVQLNVCSseevekvVEIVRSSLKDP 134
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTAT----LADLAEKYGDRLLPLALDVTD-------RAAVFAAVETA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWGL---VNNAGISTFGEVE-FTSLETYKQVaEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYC 209
Cdd:PRK08263  72 VEHFGRLdivVNNAGYGLFGMIEeVTESEARAQI-DTNFFGALWVTQAVLPYLREqRSGHIIQISSIGGISAFPMSGIYH 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYSP 250
Cdd:PRK08263 151 ASKWALEGMSEALAQEVAEFGIKVTLVEPGGY--STDWAGT 189
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 142-235 2.59e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 87.28  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 142 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 220
Cdd:PRK07109  90 VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTD 169

                         90
                 ....*....|....*
gi 530375916 221 CLRYEMYPLGVKVSV 235
Cdd:PRK07109 170 SLRCELLHDGSPVSV 184
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 140-260 3.35e-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: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  140 GLVNNAGISTFGEVEF--TSLETYKQVAEVNLWGTVRMTKSFLPLIRRaKGRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:pfam13561  74 ILVNNAGFAPKLKGPFldTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530375916  218 FSDCLRYEMYPLGVKVSVVEPGnFI---AATSLYSPESIQAIAKKM 260
Cdd:pfam13561 153 LTRYLAVELGPRGIRVNAISPG-PIktlAASGIPGFDELLAAAEAR 197
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 47-235 4.29e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 86.18  E-value: 4.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  47 ASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVfagCLMkdkGHDGvKELDSL-----NSDRLRTVQLNVCSSEEVE 121
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKL---ALV---DLEE-AELAALaaelgGDDRVLTVVADVTDLAAMQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 122 KVVEIVRSSLKDPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMA 201
Cdd:PRK05872  74 AAAEEAVERFGGIDV----VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAA 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530375916 202 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSV 235
Cdd:PRK05872 150 APGMAAYCASKAGVEAFANALRLEVAHHGVTVGS 183
PRK09072 PRK09072
SDR family oxidoreductase;
55-238 4.95e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 85.38  E-value: 4.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKG-FLVFAGclmKDKGhdgvkELDSL-----NSDRLRTVQLNVCSSEEVEKVVEIVR 128
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGaRLLLVG---RNAE-----KLEALaarlpYPGRHRWVVADLTSEAGREAVLARAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 129 SslkdpEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSP 207
Cdd:PRK09072  77 E-----MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGYAS 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:PRK09072 152 YCASKFALRGFSEALRRELADTGVRVLYLAP 182
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 141-238 7.39e-19

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 84.36  E-value: 7.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                         90
                 ....*....|....*....
gi 530375916 220 DCLRYEMYPLGVKVSVVEP 238
Cdd:PRK07666 168 ESLMQEVRKHNIRVTALTP 186
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-240 9.02e-19

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 84.15  E-value: 9.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDGVKELDSL---NSDRLRTVQLNVCSseevekvVEIVRSSLK 132
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHY---RSDEEAAEELVEAveaLGRRAQAVQADVTD-------KAALEAAVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEK---GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPY 208
Cdd:PRK12825  77 AAVErfgRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNY 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 209 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN 240
Cdd:PRK12825 157 AAAKAGLVGLTKALARELAEYGITVNMVAPGD 188
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 55-239 1.53e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 83.48  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAH-AIAADLADPASVQRFFDAAAAALG-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK12939  84 --GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGrGRIVNLASDTALWGAPKLGAYVASKG 161

                        170       180
                 ....*....|....*....|....*.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG 239
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) ...
 54-239 2.17e-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: 83.04  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAVlVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivRSSLKD 133
Cdd:cd05356    1 GTWAV-VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERI---EKELEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKGMwgLVNNAGISTFGEVEF--TSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 210
Cdd:cd05356   77 LDIGI--LVNNVGISHSIPEYFleTPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTPLLATYSA 154

                        170       180
                 ....*....|....*....|....*....
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05356  155 SKAFLDFFSRALYEEYKSQGIDVQSLLPY 183
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 141-239 6.95e-18

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 81.52  E-value: 6.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd05339   80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                         90       100
                 ....*....|....*....|...
gi 530375916 220 DCLRYEM---YPLGVKVSVVEPG 239
Cdd:cd05339  160 ESLRLELkayGKPGIKTTLVCPY 182
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 56-240 1.02e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 81.00  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-LDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARG----ARVALIGRGAAPLSQtLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK12828  82 --RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGMGAYAAAKA 159

                        170       180
                 ....*....|....*....|....*..
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPGN 240
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSI 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 56-233 1.06e-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: 80.81  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlnsdrLRTVQLNVCSSEEVEKVVEIVRSslKDPE 135
Cdd:cd05370    6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-----IHTIVLDVGDAESVEALAEALLS--EYPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMwgLVNNAGISTfgEVEFTSLETYKQVAE----VNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLG---RMANPArsp 207
Cdd:cd05370   79 LDI--LINNAGIQR--PIDLRDPASDLDKADteidTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAfvpMAANPV--- 151

                        170       180
                 ....*....|....*....|....*.
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKV 233
Cdd:cd05370  152 YCATKAALHSYTLALRHQLKDTGVEV 177
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 56-249 1.47e-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: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAkhlhskgfLVFA--GCLMKDKGHdgvkeldslNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKD 133
Cdd:cd05364    4 KVAIITGSSSGIGAGTA--------ILFArlGARLALTGR---------DAERLEETRQSCLQAGVSEKKILLVVADLTE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEK---------GMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRM 200
Cdd:cd05364   67 EEGqdriisttlAKFGrldiLVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGR 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530375916 201 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYS 249
Cdd:cd05364  147 SFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPG--VIVTGFHR 193
PRK08267 PRK08267
SDR family oxidoreductase;
56-262 1.64e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 80.75  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkDKGHDGVKEL-DSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDP 134
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAY----DINEAGLAALaAELGAGNAWTGALDVTDRAAW-------DAALADF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYC 209
Cdd:PRK08267  71 AAATGGrldvLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAIYGQPGLAVYS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG-----------NFIAATSLYS------PESiqaIAKKMWE 262
Cdd:PRK08267 151 ATKFAVRGLTEALDLEWRRHGIRVADVMPLfvdtamldgtsNEVDAGSTKRlgvrltPED---VAEAVWA 217
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 56-258 6.45e-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: 6.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEkvveivrsSLKDPE 135
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVA--------RLFDAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCIT 211
Cdd:cd05362   76 EKAFGgvdiLVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTPNYGAYAGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530375916 212 KFGVEAFSDCLRYEMYPLGVKVSVVEPGNfiAATSLY----SPESIQAIAK 258
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, ...
 58-239 1.33e-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: 78.10  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPEKG 137
Cdd:cd05367    2 IILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLL----EAIRKLDGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 MWGLVNNAG-ISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI--RRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd05367   78 RDLLINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                        170       180
                 ....*....|....*....|....*
gi 530375916 215 VEAFSDCLRYEMYplGVKVSVVEPG 239
Cdd:cd05367  158 RDMFFRVLAAEEP--DVRVLSYAPG 180
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 140-266 1.60e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 78.08  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNA-GISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07890  85 ALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAA 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG-----------NFIAATSLYSPESI-QAIAKKM-WEELPE 266
Cdd:PRK07890 165 SQSLATELGPQGIRVNSVAPGyiwgdplkgyfRHQAGKYGVTVEQIyAETAANSdLKRLPT 225
PRK07454 PRK07454
SDR family oxidoreductase;
141-255 1.73e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 77.69  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRaRGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFT 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGNfiAATSLYSPESIQA 255
Cdd:PRK07454 167 KCLAEEERSHGIRVCTITLGA--VNTPLWDTETVQA 200
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 55-239 6.61e-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: 6.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFaGClmkdkGHDGVKELDSLnsDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:cd08945    3 SEVALVTGATSGIGLAIARRLGKEGLRVF-VC-----ARGEEGLATTV--KELREAGVEADGRTCDVRSVPEIEALVAAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 eKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP---LIRRAKGRVVNISSMLGRMANPARSP 207
Cdd:cd08945   75 -VARYGpidvLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAP 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08945  154 YSASKHGVVGFTKALGLELARTGITVNAVCPG 185
PRK08264 PRK08264
SDR family oxidoreductase;
141-239 9.88e-16

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 75.31  E-value: 9.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK08264  77 LVNNAGIfRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSL 156

