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Conserved domains on  [gi|30678677|ref|NP_191965|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

Protein Classification

dTDP-4-dehydrorhamnose reductase family protein( domain architecture ID 10142884)

dTDP-4-dehydrorhamnose reductase family protein is an extended short-chain dehydrogenase similar to bacterial dTDP-4-dehydrorhamnose reductase, dTDP-4-keto-6-deoxy-D-glucose reductase, and mammalian S-adenosylmethionine synthase 2 subunit beta; in addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
6-314 1.39e-83

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


:

Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 254.09  E-value: 1.39e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNYggeCELYDVAFTHHSSplparlldafphspaFPVDLKSGLGLNSISQDFrQPDVVVN 85
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERG---YEVIGTGRSRASL---------------FKLDLTDPDAVEEAIRDY-KPDVIIN 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSVPRACEQDPDSAMSINVPTSLVNWLSSFETNkTLLIHLSTDQVYQGVKSFYKEEDETVAVNVYGKSKVAAELLIK 165
Cdd:cd05254  62 CAAYTRVDKCESDPELAYRVNVLAPENLARAAKEVG-ARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 166 DKCQSFAILRSSIIFGPQTVSP-LPKtlpiqWIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWvsddkQMRLV 244
Cdd:cd05254 141 NANPRYLILRTSWLYGELKNGEnFVE-----WMLRLAAERKEVNVVHDQIGSPTYAADLADAILELIERN-----SLTGI 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 245 LNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVR 314
Cdd:cd05254 211 YHLSNSGPISKYEFAKLIADALGLPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
 
Name Accession Description Interval E-value
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
6-314 1.39e-83

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 254.09  E-value: 1.39e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNYggeCELYDVAFTHHSSplparlldafphspaFPVDLKSGLGLNSISQDFrQPDVVVN 85
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERG---YEVIGTGRSRASL---------------FKLDLTDPDAVEEAIRDY-KPDVIIN 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSVPRACEQDPDSAMSINVPTSLVNWLSSFETNkTLLIHLSTDQVYQGVKSFYKEEDETVAVNVYGKSKVAAELLIK 165
Cdd:cd05254  62 CAAYTRVDKCESDPELAYRVNVLAPENLARAAKEVG-ARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 166 DKCQSFAILRSSIIFGPQTVSP-LPKtlpiqWIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWvsddkQMRLV 244
Cdd:cd05254 141 NANPRYLILRTSWLYGELKNGEnFVE-----WMLRLAAERKEVNVVHDQIGSPTYAADLADAILELIERN-----SLTGI 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 245 LNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVR 314
Cdd:cd05254 211 YHLSNSGPISKYEFAKLIADALGLPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
6-318 4.73e-58

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 188.42  E-value: 4.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGnyggecELYDVAFTHHSsplparlldafphspafPVDLKSGLGLNSISQDFRqPDVVVN 85
Cdd:COG1091   1 RILVTGANGQLGRALVRLLAE------RGYEVVALDRS-----------------ELDITDPEAVAALLEEVR-PDVVIN 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSVPRACEQDPDSAMSINV--PTSLVNWLssfETNKTLLIHLSTDQVYQGVKS-FYKEEDETVAVNVYGKSKVAAEL 162
Cdd:COG1091  57 AAAYTAVDKAESEPELAYAVNAtgPANLAEAC---AELGARLIHISTDYVFDGTKGtPYTEDDPPNPLNVYGRSKLAGEQ 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 163 LIKDKCQSFAILRSSIIFGPQtvsplPKTLpIQWIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWVSDdkqmr 242
Cdd:COG1091 134 AVRAAGPRHLILRTSWVYGPH-----GKNF-VKTMLRLLKEGEELRVVDDQIGSPTYAADLARAILALLEKDLSG----- 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30678677 243 lVLNAGGPERLSRVQMAQMVAEVRGYDlSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVRLTLD 318
Cdd:COG1091 203 -IYHLTGSGETSWYEFARAIAELAGLD-ALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDWREALAELLA 276
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
7-318 1.86e-41

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 145.49  E-value: 1.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     7 VLIVGGTGYLGQHLLQAFAGNyGGECelydVAFTHHssplparlldafphspafPVDLKSGLGLNSISQDFRqPDVVVNC 86
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAER-GIEV----VALTRA------------------ELDLTDPEAVARLLREIK-PDVVVNA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    87 AALSVPRACEQDPDSAMSINV--PTSLVNWLSSFETnktLLIHLSTDQVYQGVK-SFYKEEDETVAVNVYGKSKVAAELL 163
Cdd:pfam04321  57 AAYTAVDKAESEPDLAYAINAlaPANLAEACAAVGA---PLIHISTDYVFDGTKpRPYEEDDETNPLNVYGRTKLAGEQA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   164 IKDKCQSFAILRSSIIFGpQTVSPLPKTlpiqwIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWVsDDKQMRL 243
Cdd:pfam04321 134 VRAAGPRHLILRTSWVYG-EYGNNFVKT-----MLRLAAEREELKVVDDQFGRPTWARDLADVLLQLLERLA-ADPPYWG 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30678677   244 VLNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVRLTLD 318
Cdd:pfam04321 207 VYHLSNSGQTSWYEFARAIFDEAGADPSEVRPITTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLD 281
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
6-180 1.05e-11