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08264 157 TQALRAELAPQGTRVLGVHPG 177
PRK06484 PRK06484
short chain dehydrogenase; Validated
 55-239 4.28e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 76.04  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfagcLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRsslkdp 134
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRL----LIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQ------ 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWG----LVNNAGIS-TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYC 209
Cdd:PRK06484 339 --ARWGrldvLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYC 415

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06484 416 ASKAAVTMLSRSLACEWAPAGIRVNTVAPG 445
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 141-264 6.60e-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: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd08933   91 LVNNAGWHPPHQtTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAITAMT 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGNfiaatsLYSPesiqaiakkMWEEL 264
Cdd:cd08933  171 KALAVDESRYGVRVNCISPGN------IWTP---------LWEEL 200
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 58-233 7.11e-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: 73.27  E-value: 7.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGclmkdkGHDGVKeLDSLNSDR--LRTVQLNVCSSEEvekvveivRSSLKD-- 133
Cdd:COG3967    8 ILITGGTSGIGLALAKRLHARGNTVIIT------GRREEK-LEEAAAANpgLHTIVLDVADPAS--------IAALAEqv 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 ----PEKGMwgLVNNAGIS---TFGEVEFTsLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRManP-A 204
Cdd:COG3967   73 taefPDLNV--LINNAGIMraeDLLDEAED-LADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFV--PlA 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 205 RSP-YCITKFGVEAFSDCLRYEMYPLGVKV 233
Cdd:COG3967  148 VTPtYSATKAALHSYTQSLRHQLKDTSVKV 177
PRK05855 PRK05855
SDR family oxidoreductase;
141-239 1.02e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 75.02  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAK-GRVVNISSMLGRManPARS--PYCITKFGVE 216
Cdd:PRK05855 396 VVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRqMVERGTgGHIVNVASAAAYA--PSRSlpAYATSKAAVL 473

                         90       100
                 ....*....|....*....|...
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK05855 474 MLSECLRAELAAAGIGVTAICPG 496
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 56-241 1.66e-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: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIV--------INSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMwG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCI 210
Cdd:cd05347   78 EDF-GkidiLVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLLSELGGPPVPAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYF 187
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 52-275 2.06e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 72.01  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  52 PVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVfAGClmkdkghdGVKElDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSL 131
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGARV-HVC--------DVSE-AALAATAARLPGAKVTATVADVADPAQVERVF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 132 KDPEKGMWGL---VNNAGIS--TFGeVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR--RAKGRVVNISSMLGRMANPA 204
Cdd:PRK12829  78 DTAVERFGGLdvlVNNAGIAgpTGG-IDEITPEQWEQTLAVNLNGQFYFARAAVPLLKasGHGGVIIALSSVAGRLGYPG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNfiaatsLYSPES---IQAIAKKMWEELPEvVRKDYGKK 275
Cdd:PRK12829 157 RTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGI------VRGPRMrrvIEARAQQLGIGLDE-MEQEYLEK 223
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 141-288 3.57e-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: 69.85  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMkAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGNfiaatslyspesiqaIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYC 288
Cdd:cd02266  115 QQWASEGWGNGLPATAVACGT---------------WAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVA 168
PRK06484 PRK06484
short chain dehydrogenase; Validated
 55-239 3.44e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 70.26  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVfagcLMKDKGHDGVKEL-DSLNSDRlRTVQLNVcsseevekvveivrSSLKD 133
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQV----VVADRNVERARERaDSLGPDH-HALAMDV--------------SDEAQ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKGMWGL----------VNNAGIS--TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGR 199
Cdd:PRK06484  66 IREGFEQLhrefgridvlVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGL 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530375916 200 MANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06484 146 VALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPG 185
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 56-239 3.95e-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: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAG----ANIVLNGFGDA--AEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWG---LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCIT 211
Cdd:cd08940   77 RQFGGvdiLVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKkQGWGRIINIASVHGLVASANKSAYVAA 156

                        170       180
                 ....*....|....*....|....*...
gi 530375916 212 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08940  157 KHGVVGLTKVVALETAGTGVTCNAICPG 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 55-283 4.22e-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: 4.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKD 133
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFnIVLADLNLEEAAKSTIQEISEAGYNAV-AVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVN----LWGTVRMTKSFLPLIRraKGRVVNISSMLGRMANPARSPYC 209
Cdd:cd05366   81 FDV----MVNNAGIAPITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFKKLGH--GGKIINASSIAGVQGFPNLGAYS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSlyspesiqaiakkMWEELPEVVRK------DYGKKYFDEKIAK 283
Cdd:cd05366  155 ASKFAVRGLTQTAAQELAPKGITVNAYAPG--IVKTE-------------MWDYIDEEVGEiagkpeGEGFAEFSSSIPL 219
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 52-267 4.51e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 68.21  E-value: 4.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  52 PVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDgvkELDSLNSD------RLRTVQLNVcsseeveKVVE 125
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRA---EADAVAAGieaaggKALGLAFDV-------RDFA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 126 IVRSSLKDPEK---GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIR-RAKGRVVNISSMLGRM 200
Cdd:PRK12827  73 ATRAALDAGVEefgRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRaRRGGRIVNIASVAGVR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 201 ANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG---NFIAATSLYSPESIQAIAKKMWEELPEV 267
Cdd:PRK12827 153 GNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGainTPMADNAAPTEHLLNPVPVQRLGEPDEV 222
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
55-274 5.82e-13

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 67.83  E-value: 5.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAI-AVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVN----LWGTVRMTKSFLPLirRAKGRVVNISSMLGRMANPARSPYCI 210
Cdd:PRK08643  81 NV----VVNNAGVAPTTPIETITEEQFDKVYNINvggvIWGIQAAQEAFKKL--GHGGKIINATSQAGVVGNPELAVYSS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSlyspesiqaiakkMWEELPEVVRKDYGK 274
Cdd:PRK08643 155 TKFAVRGLTQTAARDLASEGITVNAYAPG--IVKTP-------------MMFDIAHQVGENAGK 203
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 56-269 6.24e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 67.43  E-value: 6.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDkghdgVKELDSLNSDR-LRTVQLNVcsSEEVEKVVEIVRSSLKDp 134
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVA--AARN-----AAALDRLAGETgCEPLRLDV--GDDAAIRAALAAAGAFD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA--KGRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK07060  80 -----GLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLPDHLAYCASK 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG---NFIAATSLYSPES----IQAIAKKMWEELPEVVR 269
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTvtlTPMAAEAWSDPQKsgpmLAAIPLGRFAEVDDVAA 218
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 52-238 1.07e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 66.99  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  52 PVGSKAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLRTVQLNV--CSSEEVEKVVEIVRS 129
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKG----ARVALLDRSEDVAEVAAQLLGGNAKGLVCDVsdSQSVEAAVAAVISAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 130 SLKDPekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPY 208
Cdd:PRK06841  88 GRIDI------LVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHVAY 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 209 CITKFGVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:PRK06841 162 CASKAGVVGMTKVLALEWGPYGITVNAISP 191
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 58-239 1.12e-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: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAgclmKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 137
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIA----TGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 mwgLVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGV 215
Cdd:PRK10538  78 ---LVNNAGLALGLEpAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154

                        170       180
                 ....*....|....*....|....
gi 530375916 216 EAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK10538 155 RQFSLNLRTDLHGTAVRVTDIEPG 178
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 56-239 1.36e-12

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 66.83  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVI--------GFD--QAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmlgrmaNPARSP------Y 208
Cdd:PRK08220  79 V----LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGS------NAAHVPrigmaaY 148

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530375916 209 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08220 149 GASKAALTSLAKCVGLELAPYGVRCNVVSPG 179
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
60-239 1.88e-12

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 66.19  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  60 VTGCDSGFGFSLAKHLHSKGFLVFAGClmkdkGHDGVKELDSLnsDRLRTVQLNVCSSEEVEKVVEIVRSSLkDPEKGMW 139
Cdd:PRK12938   8 VTGGMGGIGTSICQRLHKDGFKVVAGC-----GPNSPRRVKWL--EDQKALGFDFIASEGNVGDWDSTKAAF-DKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 G----LVNNAGISTfgEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK12938  80 GeidvLVNNAGITR--DVVFRKMtrEDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGQTNYSTAK 157

                        170       180
                 ....*....|....*....|....*..
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPG 184
FabG-like PRK07231
SDR family oxidoreductase;
56-239 2.17e-12