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 64.54  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    6 KVLIVGGTGYLGQHLLQAFAgnyggecelydvafthhssPLpARLLDAFPHSPAFPVDLKSGLGLNSISQDFRqPDVVVN 85
Cdd:PRK09987   2 NILLFGKTGQVGWELQRALA-------------------PL-GNLIALDVHSTDYCGDFSNPEGVAETVRKIR-PDVIVN 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   86 CAALSVPRACEQDPDSAMSINVpTSLVNWLSSFETNKTLLIHLSTDQVYQGVKSF-YKEEDETVAVNVYGKSKVAAELLI 164
Cdd:PRK09987  61 AAAHTAVDKAESEPEFAQLLNA-TSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIpWQETDATAPLNVYGETKLAGEKAL 139
                        170
                 ....*....|....*.
gi 30678677  165 KDKCQSFAILRSSIIF 180
Cdd:PRK09987 140 QEHCAKHLIFRTSWVY 155
 
Name Accession Description Interval E-value
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
6-314 1.39e-83

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 254.09  E-value: 1.39e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNYggeCELYDVAFTHHSSplparlldafphspaFPVDLKSGLGLNSISQDFrQPDVVVN 85
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERG---YEVIGTGRSRASL---------------FKLDLTDPDAVEEAIRDY-KPDVIIN 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSVPRACEQDPDSAMSINVPTSLVNWLSSFETNkTLLIHLSTDQVYQGVKSFYKEEDETVAVNVYGKSKVAAELLIK 165
Cdd:cd05254  62 CAAYTRVDKCESDPELAYRVNVLAPENLARAAKEVG-ARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 166 DKCQSFAILRSSIIFGPQTVSP-LPKtlpiqWIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWvsddkQMRLV 244
Cdd:cd05254 141 NANPRYLILRTSWLYGELKNGEnFVE-----WMLRLAAERKEVNVVHDQIGSPTYAADLADAILELIERN-----SLTGI 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 245 LNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVR 314
Cdd:cd05254 211 YHLSNSGPISKYEFAKLIADALGLPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
6-318 4.73e-58

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 188.42  E-value: 4.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGnyggecELYDVAFTHHSsplparlldafphspafPVDLKSGLGLNSISQDFRqPDVVVN 85
Cdd:COG1091   1 RILVTGANGQLGRALVRLLAE------RGYEVVALDRS-----------------ELDITDPEAVAALLEEVR-PDVVIN 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSVPRACEQDPDSAMSINV--PTSLVNWLssfETNKTLLIHLSTDQVYQGVKS-FYKEEDETVAVNVYGKSKVAAEL 162
Cdd:COG1091  57 AAAYTAVDKAESEPELAYAVNAtgPANLAEAC---AELGARLIHISTDYVFDGTKGtPYTEDDPPNPLNVYGRSKLAGEQ 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 163 LIKDKCQSFAILRSSIIFGPQtvsplPKTLpIQWIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWVSDdkqmr 242
Cdd:COG1091 134 AVRAAGPRHLILRTSWVYGPH-----GKNF-VKTMLRLLKEGEELRVVDDQIGSPTYAADLARAILALLEKDLSG----- 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30678677 243 lVLNAGGPERLSRVQMAQMVAEVRGYDlSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVRLTLD 318
Cdd:COG1091 203 -IYHLTGSGETSWYEFARAIAELAGLD-ALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDWREALAELLA 276
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
7-318 1.86e-41

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 145.49  E-value: 1.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     7 VLIVGGTGYLGQHLLQAFAGNyGGECelydVAFTHHssplparlldafphspafPVDLKSGLGLNSISQDFRqPDVVVNC 86
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAER-GIEV----VALTRA------------------ELDLTDPEAVARLLREIK-PDVVVNA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    87 AALSVPRACEQDPDSAMSINV--PTSLVNWLSSFETnktLLIHLSTDQVYQGVK-SFYKEEDETVAVNVYGKSKVAAELL 163
Cdd:pfam04321  57 AAYTAVDKAESEPDLAYAINAlaPANLAEACAAVGA---PLIHISTDYVFDGTKpRPYEEDDETNPLNVYGRTKLAGEQA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   164 IKDKCQSFAILRSSIIFGpQTVSPLPKTlpiqwIDSSLKKGDTVDFFHDEFRCPIYVKDLVNITFKLIDRWVsDDKQMRL 243
Cdd:pfam04321 134 VRAAGPRHLILRTSWVYG-EYGNNFVKT-----MLRLAAEREELKVVDDQFGRPTWARDLADVLLQLLERLA-ADPPYWG 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30678677   244 VLNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSASSIDRGVVSPADISMDITKLIHTLELSPTSFKEGVRLTLD 318
Cdd:pfam04321 207 VYHLSNSGQTSWYEFARAIFDEAGADPSEVRPITTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLD 281
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
6-318 8.24e-34

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 125.86  E-value: 8.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNygGecelYDV-AFTHHSSPLPArlLDAFPHSPAFPVDLKSglgLNSISQDFRQPDVVV 84
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLAR--G----HEVvGLDRSPPGAAN--LAALPGVEFVRGDLRD---PEALAAALAGVDAVV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  85 NCAALSVPRacEQDPDSAMSINVPTS--LVNWLSSFETNKtlLIHLSTDQVYQGVKSFYKEEDETVAVNVYGKSKVAAEL 162
Cdd:COG0451  70 HLAAPAGVG--EEDPDETLEVNVEGTlnLLEAARAAGVKR--FVYASSSSVYGDGEGPIDEDTPLRPVSPYGASKLAAEL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 163 LIKDKCQSF----AILRSSIIFGPQTVSPLPKtlpiqWIDsSLKKGDTVDFFHDE--FRCPIYVKDLVNITFKLIDRwvs 236
Cdd:COG0451 146 LARAYARRYglpvTILRPGNVYGPGDRGVLPR-----LIR-RALAGEPVPVFGDGdqRRDFIHVDDVARAIVLALEA--- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 237 dDKQMRLVLNAGGPERLSRVQMAQMVAEVRGYDLSLIkhvsassIDRGVVSPADISMDITKLIHTLELSP-TSFKEGVRL 315
Cdd:COG0451 217 -PAAPGGVYNVGGGEPVTLRELAEAIAEALGRPPEIV-------YPARPGDVRPRRADNSKARRELGWRPrTSLEEGLRE 288

                ...
gi 30678677 316 TLD 318
Cdd:COG0451 289 TVA 291
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
7-233 6.87e-21

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 89.66  E-value: 6.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     7 VLIVGGTGYLGQHLLQAFAGNYggecelYDVAFTHHSSPLPARLLDAfpHSPAFPVDLKSGLGLNSISQDFrQPDVVVNC 86
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKG------YEVIGLDRLTSASNTARLA--DLRFVEGDLTDRDALEKLLADV-RPDAVIHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    87 AALSVPRACEQDPDSAMSINV--PTSLVNWLssFETNKTLLIHLSTDQVYQGVKSFYKEED----ETVAVNVYGKSKVAA 160
Cdd:pfam01370  72 AAVGGVGASIEDPEDFIEANVlgTLNLLEAA--RKAGVKRFLFASSSEVYGDGAEIPQEETtltgPLAPNSPYAAAKLAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   161 ELLIKDKCQS----FAILRSSIIFGPQTVSPLPKTLPIQWIdSSLKKGDTVDFFHD-----EFrcpIYVKDLVNITFKLI 231
Cdd:pfam01370 150 EWLVLAYAAAyglrAVILRLFNVYGPGDNEGFVSRVIPALI-RRILEGKPILLWGDgtqrrDF---LYVDDVARAILLAL 225

                  ..
gi 30678677   232 DR 233
Cdd:pfam01370 226 EH 227
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
7-233 4.13e-20

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 86.59  E-value: 4.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAFAGNYggecelYDVafthhssplpaRLLDAFphspafpvdlksglglnsisqdfrqpDVVVNC 86
Cdd:cd08946   1 ILVTGGAGFIGSHLVRRLLERG------HEV-----------VVIDRL--------------------------DVVVHL 37
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  87 AALSVPRACEQDPDSAMSINVpTSLVNWLSSF-ETNKTLLIHLSTDQVYQGVKSFYKEEDE-TVAVNVYGKSKVAAELLI 164
Cdd:cd08946  38 AALVGVPASWDNPDEDFETNV-VGTLNLLEAArKAGVKRFVYASSASVYGSPEGLPEEEETpPRPLSPYGVSKLAAEHLL 116
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30678677 165 KDKCQSF----AILRSSIIFGPQTvsPLPKTLPIQWIDSSLKKGDTVDFF--HDEFRCPIYVKDLVNITFKLIDR 233
Cdd:cd08946 117 RSYGESYglpvVILRLANVYGPGQ--RPRLDGVVNDFIRRALEGKPLTVFggGNQTRDFIHVDDVVRAILHALEN 189
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
5-318 3.11e-13

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 69.12  E-value: 3.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   5 TKVLIVGGTGYLGQHLLQAFAGNYGG-ECELYDvAFTHHSSPLPARLLDAFPHSPAFPVDLKSGLGLNSISQDFRqPDVV 83
Cdd:cd05246   1 MKILVTGGAGFIGSNFVRYLLNKYPDyKIINLD-KLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLFEEEK-IDAV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  84 VNCAALS-VPRACEqDPDSAMSINV--PTSLVNwlSSFETNKTLLIHLSTDQVYQGVKS--FYKEEDETVAVNVYGKSKV 158
Cdd:cd05246  79 IHFAAEShVDRSIS-DPEPFIRTNVlgTYTLLE--AARKYGVKRFVHISTDEVYGDLLDdgEFTETSPLAPTSPYSASKA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 159 AAELLIKDKCQSFA----ILRSSIIFGP-QTVSPL-PKT---------LPIQwidsslkkGD---TVDFfhdefrcpIYV 220
Cdd:cd05246 156 AADLLVRAYHRTYGlpvvITRCSNNYGPyQFPEKLiPLFilnaldgkpLPIY--------GDglnVRDW--------LYV 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 221 KDLVNITFKLIDRWVSDDkqmrlVLNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSassiDRgvvsPA-DI--SMDITK 297
Cdd:cd05246 220 EDHARAIELVLEKGRVGE-----IYNIGGGNELTNLELVKLILELLGKDESLITYVK----DR----PGhDRryAIDSSK 286
                       330       340
                ....*....|....*....|..
gi 30678677 298 LIHTLELSP-TSFKEGVRLTLD 318
Cdd:cd05246 287 IRRELGWRPkVSFEEGLRKTVR 308
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
6-317 1.03e-11