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 66.01  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSlnSDRLRTVQLNVCSSEEvekvveivRSSLKDPE 135
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--GGRAIAVAADVSDEAD--------VEAAVAAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWG----LVNNAGIS-TFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 209
Cdd:PRK07231  76 LERFGsvdiLVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07231 156 ASKGAVITLTKALAAELGPDKIRVNAVAPV 185
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 58-243 2.92e-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: 65.43  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 137
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNP-SVEVEILDVTDEERNQLVIAELEAELGGLDL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 mwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:cd05350   79 ---VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGrGHLVLISSVAALRGLPGAAAYSASKAALS 155

                        170       180
                 ....*....|....*....|....*..
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPGnFIA 243
Cdd:cd05350  156 SLAESLRYDVKKRGIRVTVINPG-FID 181
PRK06138 PRK06138
SDR family oxidoreductase;
56-239 3.35e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 65.56  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKG-FLVFAgclmkDKGHDG-VKELDSLNSD-RLRTVQLNVCSSEEVekvveivrSSLK 132
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGaRVVVA-----DRDAEAaERVAAAIAAGgRAFARQGDVGSAEAV--------EALV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSP 207
Cdd:PRK06138  73 DFVAARWGrldvLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAA 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06138 153 YVASKGAIASLTRAMALDHATDGIRVNAVAPG 184
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 59-260 6.00e-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: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  59 LVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSseevekvvEIVRSSLKDPEKGM 138
Cdd:cd05337    5 IVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGE--------LSDHEALLDQAWED 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 139 WG----LVNNAGISTFGEVEFTSL--ETYKQVAEVNLWGTVRMTKSF-LPLIRRAK------GRVVNISSMLGRMANPAR 205
Cdd:cd05337   77 FGrldcLVNNAGIAVRPRGDLLDLteDSFDRLIAINLRGPFFLTQAVaRRMVEQPDrfdgphRSIIFVTSINAYLVSPNR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAA--TSLYSPESIQAIAKKM 260
Cdd:cd05337  157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPG-LIHTdmTAPVKEKYDELIAAGL 212
PRK07775 PRK07775
SDR family oxidoreductase;
58-239 6.87e-12

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 64.78  E-value: 6.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRSSLKDPEKg 137
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAV-AFPLDVTDPDSVKSFVAQAEEALGEIEV- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 138 mwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:PRK07775  91 ---LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167

                        170       180
                 ....*....|....*....|...
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07775 168 AMVTNLQMELEGTGVRASIVHPG 190
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-250 8.71e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 64.21  E-value: 8.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEvekvveivRSSLKDP 134
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFdLAINDRPDDEELAATQQELRALGV-EVIFFPADVADLSA--------HEAMLDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWG----LVNNAGISTF--GEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGR------VVNISSMLGRMA 201
Cdd:PRK12745  74 AQAAWGridcLVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKrMLAQPEPEelphrsIVFVSSVNAIMV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530375916 202 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSLYSP 250
Cdd:PRK12745 154 SPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPG--LIKTDMTAP 200
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 56-292 1.04e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 64.26  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC-LMKDKGHDGVKELDSlNSDRLRTVQLNVcsseevekVVEIVRSSLKDP 134
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINYnSSKEAAENLVNELGK-EGHDVYAVQADV--------SKVEDANRLVEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYC 209
Cdd:PRK12935  78 AVNHFGkvdiLVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTNYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAiakKMWEELPevvRKDYGKKyfdEKIAKMETY-C 288
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQ---KIVAKIP---KKRFGQA---DEIAKGVVYlC 228


                 ....
gi 530375916 289 SSGS 292
Cdd:PRK12935 229 RDGA 232
PRK07201 PRK07201
SDR family oxidoreductase;
50-221 1.28e-11

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 65.74  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  50 AEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdrlrTVQLNVCSseevekvveivrs 129
Cdd:PRK07201 366 RGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG----TAHAYTCD------------- 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 130 sLKDPE------KGMWG-------LVNNAGISTFGEVE--FTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNI 193
Cdd:PRK07201 429 -LTDSAavdhtvKDILAehghvdyLVNNAGRSIRRSVEnsTDRFHDYERTMAVNYFGAVRLILGLLPHMReRRFGHVVNV 507

                        170       180
                 ....*....|....*....|....*....
gi 530375916 194 SSmLGRMANPAR-SPYCITKFGVEAFSDC 221
Cdd:PRK07201 508 SS-IGVQTNAPRfSAYVASKAALDAFSDV 535
PRK08589 PRK08589
SDR family oxidoreductase;
55-239 1.33e-11

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 64.03  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDP 134
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAYVLAVDI-AEAVSETVDKIKS-NGGKAKAYHVDISDEQQVKDFA----SEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWGLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK08589  80 FGRVDVLFNNAGVDNaAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKG 159

                        170       180
                 ....*....|....*....|....*.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08589 160 AVINFTKSIAIEYGRDGIRANAIAPG 185
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 55-239 1.56e-11

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 63.65  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFagcLMKDKGHDGVKELDSLNSDrlrTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVA---VLYNSAENEAKELREKGVF---TIKCDVGNRDQVKKSKEVVEKEFGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGrMANPARSP--YCIT 211
Cdd:PRK06463  81 DV----LVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAG-IGTAAEGTtfYAIT 155

                        170       180
                 ....*....|....*....|....*...
gi 530375916 212 KFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPG 183
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-239 1.56e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 63.44  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagclmkdkGHDgvKELDSLNSDRLRTVQLNVCSSEEVEKvveivrSSLKDPE 135
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFLAQGAQVY--------GVD--KQDKPDLSGNFHFLQLDLSDDLEPLF------DWVPSVD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KgmwgLVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK06550  70 I----LCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVAGGGGAAYTASKH 145

                        170       180
                 ....*....|....*....|....*.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06550 146 ALAGFTKQLALDYAKDGIQVFGIAPG 171
PRK07577 PRK07577
SDR family oxidoreductase;
55-239 2.81e-11

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 62.44  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDKGHDGVKELDSLN-SDRLRTvqlnvcsseevekvveivRSSLKD 133
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDFPGELFACDlADIEQT------------------AATLAQ 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 --PEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmLGRMANPARSPYCI 210
Cdd:PRK07577  63 inEIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEgMKLREQGRIVNICS-RAIFGALDRTSYSA 141

                        170       180
                 ....*....|....*....|....*....
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07577 142 AKSALVGCTRTWALELAEYGITVNAVAPG 170
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 56-270 5.59e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 62.22  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-LDSLNSDRLRTVQL--NVCSSEEVEKVVEIVRSSLK 132
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAG----AAVAIADLNQDGANAvADEINKAGGKAIGVamDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCI 210
Cdd:PRK13394  84 SVDI----LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYVT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIaATSLYSPEsIQAIAKKMWEELPEVVRK 270
Cdd:PRK13394 160 AKHGLLGLARVLAKEGAKHNVRSHVVCPG-FV-RTPLVDKQ-IPEQAKELGISEEEVVKK 216
PRK07831 PRK07831
SDR family oxidoreductase;
141-238 6.09e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 61.97  E-value: 6.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07831 101 LVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhgGVIVNNASVLGWRAQHGQAHYAAAKAGVMAL 180

                         90       100
                 ....*....|....*....|
gi 530375916 219 SDCLRYEMYPLGVKVSVVEP 238
Cdd:PRK07831 181 TRCSALEAAEYGVRINAVAP 200
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 56-265 8.30e-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: 61.58  E-value: 8.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05352    9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSF-LPLIRRAKGRVVNISSMLGRMAN-PA-RSPYCITK 212
Cdd:cd05352   89 ----ILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAaKIFKKQGKGSLIITASMSGTIVNrPQpQAAYNASK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaiaKKMWEELP 265
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 ...
 58-239 9.25e-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: 9.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLVFA-----GCLMKDKGHDGVKELDSLNSDRLRTVQlnvcsseevekvveivrSSLK 132
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIAldlpfVLLLEYGDPLRLTPLDVADAAAVREVC-----------------SRLL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSmlgrmaNPARSP---- 207
Cdd:cd05331   64 AEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRRTGAIVTVAS------NAAHVPrism 137

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530375916 208 --YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05331  138 aaYGASKAALASLSKCLGLELAPYGVRCNVVSPG 171
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 140-239 1.04e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.04  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK08945  95 GVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQGRANWGAYAVSKFATEG 174

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08945 175 MMQVLADEYQGTNLRVNCINPG 196
PRK12746 PRK12746
SDR family oxidoreductase;
56-239 1.51e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 60.82  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLV-FAGCLMKDKGHDGVKELDSlNSDR--LRTVQLNVCSSEEVEKVVEIVRSSLK 132
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIES-NGGKafLIEADLNSIDGVKKLVEQLKNELQIR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIrRAKGRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK12746  86 VGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL-RAEGRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180
                 ....*....|....*....|....*..
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12746 165 GALNTMTLPLAKHLGERGITVNTIMPG 191
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 56-239 1.64e-10

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: 60.75  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARV-AICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kgmwGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:cd05344   81 ----ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPgMKERGWGRIVNISSLTVKEPEPNLVLSNVARAG 156

                        170       180
                 ....*....|....*....|....*
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPG 181
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 55-243 2.14e-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: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EkgmwGLVNNAGISTFGEVE-FT--SLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMA-------NP 203
Cdd:cd08930   82 D----ILINNAYPSPKVWGSrFEefPYEQWNEVLNVNLGGAFLCSQAFIKLFkKQGKGSIINIASIYGVIApdfriyeNT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530375916 204 AR-SP--YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIA 243
Cdd:cd08930  158 QMySPveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILN 200
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 141-268 2.73e-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: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd05338   96 LVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSLRPARGDVAYAAGKAGMSRLT 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGNFI--AATSLYSPESIQAIAKKmweelPEVV 268
Cdd:cd05338  176 LGLAAELRRHGIAVNSLWPSTAIetPAATELSGGSDPARARS-----PEIL 221
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
56-239 3.34e-10

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 59.81  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLR--TVQLNVCSSEEVekvveivRSSLKD 133
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHG----ANLILLDISPEIEKLADELCGRGHRctAVVADVRDPASV-------AAAIKR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKgMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM-ANPARSP 207
Cdd:PRK08226  76 AKE-KEGridiLVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMvADPGETA 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08226 155 YALTKAAIVGLTKSLAVEYAQSGIRVNAICPG 186
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 141-239 4.28e-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: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:cd08944   81 LVNNAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08944  161 TRTLAAELRHAGIRCNALAPG 181
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 56-239 7.62e-10

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 58.74  E-value: 7.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGcLMKDKGHDGVKELDSLNSDRLrTVQLNVcsseevekvveivrSSLKDP 134
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAkVVIAD-LNDEAAAAAAEALQKAGGKAI-GVAMDV--------------TDEEAI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGM------WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANP 203
Cdd:PRK12429  69 NAGIdyavetFGgvdiLVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSA 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530375916 204 ARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12429 149 GKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPG 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
 141-238 8.16e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.57  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKAAVASLT 162

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530375916 220 -----DCLRYEM-------YPLGVKVSVVEP 238
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; ...
 141-239 9.11e-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: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGE-VEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANpaRSPYCITKFGVEAF 218
Cdd:cd08937   84 LINNVGGTIWAKpYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATRGIY--RIPYSAAKGGVNAL 161

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
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 ...
 141-250 1.02e-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: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd05329   88 LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAsGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLT 167

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGnfIAATSLYSP 250
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 ...
 141-259 1.15e-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: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTV--------RMTKSflplirRAKGRVVNISSMLGRMANPARSPYCITK 212
Cdd:cd05358   85 LVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFlcareaikRFRKS------KIKGKIINMSSVHEKIPWPGHVNYAASK 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPGNF---IAATSLYSPESIQAIAKK 259
Cdd:cd05358  159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAIntpINAEAWDDPEQRADLLSL 208
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
56-260 1.45e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 59.09  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDslNSDRLRTVQLNVCSseevekvveivRSSLKDP- 134
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELG--GPDRALGVACDVTD-----------EAAVQAAf 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKG--MWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARS 206
Cdd:PRK08324 490 EEAalAFGgvdiVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIASKNAVNPGPNFG 569

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKM 260
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 ...
 56-265 2.02e-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: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfagCLM---KDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrsslK 132
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFAELGASV---AIAgrkPEVLEAAAEEISSATGGRAHPIQCDV-----------------R 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPE------KGMW-------GLVNNAG---ISTFGEVeftSLETYKQVAEVNLWGTVRMTKSFLP-LIRR-AKGRVVNIS 194
Cdd:cd05369   64 DPEaveaavDETLkefgkidILINNAAgnfLAPAESL---SPNGFKTVIDIDLNGTFNTTKAVGKrLIEAkHGGSILNIS 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375916 195 SMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKMWEELP 265
Cdd:cd05369  141 ATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVP 211
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 56-263 2.25e-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: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMKDKGHDGVKElDSLNSDRLRTVQLNVCSSEEVekvveivRSSLKDPE 135
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAV-VVADIDPEIAEKVAE-AAQGGPRALGVQCDVTSEAQV-------QSAFEQAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGL---VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK--GRVVNISSMLGRMANPARSPYCI 210
Cdd:cd08943   73 LEFGGLdivVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 211 TKFGVEAFSDCLRYEMYPLGVKVSVVEPgNFIAATSLYSPESIQ---AIAKKMWEE 263
Cdd:cd08943  153 AKAAEAHLARCLALEGGEDGIRVNTVNP-DAVFRGSKIWEGVWRaarAKAYGLLEE 207
PRK06398 PRK06398
aldose dehydrogenase; Validated
 56-285 2.82e-09

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 57.15  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmKDKGHDGVK--ELDSLNSDRLRTVQLNVCSSEEvekvveivRSSLkd 133
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI-KEPSYNDVDyfKVDVSNKEQVIKGIDYVISKYG--------RIDI-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 pekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK06398  76 -------LVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRNAAAYVTSK 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530375916 213 FGVEAFSDCLRYEMYPLgVKVSVVEPGnfiaatSLYSPESIQAIAKKMWEELPEVVRK--DYGKKYFDEKIAKME 285
Cdd:PRK06398 149 HAVLGLTRSIAVDYAPT-IRCVAVCPG------SIRTPLLEWAAELEVGKDPEHVERKirEWGEMHPMKRVGKPE 216
PRK07774 PRK07774
SDR family oxidoreductase;
55-239 3.32e-09

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 56.68  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELdSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQI-VADGGTAIAVQVDVSDPDSAKAMADATVSAFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGIstFGEVEFTSLET-----YKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMlgrMANPARSPY 208
Cdd:PRK07774  83 --GIDYLVNNAAI--YGGMKLDLLITvpwdyYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSST---AAWLYSNFY 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530375916 209 CITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPG 186
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 143-249 3.60e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 56.89  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 143 NNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP--LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSD 220
Cdd:PRK05876  89 SNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAE 168

                         90       100
                 ....*....|....*....|....*....
gi 530375916 221 CLRYEMYPLGVKVSVVEPgnFIAATSLYS 249
Cdd:PRK05876 169 TLAREVTADGIGVSVLCP--MVVETNLVA 195
PRK07063 PRK07063
SDR family oxidoreductase;
56-239 6.05e-09

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 56.21  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKEL-DSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIaRDVAGARVLAVPADVTDAASVAAAVAAAEEAFG-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK07063  86 --PLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180
                 ....*....|....*....|....*.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPG 189
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 56-257 7.70e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 55.79  E-value: 7.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDgvkeldslnsDRLRTVQLNVCSSEEVEKVVeivrSSLKDPE 135
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH----------ENYQFVPTDVSSAEEVNHTV----AEIIEKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGIS----------TFGEVEFTSlETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPA 204
Cdd:PRK06171  76 GRIDGLVNNAGINiprllvdekdPAGKYELNE-AAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFIAATSLYSPESIQAIA 257
Cdd:PRK06171 155 QSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPG-ILEATGLRTPEYEEALA 206
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 56-238 1.16e-08

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: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAgcLMKDKghdgvKELDSLNSD--RLRTVQLNVcsseevekvveivrSSLKD 133
Cdd:cd05351    8 KRALVTGAGKGIGRATVKALAKAGARVVA--VSRTQ-----ADLDSLVREcpGIEPVCVDL--------------SDWDA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEKGMW------GLVNNAGIST---FGEVeftSLETYKQVAEVNLWGTVRMTKSFLP-LI-RRAKGRVVNISSMLGRMAN 202
Cdd:cd05351   67 TEEALGsvgpvdLLVNNAAVAIlqpFLEV---TKEAFDRSFDVNVRAVIHVSQIVARgMIaRGVPGSIVNVSSQASQRAL 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530375916 203 PARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:cd05351  144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNP 179
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
56-283 1.22e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 55.07  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFagCLMKDKGhdgvKELDSL---NSDRLRTVQLNVCSSEEVEKVVEIVRSSLK 132
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVI--SISRTEN----KELTKLaeqYNSNLTFHSLDLQDVHELETNFNEILSSIQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWGLVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG--RVVNISSMLGRMANPARSPYC 209
Cdd:PRK06924  76 EDNVSSIHLINNAGMVApIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGWSAYC 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530375916 210 ITKFGVEAFSDCLRYEM----YPlgVKVSVVEPGnfIAATSLysPESIQAIAKKMWEELPEVVR-KDYGKKYFDEKIAK 283
Cdd:PRK06924 156 SSKAGLDMFTQTVATEQeeeeYP--VKIVAFSPG--VMDTNM--QAQIRSSSKEDFTNLDRFITlKEEGKLLSPEYVAK 228
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 141-241 1.23e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 54.95  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSF--LPLIRRAKGRVVNISSMLGRMANPARSP----YCITKFG 214
Cdd:PRK08213  93 LVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVakRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNTSKGA 172