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 64.65  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNYggeceLYDVAFTHHSSP--LPARLLDAFPHSPAFPVDLKSGLglnsisqdfRQPDVV 83
Cdd:cd05264   1 RVLIVGGNGFIGSHLVDALLEEG-----PQVRVFDRSIPPyeLPLGGVDYIKGDYENRADLESAL---------VGIDTV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  84 VNCAALSVPRACEQDPDSAMSINVpTSLVNWLSSF-ETNKTLLIHLST-DQVYqGV--KSFYKEEDETVAVNVYGKSKVA 159
Cdd:cd05264  67 IHLASTTNPATSNKNPILDIQTNV-APTVQLLEACaAAGIGKIIFASSgGTVY-GVpeQLPISESDPTLPISSYGISKLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 160 AELLIKDKCQ----SFAILRSSIIFGPQTvSPLPKTLPIQWIDSSLKKGDTVDFFHD--EFRCPIYVKDLVNITFKLidr 233
Cdd:cd05264 145 IEKYLRLYQYlyglDYTVLRISNPYGPGQ-RPDGKQGVIPIALNKILRGEPIEIWGDgeSIRDYIYIDDLVEALMAL--- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 234 wvSDDKQMRLVLNAGGPERLSRVQMAQMVAEVRGYDLSLIKHVSassidRGVVSPADIsMDITKLIHTLELSP-TSFKEG 312
Cdd:cd05264 221 --LRSKGLEEVFNIGSGIGYSLAELIAEIEKVTGRSVQVIYTPA-----RTTDVPKIV-LDISRARAELGWSPkISLEDG 292

                ....*
gi 30678677 313 VRLTL 317
Cdd:cd05264 293 LEKTW 297
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
6-180 1.05e-11

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 64.54  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    6 KVLIVGGTGYLGQHLLQAFAgnyggecelydvafthhssPLpARLLDAFPHSPAFPVDLKSGLGLNSISQDFRqPDVVVN 85
Cdd:PRK09987   2 NILLFGKTGQVGWELQRALA-------------------PL-GNLIALDVHSTDYCGDFSNPEGVAETVRKIR-PDVIVN 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   86 CAALSVPRACEQDPDSAMSINVpTSLVNWLSSFETNKTLLIHLSTDQVYQGVKSF-YKEEDETVAVNVYGKSKVAAELLI 164
Cdd:PRK09987  61 AAAHTAVDKAESEPEFAQLLNA-TSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIpWQETDATAPLNVYGETKLAGEKAL 139
                        170
                 ....*....|....*.
gi 30678677  165 KDKCQSFAILRSSIIF 180
Cdd:PRK09987 140 QEHCAKHLIFRTSWVY 155
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
6-183 4.00e-10

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 59.67  E-value: 4.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNyggecelydvaftHHSSPLPARLLDAFPHSpafpVDLKSGLGLNSISQDFRQPDVVVN 85
Cdd:cd05232   1 KVLVTGANGFIGRALVDKLLSR-------------GEEVRIAVRNAENAEPS----VVLAELPDIDSFTDLFLGVDAVVH 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALS-VPRACEQDPDSAMsinvptslvnwlssFETNKTLLIHLSTDQVYQGVKSF-----------------YKEEDET 147
Cdd:cd05232  64 LAARVhVMNDQGADPLSDY--------------RKVNTELTRRLARAAARQGVKRFvflssvkvngegtvgapFDETDPP 129
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30678677 148 VAVNVYGKSKVAAELLIKDKCQSF----AILRSSIIFGPQ 183
Cdd:cd05232 130 APQDAYGRSKLEAERALLELGASDgmevVILRPPMVYGPG 169
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
6-277 9.07e-10

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 58.07  E-value: 9.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNyGgecelYDVAFTHHSSplpaRLLDAFPHSPAFPVDLKSGLGLNSISQdFRQPDVVVN 85
Cdd:cd05265   2 KILIIGGTRFIGKALVEELLAA-G-----HDVTVFNRGR----TKPDLPEGVEHIVGDRNDRDALEELLG-GEDFDVVVD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  86 CAALSvPRACEQDpdsamsinvptslvnwLSSFETNKTLLIHLSTDQVYQGVKSFYKE-----EDETVAVNV---YGKSK 157
Cdd:cd05265  71 TIAYT-PRQVERA----------------LDAFKGRVKQYIFISSASVYLKPGRVITEstplrEPDAVGLSDpwdYGRGK 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 158 VAAELLIKDKCQ-SFAILRSSIIFGPQTvsPLPKtLPiQWIDsSLKKGDTVdFFHDEFRCP---IYVKDLVnitfKLIDR 233
Cdd:cd05265 134 RAAEDVLIEAAAfPYTIVRPPYIYGPGD--YTGR-LA-YFFD-RLARGRPI-LVPGDGHSLvqfIHVKDLA----RALLG 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 30678677 234 WVSDDKQMRLVLNAGGPERLSRVQMAQMVAEVRGYDLSLIkHVS 277
Cdd:cd05265 204 AAGNPKAIGGIFNITGDEAVTWDELLEACAKALGKEAEIV-HVE 246
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6-273 1.04e-09