                         90       100
                 ....*....|....*....|....*..
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK08213 173 VINFTRALAAEWGPHGIRVNAIAPGFF 199
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 56-269 1.54e-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: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGClmkDKGHDGVKEL-DSLNSDRLR--TVQLNVCSSEEVEKvveivrssLK 132
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHY---NRSEAEAQRLkDELNALRNSavLVQADLSDFAACAD--------LV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIR-RAKGRVVNIS-SMLGRmANPARS 206
Cdd:cd05357   70 AAAFRAFGrcdvLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAgSRNGSIINIIdAMTDR-PLTGYF 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLgVKVSVVEPGNFIAATSLYSPESIQAIAK---KMWEELPEVVR 269
Cdd:cd05357  149 AYCMSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEDMDAEYRENALRKvplKRRPSAEEIAD 213
PRK12743 PRK12743
SDR family oxidoreductase;
141-239 2.33e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 54.27  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGtvrmtkSFLPLIRRAK--------GRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK12743  84 LVNNAGAMTKAPFLDMDFDEWRKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEHTPLPGASAYTAAK 157

                         90       100
                 ....*....|....*....|....*..
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12743 158 HALGGLTKAMALELVEHGILVNAVAPG 184
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-258 2.37e-08

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 54.20  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVEIVRSSLkdpe 135
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTE-VRGYAANVTDEEDVEATFAQIAEDF---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWGLVNNAGI--------STFGEVEFT-SLETYKQVAEVNLWGT--------VRMTKSflplirRAKGRVVNISSmLG 198
Cdd:PRK08217  81 GQLNGLINNAGIlrdgllvkAKDGKVTSKmSLEQFQSVIDVNLTGVflcgreaaAKMIES------GSKGVIINISS-IA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530375916 199 RMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnFI--AATSLYSPESIQAIAK 258
Cdd:PRK08217 154 RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPG-VIetEMTAAMKPEALERLEK 214
PRK07024 PRK07024
SDR family oxidoreductase;
144-239 2.88e-08

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 53.78  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 144 NAGIS--TFGEvEFTSLETYKQVAEVNLWGTVrmtKSFLPLI----RRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK07024  85 NAGISvgTLTE-EREDLAVFREVMDTNYFGMV---ATFQPFIapmrAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIK 160

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07024 161 YLESLRVELRPAGVRVVTIAPG 182
PRK06194 PRK06194
hypothetical protein; Provisional
 141-222 4.27e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 53.87  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPL-IRRAK------GRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLmLAAAEkdpayeGHIVNTASMAGLLAPPAMGIYNVSKH 166


                 ....*....
gi 530375916 214 GVEAFSDCL 222
Cdd:PRK06194 167 AVVSLTETL 175
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 56-251 4.46e-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: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRtVQLNVcsseevekvveIVRSSL---K 132
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIA-LAADV-----------LDRASLeraR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWG----LVNNAG--------ISTFGEVEFT------SLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNI 193
Cdd:cd08935   74 EEIVAQFGtvdiLINGAGgnhpdattDPEHYEPETEqnffdlDEEGWEFVFDLNLNGSFLPSQVFGkDMLEQKGGSIINI 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530375916 194 SSM-----LGRManPArspYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATS---LYSPE 251
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) ...
 56-239 4.64e-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: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLmkdKGHDGVKELDSLNSDRLRTVQLNVCSSEEVekvveivrSSLKDPE 135
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY---RSTESAEAVAAEAGERAIAIQADVRDRDQV--------QAMIEEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWG----LVNNAGI---------STFGEVEFtslETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMA 201
Cdd:cd05349   70 KNHFGpvdtIVNNALIdfpfdpdqrKTFDTIDW---EDYQQQLEGAVKGALNLLQAVLPdFKERGSGRVINIGTNLFQNP 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530375916 202 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05349  147 VVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGG 184
PRK07062 PRK07062
SDR family oxidoreductase;
140-239 6.08e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 53.12  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAG---ISTFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANP-------ARSpy 208
Cdd:PRK07062  90 MLVNNAGqgrVSTFAD---TTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPhmvatsaARA-- 164

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530375916 209 citkfGVEAFSDCLRYEMYPLGVKVS-----VVEPG 239
Cdd:PRK07062 165 -----GLLNLVKSLATELAPKGVRVNsillgLVESG 195
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 51-239 6.21e-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: 6.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  51 EPVGSKAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGV-KELDSLNSDRLrTVQLNVCSSEEVEKVVEIVRS 129
Cdd:cd08936    6 DPLANKVALVTASTDGIGLAIARRLAQDG----AHVVVSSRKQQNVdRAVATLQGEGL-SVTGTVCHVGKAEDRERLVAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 130 SLKDpEKGMWGLVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMANPARSP 207
Cdd:cd08936   81 AVNL-HGGVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMeKRGGGSVVIVSSVAAFHPFPGLGP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530375916 208 YCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPG 191
PRK06139 PRK06139
SDR family oxidoreductase;
142-228 6.94e-08

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 53.19  E-value: 6.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 142 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPlIRRAKGR--VVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK06139  89 VNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALP-IFKKQGHgiFINMISLGGFAAQPYAAAYSASKFGLRGFS 167


                 ....*....
gi 530375916 220 DCLRYEMYP 228
Cdd:PRK06139 168 EALRGELAD 176
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 140-239 8.33e-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: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd09761   78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVALT 157

                         90       100
                 ....*....|....*....|
gi 530375916 220 DCLRYEMYPlGVKVSVVEPG 239
Cdd:cd09761  158 HALAMSLGP-DIRVNCISPG 176
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-239 9.76e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 52.38  E-value: 9.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCD--SGFGFSLAKHLHSKGFLVFA----------GCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKV 123
Cdd:PRK12748   6 KIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmPWGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYAPNRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 124 VEIVRSSLKDPEKgmwgLVNNAGIST---FGEVEFTSL-ETYKqvaeVNLWGTVRMTKSFlplIR----RAKGRVVNISS 195
Cdd:PRK12748  86 FYAVSERLGDPSI----LINNAAYSThtrLEELTAEQLdKHYA----VNVRATMLLSSAF---AKqydgKAGGRIINLTS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530375916 196 --MLGRManPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
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 ...
 141-300 1.11e-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: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM-ANPARSPYCITKFGVEAF 218
Cdd:cd05368   74 LFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPGnfiaatSLYSPeSIQAIAKKmwEELPEVVRKDY------GKKYFDEKIAKMETYCSSGS 292
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPG------TVDTP-SLEERIQA--QPDPEEALKAFaarqplGRLATPEEVAALAVYLASDE 224

                        170
                 ....*....|..
gi 530375916 293 ----TDTSPVID 300
Cdd:cd05368  225 sayvTGTAVVID 236
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 53-258 1.38e-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: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  53 VGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLK 132
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERSDRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPekgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-----GRVVNISSMLGRMANPARS- 206
Cdd:cd08942   84 DV------LVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVVSGLENy 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF---IAATSLYSPESIQAIAK 258
Cdd:cd08942  158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFpskMTAFLLNDPAALEAEEK 212
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 54-238 1.56e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 52.18  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAvLVTGCDSGFGFSLAKHLHSKGF-LVFAGclmkdKGHDGVKEL-DSLNSDRLRTVQLNVCS--SEEVEKVVEIVRS 129
Cdd:PLN02780  53 GSWA-LVTGPTDGIGKGFAFQLARKGLnLVLVA-----RNPDKLKDVsDSIQSKYSKTQIKTVVVdfSGDIDEGVKRIKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 130 SLKDPEKGMwgLVNNAGIST-----FGEVEftsLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRM--A 201
Cdd:PLN02780 127 TIEGLDVGV--LINNVGVSYpyarfFHEVD---EELLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIVipS 201