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 58.41  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAgnYGGecelYDVAFTHHSSPLPARLLDA--FPHSPAFPVDLKSglgLNSISQDFRQPDVV 83
Cdd:cd05271   2 VVTVFGATGFIGRYVVNRLA--KRG----SQVIVPYRCEAYARRLLVMgdLGQVLFVEFDLRD---DESIRKALEGSDVV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  84 VNCAALSVpracEQDPDSAMSINV--PTSLVNWlsSFETNKTLLIHLSTdqvyQGVksfykeedETVAVNVYGKSKVAAE 161
Cdd:cd05271  73 INLVGRLY----ETKNFSFEDVHVegPERLAKA--AKEAGVERLIHISA----LGA--------DANSPSKYLRSKAEGE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 162 LLIKDKCQSFAILRSSIIFGPQ-----TVSPLPKTLPIQwidSSLKKGDTVdffhdeFRcPIYVKDLVnitfKLIDRWVS 236
Cdd:cd05271 135 EAVREAFPEATIVRPSVVFGREdrflnRFAKLLAFLPFP---PLIGGGQTK------FQ-PVYVGDVA----EAIARALK 200
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 30678677 237 DDKQMRLVLNAGGPERLSRVQMAQMVAEVRGYDLSLI 273
Cdd:cd05271 201 DPETEGKTYELVGPKVYTLAELVELLRRLGGRKRRVL 237
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
7-183 1.29e-09

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 58.15  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAFAGNyggECELYdvAFTHHSSPLPAR-LLDAFPHSPAFPVDL-----KSGLGLNSISQDFRQP 80
Cdd:cd05263   1 VFVTGGTGFLGRHLVKRLLEN---GFKVL--VLVRSESLGEAHeRIEEAGLEADRVRVLegdltQPNLGLSAAASRELAG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  81 --DVVVNCAALSVPRACEQDPDSAmSINVPTSLVNWLSSFETNKtlLIHLSTDQV---YQGVksFYKEEDETVA--VNVY 153
Cdd:cd05263  76 kvDHVIHCAASYDFQAPNEDAWRT-NIDGTEHVLELAARLDIQR--FHYVSTAYVagnREGN--IRETELNPGQnfKNPY 150
                       170       180       190
                ....*....|....*....|....*....|..
gi 30678677 154 GKSKVAAELLIKDKCQSF--AILRSSIIFGPQ 183
Cdd:cd05263 151 EQSKAEAEQLVRAAATQIplTVYRPSIVVGDS 182
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
6-318 5.77e-09

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 56.54  E-value: 5.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNyggECELYdvAFTHHSSPLPARLLDAFPHsPAFPV---DLKSGLGLNSISQDFrqpDV 82
Cdd:cd05257   1 NVLVTGADGFIGSHLTERLLRE---GHEVR--ALDIYNSFNSWGLLDNAVH-DRFHFisgDVRDASEVEYLVKKC---DV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  83 VVNCAALsvpraceqdpdsamsINVPTSLVNWLSSFETN---------------KTLLIHLSTDQVYQGVKSFY-KEEDE 146
Cdd:cd05257  72 VFHLAAL---------------IAIPYSYTAPLSYVETNvfgtlnvleaacvlyRKRVVHTSTSEVYGTAQDVPiDEDHP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 147 TVAVNV----YGKSKVAAELLIKDKCQSF----AILR---------SSIIFGPQTVSPLPKTLPIqwidssLKKGDT--- 206
Cdd:cd05257 137 LLYINKprspYSASKQGADRLAYSYGRSFglpvTIIRpfntygprqSARAVIPTIISQRAIGQRL------INLGDGspt 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 207 --VDFFHDEFRCPIYVKDlvnitfklidrwvSDDKQMRLVLNAGGPE--------RLSRVQMAQMVAEV----RGYDlsl 272
Cdd:cd05257 211 rdFNFVKDTARGFIDILD-------------AIEAVGEIINNGSGEEisignpavELIVEELGEMVLIVyddhREYR--- 274
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 30678677 273 ikhVSASSIDRGVVspadismDITKLIHTLELSP-TSFKEGVRLTLD 318
Cdd:cd05257 275 ---PGYSEVERRIP-------DIRKAKRLLGWEPkYSLRDGLRETIE 311
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-318 6.96e-09

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 56.07  E-value: 6.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAGNyGGECELYDVAFTHHSSPLParlldafPHSPAFP---VDLKSGLGLNSISQDfrqPDV 82
Cdd:cd05256   1 RVLVTGGAGFIGSHLVERLLER-GHEVIVLDNLSTGKKENLP-------EVKPNVKfieGDIRDDELVEFAFEG---VDY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  83 VVNCAAL-SVPRACEqDPDSAMSINVPTSLVNWLSSFETNKTLLIHLSTDQVYQGVKSFYKEEDETVA-VNVYGKSKVAA 160
Cdd:cd05256  70 VFHQAAQaSVPRSIE-DPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDEDHPPNpLSPYAVSKYAG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 161 ELLIKDKCQSFAI----LRSSIIFGPQ--TVSPLPKTLPIqWIDSSLKK------GD---TVDFfhdefrcpIYVKDLVN 225
Cdd:cd05256 149 ELYCQVFARLYGLptvsLRYFNVYGPRqdPNGGYAAVIPI-FIERALKGepptiyGDgeqTRDF--------TYVEDVVE 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 226 ITFKLIDRWVSDDkqmrlVLNAGGPERLSRVQMAQMVAEVRGYDLslikhvsasSIDRGVVSPADIS---MDITKLIHTL 302
Cdd:cd05256 220 ANLLAATAGAGGE-----VYNIGTGKRTSVNELAELIREILGKEL---------EPVYAPPRPGDVRhslADISKAKKLL 285
                       330
                ....*....|....*..
gi 30678677 303 ELSP-TSFKEGVRLTLD 318
Cdd:cd05256 286 GWEPkVSFEEGLRLTVE 302
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
6-175 1.09e-07