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530375916 202 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:PLN02780 202 DPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVP 238
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 59-260 2.43e-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: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  59 LVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKeldslNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDPEKGM 138
Cdd:cd05371    6 VVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-----LGDNCRFVPVDVTSEKDVKAAL----ALAKAKFGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 139 WGLVNNAGISTF-------GEVEFtSLETYKQVAEVNLWGTVRMTKSFLPLIRR-------AKGRVVNISSMLGRMANPA 204
Cdd:cd05371   77 DIVVNCAGIAVAaktynkkGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKnepdqggERGVIINTASVAAFEGQIG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFiaATSLYS--PESIQAIAKKM 260
Cdd:cd05371  156 QAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLF--DTPLLAglPEKVRDFLAKQ 211
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 56-239 2.73e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 50.84  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGC-LMKDKGHDGVKELDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDP 134
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYgNRKEEAEETVYEIQS-NGGSAFSIGANLESLHGVEALYSSLDNELQNR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 --EKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRaKGRVVNISSMLGRMANPARSPYCITK 212
Cdd:PRK12747  84 tgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRISLPDFIAYSMTK 162

                        170       180
                 ....*....|....*....|....*..
gi 530375916 213 FGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPG 189
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 141-239 2.76e-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: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGiSTFGEVEFTSLETYKQVAEVN--LWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANpaRSPYCITKFGVEA 217
Cdd:PRK12823  88 LINNVG-GTIWAKPFEEYEEEQIEAEIRrsLFPTLWCCRAVLPhMLAQGGGAIVNVSSIATRGIN--RVPYSAAKGGVNA 164

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK12823 165 LTASLAFEYAEHGIRVNAVAPG 186
PRK09242 PRK09242
SDR family oxidoreductase;
128-238 3.69e-07

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 50.52  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 128 RSSLKDPEKGMWG----LVNNAGIS-TFGEVEFTSLEtYKQVAEVNLWGTVRMTKSFLPLI-RRAKGRVVNISSMLGRMA 201
Cdd:PRK09242  75 RRAILDWVEDHWDglhiLVNNAGGNiRKAAIDYTEDE-WRGIFETNLFSAFELSRYAHPLLkQHASSAIVNIGSVSGLTH 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530375916 202 NPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:PRK09242 154 VRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 141-240 3.84e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 50.67  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANP-ARSPYCITKFGVE 216
Cdd:PRK06523  81 LVHVLGGSSAPAGGFAALtdEEWQDELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPeSTTAYAAAKAALS 160

                         90       100
                 ....*....|....*....|....
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPGN 240
Cdd:PRK06523 161 TYSKSLSKEVAPKGVRVNTVSPGW 184
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 56-263 5.18e-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: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKE-----LDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSS 130
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEG----AKLSLVDLNEEGLEAakaalLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 131 LKDPEkgmwGLVNNAGIStfGEVEFT---SLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARS 206
Cdd:cd05330   80 FGRID----GFFNNAGIE--GKQNLTedfGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530375916 207 PYCITKFGVEAFS--DCLRYEMYplGVKVSVVEPGnfiAATSLYSPESIQAIAKKMWEE 263
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) ...
 56-238 5.77e-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: 50.08  E-value: 5.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05345    6 KVAIVTGAGSGFGEGIARRFAQEG----ARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KgmwgLVNNAGISTF-GEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:cd05345   82 I----LVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPhMEEQGGGVIINIASTAGLRPRPGLTWYNASKG 157

                        170       180
                 ....*....|....*....|....*
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEP 238
Cdd:cd05345  158 WVVTATKAMAVELAPRNIRVNCLCP 182
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 56-199 5.95e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 50.06  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGF-LVFAGcLMKDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVEIVRSslkdp 134
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGAtIVFND-INQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEK----- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWG-LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKGRVVNISSM---LGR 199
Cdd:PRK07097  84 EVGVIDiLVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMmseLGR 153
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 56-202 6.81e-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: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDS-LNSDRLRTVQLNVCSseevekvveiVRS----- 129
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKeTGNAKVEVIQLDLSS----------LASvrqfa 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530375916 130 -SLKDPEKGMWGLVNNAGI--STFGEVEfTSLEtyKQVAeVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMAN 202
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, ...
 58-207 7.32e-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: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCDSGFGFSLAKHLHSKGFLV--------FAGCLMKDKGhdGVKELdslnsdrlrTVQLnvcsseevekvveivrs 129
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVigidlreaDVIADLSTPE--GRAAA---------IADV----------------- 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530375916 130 sLKDPEKGMWGLVNNAGISTFGEVEFtsletykqVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSP 207
Cdd:cd05328   54 -LARCSGVLDGLVNCAGVGGTTVAGL--------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGAGWAQDKLE 123
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
141-239 7.62e-07

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 49.64  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP-LIRRAKG-RVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07067  84 LFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARhMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAVISY 163

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07067 164 TQSAALALIRHGINVNAIAPG 184
PRK06500 PRK06500
SDR family oxidoreductase;
144-265 7.71e-07

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 49.57  E-value: 7.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 144 NAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVN--ISSMLGRmanPARSPYCITKFGVEAFSDC 221
Cdd:PRK06500  87 NAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNgsINAHIGM---PNSSVYAASKAALLSLAKT 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530375916 222 LRYEMYPLGVKVSVVEPGNfiAATSLY-----SPESIQAIAKKMWEELP 265
Cdd:PRK06500 164 LSGELLPRGIRVNAVSPGP--VQTPLYgklglPEATLDAVAAQIQALVP 210
PRK08251 PRK08251
SDR family oxidoreductase;
144-243 7.76e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 49.55  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 144 NAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRA-KGRVVNISSMLGRMANP-ARSPYCITKFGVEAFSDC 221
Cdd:PRK08251  88 NAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQgSGHLVLISSVSAVRGLPgVKAAYAASKAGVASLGEG 167

                         90       100
                 ....*....|....*....|..
gi 530375916 222 LRYEMYPLGVKVSVVEPGnFIA 243
Cdd:PRK08251 168 LRAELAKTPIKVSTIEPG-YIR 188
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 141-251 9.23e-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: 9.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:cd05359   80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGnFI---AATSLYSPE 251
Cdd:cd05359  160 RYLAVELGPRGIRVNAVSPG-VIdtdALAHFPNRE 193
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 141-239 1.02e-06

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 49.40  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTfgEVEFTSL--ETYKQVAEVNLWGTVRMTKSFLPLIRRAKG-RVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK12859 100 LVNNAAYST--NNDFSNLtaEELDKHYMVNVRATTLLSSQFARGFDKKSGgRIINMTSGQFQGPMVGELAYAATKGAIDA 177

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
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 ...
 141-247 1.27e-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: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI---STFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:cd05353   92 LVNNAGIlrdRSFAK---MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGQANYSAAKLGLL 168

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPgnfIAATSL 247
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 ...
 140-239 1.40e-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: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAG-ISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK-GRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:cd05340   87 GVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAVSKFATEG 166

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05340  167 L*QVLADEYQQRNLRVNCINPG 188
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
58-242 2.35e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.44  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  58 VLVTGCdSGF-GFSLAKHLHSKGFLVFAGclmkDKGHDGVKELDSLnsDRLRTVQLNVCSseevekvVEIVRSSLKDPEk 136
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGL----DRSPPGAANLAAL--PGVEFVRGDLRD-------PEALAAALAGVD- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 137 gmwGLVNNAGISTFGEveftslETYKQVAEVNLWGTVRMtksfLPLIRRAK-GRVVNISSM--LGRMANP--------AR 205
Cdd:COG0451   67 ---AVVHLAAPAGVGE------EDPDETLEVNVEGTLNL----LEAARAAGvKRFVYASSSsvYGDGEGPidedtplrPV 133

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530375916 206 SPYCITKFGVEAFsdcLRYEMYPLGVKVSVVEPGNFI 242
Cdd:COG0451  134 SPYGASKLAAELL---ARAYARRYGLPVTILRPGNVY 167
PRK06124 PRK06124
SDR family oxidoreductase;
141-246 2.55e-06

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 48.17  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI---STFGEvefTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:PRK06124  92 LVNNVGArdrRPLAE---LDDAAIRALLETDLVAPILLSRLAAQRMKRqGYGRIIAITSIAGQVARAGDAVYPAAKQGLT 168

                         90       100       110
                 ....*....|....*....|....*....|
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPGNFiaATS 246
Cdd:PRK06124 169 GLMRALAAEFGPHGITSNAIAPGYF--ATE 196
PRK06114 PRK06114
SDR family oxidoreductase;
59-239 2.99e-06

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 47.85  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  59 LVTGCDSGFGFSLAKHLHSKGFLVfagCLMKDKGHDGVKE-LDSLNSDRLRTVQL--NVCSSEEVEKVVEIVRSSLkdpe 135
Cdd:PRK06114  12 FVTGAGSGIGQRIAIGLAQAGADV---ALFDLRTDDGLAEtAEHIEAAGRRAIQIaaDVTSKADLRAAVARTEAEL---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 kGMWGL-VNNAGISTFGEVEFTSLETYKQVAEVNLWGTvrmtksFLP-------LIRRAKGRVVNISSMLGRMANPA--R 205
Cdd:PRK06114  85 -GALTLaVNAAGIANANPAEEMEEEQWQTVMDINLTGV------FLScqaearaMLENGGGSIVNIASMSGIIVNRGllQ 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPG 191
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 161-290 3.72e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 47.64  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 161 YKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGn 240
Cdd:PRK07576 110 FKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG- 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530375916 241 FIAATSLY-----SPESIQAIAKKmweelpeVVRKDYGKKyfdEKIAKMETYCSS 290
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 ...
 56-318 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 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfAGCLMK-DKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVeivrSSLKDP 134
Cdd:cd05343    7 RVALVTGASVGIGAAVARALVQHGMKV-VGCARRvDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMF----SAIRTQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 EKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK---GRVVNISSMLGRMANPARSP--YC 209
Cdd:cd05343   82 HQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGHRVPPVSVFhfYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 210 ITKFGVEAFSDCLRYEMYPL--GVKVSVVEPGnfiaatslyspesiqaiakkmweelpeVVRKDYGKKYFDEKIAKME-T 286
Cdd:cd05343  162 ATKHAVTALTEGLRQELREAktHIRATSISPG---------------------------LVETEFAFKLHDNDPEKAAaT 214

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530375916 287 YCSSGSTDTSPVIDAVTHALTaTTPYTRYHPM 318
Cdd:cd05343  215 YESIPCLKPEDVANAVLYVLS-TPPHVQIHDI 245
PRK07035 PRK07035
SDR family oxidoreductase;
141-239 5.19e-06

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 47.32  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGIST-FGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07035  89 LVNNAAANPyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGVSPGDFQGIYSITKAAVISM 168

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07035 169 TKAFAKECAPFGIRVNALLPG 189
PRK06947 PRK06947
SDR family oxidoreductase;
55-239 6.29e-06

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 46.72  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKdp 134
Cdd:PRK06947   2 RKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 135 ekGMWGLVNNAGI----STFGEVEFTSLetyKQVAEVNLWGTV--------RMTKSflplirR--AKGRVVNISSMLGRM 200
Cdd:PRK06947  80 --RLDALVNNAGIvapsMPLADMDAARL---RRMFDTNVLGAYlcareaarRLSTD------RggRGGAIVNVSSIASRL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530375916 201 ANPAR-SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06947 149 GSPNEyVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPG 188
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 56-247 6.34e-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: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLR---TVQLNVcsseevekvveivrSSLK 132
Cdd:cd05326    5 KVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVHcdvTVEADV--------------RAAV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 133 DPEKGMWG----LVNNAGIS--TFGEVEFTSLETYKQVAEVNLWGTVRMTK-SFLPLIRRAKGRVVNISSMLGRMANPAR 205
Cdd:cd05326   71 DTAVARFGrldiMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVGGLGP 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530375916 206 SPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGnfIAATSL 247
Cdd:cd05326  151 HAYTASKHAVLGLTRSAATELGEHGIRVNCVSPY--GVATPL 190
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 141-239 7.24e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 46.95  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAG----ISTFGEVEFTSLE-TYKqvaeVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFGV 215
Cdd:PRK06701 128 LVNNAAfqypQQSLEDITAEQLDkTFK----TNIYSYFHMTKAALPHLKQG-SAIINTGSITGYEGNETLIDYSATKGAI 202

                         90       100
                 ....*....|....*....|....
gi 530375916 216 EAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06701 203 HAFTRSLAQSLVQKGIRVNAVAPG 226
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 141-258 1.12e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 45.99  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGIStfGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVV-NISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK06113  92 LVNNAGGG--GPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAENKNINMTSYASSKAAASHL 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPGNFI--AATSLYSPESIQAIAK 258
Cdd:PRK06113 170 VRNMAFDLGEKNIRVNGIAPGAILtdALKSVITPEIEQKMLQ 211
PRK06949 PRK06949
SDR family oxidoreductase;
56-274 1.33e-05

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 45.91  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDKGHDGVKEL----DSLNSDRlRTVQLNVCSSEEVekvveivRSSL 131
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAG----AKVVLASRRVERLKELraeiEAEGGAA-HVVSLDVTDYQSI-------KAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 132 KDPEKGMWG---LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTV--------RMtksflplIRRAKG--------RVVN 192
Cdd:PRK06949  78 AHAETEAGTidiLVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFfvaqevakRM-------IARAKGagntkpggRIIN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 193 ISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQaiAKKMWEELPevvRKDY 272
Cdd:PRK06949 151 IASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQ--GQKLVSMLP---RKRV 225


                 ..
gi 530375916 273 GK 274
Cdd:PRK06949 226 GK 227
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 141-275 1.36e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 45.80  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLI--RRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK12384  85 LVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMirDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPGNFiaatsLYSPesiqaiakkMWEEL-----------PEVVRKDYGKK 275
Cdd:PRK12384 165 TQSLALDLAEYGITVHSLMLGNL-----LKSP---------MFQSLlpqyakklgikPDEVEQYYIDK 218
PRK05717 PRK05717
SDR family oxidoreductase;
140-239 1.53e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 45.65  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAGISTFGEVEFTSLET--YKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK05717  87 ALVCNAAIADPHNTTLESLSLahWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLA 166

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPlGVKVSVVEPG 239
Cdd:PRK05717 167 LTHALAISLGP-EIRVNAVSPG 187
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 56-216 1.99e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 45.38  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKG--FLVFAGcLMKDKGHDGVKELDSLNSDrLRTVQLNVcsseevekvveivrSSLKD 133
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAERGaaGLVICG-RNAEKGEAQAAELEALGAK-AVFVQADL--------------SDVED 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEK----------GMWGLVNNAGISTFGEVEFTSLETYKQVAEVNL-------WGTVRMtksflpLIRR-AKGRVVNISS 195
Cdd:PRK06198  71 CRRvvaaadeafgRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVrapfflmQEAIKL------MRRRkAEGTIVNIGS 144

                        170       180
                 ....*....|....*....|.
gi 530375916 196 MLGRMANPARSPYCITKFGVE 216
Cdd:PRK06198 145 MSAHGGQPFLAAYCASKGALA 165
PRK08628 PRK08628
SDR family oxidoreductase;
140-259 2.87e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.95  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 140 GLVNNAGISTFGEVEfTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK08628  86 GLVNNAGVNDGVGLE-AGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530375916 220 DCLRYEMYPLGVKVSVVEPGNfiAATSLYS--------PES-IQAIAKK 259
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAE--VMTPLYEnwiatfddPEAkLAAITAK 211
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 56-281 4.21e-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: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KgmwgLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR--AKGRVVNISSMLGRMANPARSPYCITKF 213
Cdd:cd05322   83 L----LVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRdgIQGRIIQINSKSGKVGSKHNSGYSAAKF 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPGNFiaatsLYSP--ES-IQAIAKKMWEELPEVvrkdygKKYFDEKI 281
Cdd:cd05322  159 GGVGLTQSLALDLAEHGITVNSLMLGNL-----LKSPmfQSlLPQYAKKLGIKESEV------EQYYIDKV 218
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 141-239 5.28e-05

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 44.33  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLP--LIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK08936  89 MINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKyfVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLM 168

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08936 169 TETLAMEYAPKGIRVNNIGPG 189
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 59-241 6.53e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 43.99  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  59 LVTGCDSGFGFSLAKHLHSKGFLVFAgclmkdKGHDGVKeLDSlNSDRLRTVQLNVCSSEEVEKVVEIVRSSLK--DPEK 136
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLAQAGAEVIL------NGRDPAK-LAA-AAESLKGQGLSAHALAFDVTDHDAVRAAIDafEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 137 GMWG-LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMANPARSPYCITKFG 214
Cdd:PRK07523  86 GPIDiLVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGIAPYTATKGA 165

                        170       180
                 ....*....|....*....|....*..
gi 530375916 215 VEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK07523 166 VGNLTKGMATDWAKHGLQCNAIAPGYF 192
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
141-239 8.43e-05