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 52.54  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQH----LLQAfagnyGGECELYDVAFTHHSSPLPARlldAFPHSPAFPVDLKSGLGLNSISQDFRqPD 81
Cdd:cd05247   1 KVLVTGGAGYIGSHtvveLLEA-----GYDVVVLDNLSNGHREALPRI---EKIRIEFYEGDIRDRAALDKVFAEHK-ID 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  82 VVVNCAAL-SVPRACeQDPDSAMSINVpTSLVNWLSSF-ETNKTLLIHLSTDQVYqGVKSF--YKEEDETVAVNVYGKSK 157
Cdd:cd05247  72 AVIHFAALkAVGESV-QKPLKYYDNNV-VGTLNLLEAMrAHGVKNFVFSSSAAVY-GEPETvpITEEAPLNPTNPYGRTK 148
                       170       180
                ....*....|....*....|..
gi 30678677 158 VAAELLIKDKCQS----FAILR 175
Cdd:cd05247 149 LMVEQILRDLAKApglnYVILR 170
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
7-181 1.49e-07

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. 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.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 50.48  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAfAGNYGgecelydvafthHSSPLPARLLDAFPHSPAFPVDLKSG--LGLNSISQDFRQPDVVV 84
Cdd:cd05226   1 ILILGATGFIGRALARE-LLEQG------------HEVTLLVRNTKRLSKEDQEPVAVVEGdlRDLDSLSDAVQGVDVVI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  85 NCAALSVPRA--CEQDPDSAMSInVPTSLVNWLSSFetnktllIHLSTDQVYQGVksfyKEEDETVAVNVYGKSKVAAEL 162
Cdd:cd05226  68 HLAGAPRDTRdfCEVDVEGTRNV-LEAAKEAGVKHF-------IFISSLGAYGDL----HEETEPSPSSPYLAVKAKTEA 135
                       170
                ....*....|....*....
gi 30678677 163 LIKDKCQSFAILRSSIIFG 181
Cdd:cd05226 136 VLREASLPYTIVRPGVIYG 154
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
7-182 1.56e-07

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 51.98  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAFAGNYGGECELYDVAFTHHSSPLPArlldafPHSPAFPVDLKSGLGLNSISqDFRQPDVVVNC 86
Cdd:cd09813   2 CLVVGGSGFLGRHLVEQLLRRGNPTVHVFDIRPTFELDPSSS------GRVQFHTGDLTDPQDLEKAF-NEKGPNVVFHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  87 AAlsvpraceqdPDSAM------SINVPTSLVNWLSSFETNKTLLIHLSTDQVYQGVKSFyKEEDET-----VAVNVYGK 155
Cdd:cd09813  75 AS----------PDHGSnddlyyKVNVQGTRNVIEACRKCGVKKLVYTSSASVVFNGQDI-INGDESlpypdKHQDAYNE 143
                       170       180       190
                ....*....|....*....|....*....|..
gi 30678677 156 SKVAAELLI---KDKCQSF--AILRSSIIFGP 182
Cdd:cd09813 144 TKALAEKLVlkaNDPESGLltCALRPAGIFGP 175
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
5-314 1.64e-07

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 52.29  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   5 TKVLIVGGTGYLGQHLLQAFAGNyGGECELYDvAFTHHSSPLPARLLDAFPHSPAF---PVDLKSglgLNSISQDFRQPD 81
Cdd:cd05258   1 MRVLITGGAGFIGSNLARFFLKQ-GWEVIGFD-NLMRRGSFGNLAWLKANREDGGVrfvHGDIRN---RNDLEDLFEDID 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  82 VVVNCAAlsvpraceqDPDSAMSINVPTSLvnwlssFETN----------------KTLLIHLSTDQVYQGVKSFYK-EE 144
Cdd:cd05258  76 LIIHTAA---------QPSVTTSASSPRLD------FETNalgtlnvleaarqhapNAPFIFTSTNKVYGDLPNYLPlEE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 145 DET---------------------VAVNVYGKSKVAAELLIKDKCQSF----AILRSSIIFGPQ---------------- 183
Cdd:cd05258 141 LETryelapegwspagisesfpldFSHSLYGASKGAADQYVQEYGRIFglktVVFRCGCLTGPRqfgtedqgwvayflkc 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 184 TVSPLPKTLpiqwidSSLKKGDTVDFFHdefrcpiyVKDLVNitfkLIDRWV-SDDKQMRLVLN-AGGPErlSRVQMAQM 261
Cdd:cd05258 221 AVTGKPLTI------FGYGGKQVRDVLH--------SADLVN----LYLRQFqNPDRRKGEVFNiGGGRE--NSVSLLEL 280
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30678677 262 VAEVRgyDLSLIKHVSASSIDRgvvsPAD----ISmDITKLIHTLELSPT-SFKEGVR 314
Cdd:cd05258 281 IALCE--EITGRKMESYKDENR----PGDqiwyIS-DIRKIKEKPGWKPErDPREILA 331
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
6-182 1.77e-07