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 43.57  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWG----TVRMTKSFlplIRRAKGRVVNISSMLGRMANPARSPYCITKFGVE 216
Cdd:PRK06935  95 LVNNAGTIRRAPLLEYKDEDWNAVMDINLNSvyhlSQAVAKVM---AKQGSGKIINIASMLSFQGGKFVPAYTASKHGVA 171

                         90       100
                 ....*....|....*....|...
gi 530375916 217 AFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06935 172 GLTKAFANELAAYNIQVNAIAPG 194
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 57-239 1.20e-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: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   57 AVLVTGCDSGFGFSLAKHLHSKGFLVfagCL-MKDKGHDGVKELDSLNSDRLRTVQlnVCSSEEVEKVVEIVR-SSLKDP 134
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRV---VLhYHRSAAAASTLAAELNARRPNSAV--TCQADLSNSATLFSRcEAIIDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  135 EKGMWG----LVNNA----------GISTFGEVEFTSLETykQVAEvnLWGTVRMTKSFL--PLIRRAKGR--------- 189
Cdd:TIGR02685  78 CFRAFGrcdvLVNNAsafyptpllrGDAGEGVGDKKSLEV--QVAE--LFGSNAIAPYFLikAFAQRQAGTraeqrstnl 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530375916  190 -VVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:TIGR02685 154 sIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG 204
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 141-239 1.98e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 42.30  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAgiSTFGEVEF-TSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFS 219
Cdd:PRK08265  84 LVNLA--CTYLDDGLaSSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLT 161

                         90       100
                 ....*....|....*....|
gi 530375916 220 DCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK08265 162 RSMAMDLAPDGIRVNSVSPG 181
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 56-239 2.19e-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: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGflvfAGCLMKDkghdgvkeldsLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPE 135
Cdd:cd05363    4 KTALITGSARGIGRAFAQAYVREG----ARVAIAD-----------INLEAARATAAEIGPAACAISLDVTDQASIDRCV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGM---WG----LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKG-RVVNISSMLGRMANPARS 206
Cdd:cd05363   69 AALvdrWGsidiLVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVArAMIAQGRGgKIINMASQAGRRGEALVG 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530375916 207 PYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:cd05363  149 VYCATKAAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK07074 PRK07074
SDR family oxidoreductase;
141-239 3.05e-04

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 41.68  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKGRVVNISSMLGRMA--NPArspYCITKFGVEA 217
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLeGMLKRSRGAVVNIGSVNGMAAlgHPA---YSAAKAGLIH 157

                         90       100
                 ....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK07074 158 YTKLLAVEYGRFGIRANAVAPG 179
PRK07023 PRK07023
SDR family oxidoreductase;
141-239 3.32e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.54  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI-STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR-AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07023  81 LINNAGTvEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGWSVYCATKAALDHH 160

                         90       100
                 ....*....|....*....|.
gi 530375916 219 SDCLRYEmYPLGVKVSVVEPG 239
Cdd:PRK07023 161 ARAVALD-ANRALRIVSLAPG 180
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 141-276 4.51e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 41.24  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGI---STFGEVEFTSLEtyKQVaEVNLWGTVRMTKSFLPLIRRAkGRVVNISSMLGRMANPARSPYCITKFGVEA 217
Cdd:PRK06077  88 LVNNAGLglfSPFLNVDDKLID--KHI-STDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGLSIYGAMKAAVIN 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530375916 218 FSDCLRYEMYPlGVKVSVVEPGnfiaatslyspesiqAIAKKMWEELPEVV---RKDYGKKY 276
Cdd:PRK06077 164 LTKYLALELAP-KIRVNAIAPG---------------FVKTKLGESLFKVLgmsEKEFAEKF 209
PRK06101 PRK06101
SDR family oxidoreductase;
55-239 5.08e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 41.01  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  55 SKAVLVTGCDSGFGFSLAKHLHSKGFLVFAgClmkDKGHDGVKELDSLNSDrLRTVQLNVCSSEEVEKVVeivrSSLK-D 133
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIA-C---GRNQSVLDELHTQSAN-IFTLAFDVTDHPGTKAAL----SQLPfI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 134 PEkgMWglVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKgRVVNISSMLGRMANPARSPYCITKF 213
Cdd:PRK06101  72 PE--LW--IFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPRAEAYGASKA 146

                        170       180
                 ....*....|....*....|....*.
gi 530375916 214 GVEAFSDCLRYEMYPLGVKVSVVEPG 239
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPG 172
PRK07856 PRK07856
SDR family oxidoreductase;
141-258 8.60e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 40.30  E-value: 8.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 141 LVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRR--AKGRVVNISSMLGRMANPARSPYCITKFGVEAF 218
Cdd:PRK07856  79 LVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNL 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530375916 219 SDCLRYEMYPlGVKVSVVEPGNFI--AATSLY-SPESIQAIAK 258
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, ...
 56-253 2.14e-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: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVfaGCLmkDKGHDGVKELDSLNSDRLRTVQLNVcsseevekvveivrSSLKDPE 135
Cdd:cd05348    5 EVALITGGGSGLGRALVERFVAEGAKV--AVL--DRSAEKVAELRADFGDAVVGVEGDV--------------RSLADNE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGM------WG----LVNNAGISTFgeveFTSL---------ETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSM 196
Cdd:cd05348   67 RAVarcverFGkldcFIGNAGIWDY----STSLvdipeekldEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSN 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530375916 197 LGRMANPARSPYCITKFGVEAFSDCLRYEMYPLgVKVSVVEPGNFiaATSLYSPESI 253
Cdd:cd05348  143 AGFYPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGM--VTDLRGPASL 196
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 59-266 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916   59 LVTGCDSGFGFS----LAKHLHSKGFLVfagcLMKDKGHDGVKELDS-----LNSDRLRTVQLNVCSSEEVEKVVEIVRS 129
Cdd:TIGR01500   4 LVTGASRGFGRTiaqeLAKCLKSPGSVL----VLSARNDEALRQLKAeigaeRSGLRVVRVSLDLGAEAGLEQLLKALRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  130 SLKDPEKGMWGLVNNAGI---STFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKG---RVVNISSMLGRMANP 203
Cdd:TIGR01500  80 LPRPKGLQRLLLINNAGTlgdVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530375916  204 ARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF-IAATSLYSPESIQAIAKKMWEELPE 266
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLdTDMQQQVREESVDPDMRKGLQELKA 223
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 56-241 2.67e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 38.97  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  56 KAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSdRLRTVQLNVCSSEEVekvveivRSSLKDPE 135
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGI-KAHAAPFNVTHKQEV-------EAAIEHIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 136 KGMWG---LVNNAGI------STFGEVEFTSLETYKQVAEVNLWGTV--RMtksflplIRRAKGRVVNISSMLGRMANPA 204
Cdd:PRK08085  82 KDIGPidvLINNAGIqrrhpfTEFPEQEWNDVIAVNQTAVFLVSQAVarYM-------VKRQAGKIINICSMQSELGRDT 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530375916 205 RSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNF 241
Cdd:PRK08085 155 ITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYF 191
PRK05867 PRK05867
SDR family oxidoreductase;
142-301 3.53e-03

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 38.48  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 142 VNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL-PLIRRAKG-RVVNISSMLGRMAN-PAR-SPYCITKFGVEA 217
Cdd:PRK05867  91 VCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAkAMVKQGQGgVIINTASMSGHIINvPQQvSHYCASKAAVIH 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916 218 FSDCLRYEMYPLGVKVSVVEPGnFIaATSLYSPesiQAIAKKMWEelPEVVRKDYGKKyfdEKIAKMETYCSSGS----T 293
Cdd:PRK05867 171 LTKAMAVELAPHKIRVNSVSPG-YI-LTELVEP---YTEYQPLWE--PKIPLGRLGRP---EELAGLYLYLASEAssymT 240


                 ....*...
gi 530375916 294 DTSPVIDA 301
Cdd:PRK05867 241 GSDIVIDG 248
PRK05854 PRK05854
SDR family oxidoreductase;
54-199 6.56e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 37.74  E-value: 6.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530375916  54 GSKAVlVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSD-RLRTVQLNVCSseevEKVVEIVRSSLK 132
Cdd:PRK05854  14 GKRAV-VTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDaKLSLRALDLSS----LASVAALGEQLR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530375916 133 DPEKGMWGLVNNAGIST----------FgEVEFTSletykqvaevNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGR 199
Cdd:PRK05854  89 AEGRPIHLLINNAGVMTpperqttadgF-ELQFGT----------NHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
 
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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