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 52.00  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFagnyggeceLYDVAFTHhssplpARLLDAFphSPAFPVDLKSglgLNSISQDFRQP----- 80
Cdd:cd05238   2 KVLITGASGFVGQRLAERL---------LSDVPNER------LILIDVV--SPKAPSGAPR---VTQIAGDLAVPaliea 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  81 -----DVVVNCAALSVPRACEQDPDSAMSINVPTSLvNWLSSFETN--KTLLIHLSTDQVYQGVKSfYKEEDETVAV--N 151
Cdd:cd05238  62 langrPDVVFHLAAIVSGGAEADFDLGYRVNVDGTR-NLLEALRKNgpKPRFVFTSSLAVYGLPLP-NPVTDHTALDpaS 139
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30678677 152 VYGKSKVAAELLIKD-----KCQSFAILRSSIIFGP 182
Cdd:cd05238 140 SYGAQKAMCELLLNDysrrgFVDGRTLRLPTVCVRP 175
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
7-224 3.03e-07

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 51.28  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAFAGNYGGECELYDVAFThhssplparlldAFPHSPAFPVDLKSGLG----LNSISQDFRQPDV 82
Cdd:cd05241   2 VLVTGGSGFFGERLVKQLLERGGTYVRSFDIAPP------------GEALSAWQHPNIEFLKGditdRNDVEQALSGADC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  83 VVNCAALsVPRACEQdpDSAMSINVPTSLVNWLSSFETNKTLLIHLSTDQVYQGVKSFYKEEDET----VAVNVYGKSKV 158
Cdd:cd05241  70 VFHTAAI-VPLAGPR--DLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGGQNIHNGDETLpyppLDSDMYAETKA 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30678677 159 AAELLI-KDKCQS---FAILRSSIIFGPQTVSPLPKTLpiqwiDSSLKKGDTVDFFHDEFR-CPIYVKDLV 224
Cdd:cd05241 147 IAEIIVlEANGRDdllTCALRPAGIFGPGDQGLVPILF-----EWAEKGLVKFVFGRGNNLvDFTYVHNLA 212
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
9-184 2.53e-06

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 47.99  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     9 IVGGTGYLGQHLLQAFAGNYGGECELYdvAFTHHSSPLPA--RLLDAFPHSPAF------------PV--DL-KSGLGLN 71
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIY--LLVRAKDGESAleRLRQELEKYPLFdallkealerivPVagDLsEPNLGLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    72 SisQDFR----QPDVVVNCAAL--SVPRAceqdpDSAMSINV-PTSLVNWLSSFETNKTLLIHLST------------DQ 132
Cdd:pfam07993  79 E--EDFQelaeEVDVIIHSAATvnFVEPY-----DDARAVNVlGTREVLRLAKQGKQLKPFHHVSTayvngergglveEK 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30678677   133 VYQGVKSFYKEEDETVAV-----NVYGKSKVAAELLIKDKCQS---FAILRSSIIFG-PQT 184
Cdd:pfam07993 152 PYPEGEDDMLLDEDEPALlgglpNGYTQTKWLAEQLVREAARRglpVVIYRPSIITGePKT 212
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
8-179 2.65e-06

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 48.31  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     8 LIVGGTGYLGQHLLQAFAGNYggecelYDV-AFTHHSSPLPARLLDAFPHSPAFP------VDLKSGLGLNSISQDFrQP 80
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKG------YEVhGIVRRSSSFNTGRLEHLYDDHLNGnlvlhyGDLTDSSNLVRLLAEV-QP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677    81 DVVVNCAALS-VPRACEQdPDSAMSINVpTSLVNWLSSFET----NKTLLIHLSTDQVYQGVK-SFYKEEDETVAVNVYG 154
Cdd:pfam16363  74 DEIYNLAAQShVDVSFEQ-PEYTADTNV-LGTLRLLEAIRSlgleKKVRFYQASTSEVYGKVQeVPQTETTPFYPRSPYA 151
                         170       180
                  ....*....|....*....|....*
gi 30678677   155 KSKVAAELLIKDKCQSFAILRSSII 179
Cdd:pfam16363 152 AAKLYADWIVVNYRESYGLFACNGI 176
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
7-187 4.60e-06

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 47.67  E-value: 4.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   7 VLIVGGTGYLGQHLLQAFAGnyggecELYDV-AFTHHSSPLparlldafPHSPAFPVDLKSG--LGLNSISQDFRQPDVV 83
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLA------QGYRVrALVRSGSDA--------VLLDGLPVEVVEGdlTDAASLAAAMKGCDRV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  84 VNCAAlsVPRACEQDPDSAMSINVpTSLVNWL-SSFETNKTLLIHLSTDQVYQGVKSFYKEEDETVAV----NVYGKSKV 158
Cdd:cd05228  67 FHLAA--FTSLWAKDRKELYRTNV-EGTRNVLdAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWNErpfpNDYYRSKL 143
                       170       180       190
                ....*....|....*....|....*....|..
gi 30678677 159 AAELLIK---DKCQSFAILRSSIIFGPQTVSP 187
Cdd:cd05228 144 LAELEVLeaaAEGLDVVIVNPSAVFGPGDEGP 175
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
3-181 1.52e-05

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 45.69  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   3 KKTKVLIVGGTGYLGQHLLQAFAGNYGGECELYDVA-FTHHSspLPARLLDAFPHspafpVDLKSGLG-------LNSIS 74
Cdd:cd05237   1 KGKTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDeNKLHE--LVRELRSRFPH-----DKLRFIIGdvrdkerLRRAF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  75 QDfRQPDVVVNCAALSVPRACEQDPDSAMSINVPTS--LVNWLSSFETNKTLLIhlSTDqvyqgvKSFYkeedetvAVNV 152
Cdd:cd05237  74 KE-RGPDIVFHAAALKHVPSMEDNPEEAIKTNVLGTknVIDAAIENGVEKFVCI--STD------KAVN-------PVNV 137
                       170       180       190
                ....*....|....*....|....*....|
gi 30678677 153 YGKSKVAAELLIKDK-CQSFAILRSSIIFG 181
Cdd:cd05237 138 MGATKRVAEKLLLAKnEYSSSTKFSTVRFG 167
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
6-318 1.96e-05

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 45.71  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFAgNYGGECELYDVAFTHHSSPLpARLLDAfphsPAFPVdlksglglnsISQDFRQP----- 80
Cdd:cd05230   2 RILITGGAGFLGSHLCDRLL-EDGHEVICVDNFFTGRKRNI-EHLIGH----PNFEF----------IRHDVTEPlylev 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  81 DVVVNCAALSVPRACEQDPDSAMSINVPTSLvNWLSSFETNKTLLIHLSTDQVY-------Q-----------GVKSFYK 142
Cdd:cd05230  66 DQIYHLACPASPVHYQYNPIKTLKTNVLGTL-NMLGLAKRVGARVLLASTSEVYgdpevhpQpesywgnvnpiGPRSCYD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 143 EedetvavnvygkSKVAAELLIKDKCQSFAI-LRSSIIF---GP-------QTVSplpktlpiQWIDSSLKkGDTVDFFH 211
Cdd:cd05230 145 E------------GKRVAETLCMAYHRQHGVdVRIARIFntyGPrmhpndgRVVS--------NFIVQALR-GEPITVYG 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 212 D--EFRCPIYVKDLVNITFKLIDrwvSDDKQMrlVLNAGGPERLSRVQMAQMVAEVRGYDlSLIKHVSASSIDrgvvsPA 289
Cdd:cd05230 204 DgtQTRSFQYVSDLVEGLIRLMN---SDYFGG--PVNLGNPEEFTILELAELVKKLTGSK-SEIVFLPLPEDD-----PK 272
                       330       340       350
                ....*....|....*....|....*....|
gi 30678677 290 DISMDITKLIHTLELSPT-SFKEGVRLTLD 318
Cdd:cd05230 273 RRRPDISKAKELLGWEPKvPLEEGLRRTIE 302
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
6-163 7.09e-04

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 40.66  E-value: 7.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTG----YLGQHLLQAfagnygGecelYDV--AFTHHSSPLPARLLDAFPHSPAF---PVDLKSGLGLNSISQD 76
Cdd:cd05260   1 RALITGITGqdgsYLAEFLLEK------G----YEVhgIVRRSSSFNTDRIDHLYINKDRItlhYGDLTDSSSLRRAIEK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  77 FrQPDVVVNCAALSVPRACEQDPDSAMSINVPTSLvNWLSSFETNK--TLLIHLSTDQVYQGVKSFYKEEDETV-AVNVY 153
Cdd:cd05260  71 V-RPDEIYHLAAQSHVKVSFDDPEYTAEVNAVGTL-NLLEAIRILGldARFYQASSSEEYGKVQELPQSETTPFrPRSPY 148
                       170
                ....*....|
gi 30678677 154 GKSKVAAELL 163
Cdd:cd05260 149 AVSKLYADWI 158
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
6-233 9.47e-04

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 40.40  E-value: 9.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAFA------------GNYggecelYDVAFTHHSsplpARLLDAFPHSPAFPVDLKSGLGLNSI 73
Cdd:cd05253   2 KILVTGAAGFIGFHVAKRLLergdevvgidnlNDY------YDVRLKEAR----LELLGKSGGFKFVKGDLEDREALRRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  74 SQDFrQPDVVVNCAALSVPRACEQDPDSAMSINVPTSLvNWLSSFETNKTL-LIHLSTDQVYQGVKSFYKEEDETVA--V 150
Cdd:cd05253  72 FKDH-EFDAVIHLAAQAGVRYSLENPHAYVDSNIVGFL-NLLELCRHFGVKhLVYASSSSVYGLNTKMPFSEDDRVDhpI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677 151 NVYGKSKVAAELLIKDKCQSFAI----LRSSIIFGPQTVSPLPKTLPIQWIDsslkKGDTVDFFHD-----EFrcpIYVK 221
Cdd:cd05253 150 SLYAATKKANELMAHTYSHLYGIpttgLRFFTVYGPWGRPDMALFLFTKAIL----EGKPIDVFNDgnmsrDF---TYID 222
                       250
                ....*....|..
gi 30678677 222 DLVNITFKLIDR 233
Cdd:cd05253 223 DIVEGVVRALDT 234
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
5-108 1.06e-03

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 395010 [Multi-domain]  Cd Length: 141  Bit Score: 38.74  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677     5 TKVLIVGGTGYLGQHLLQAFA-GNYGGECELYDVAFTHhsspLPARLLDaFPHSPAF-PVDLKSGLGLNSisqDFRQPDV 82
Cdd:pfam00056   1 VKVAVVGAAGGVGQSLAFLLAnKGLADELVLYDIVKEK----LEGVAMD-LSHGSTFlLVPGIVGGGDYE---DLKDADV 72
                          90       100
                  ....*....|....*....|....*.
gi 30678677    83 VVNCAAlsVPRACEQDPDSAMSINVP 108
Cdd:pfam00056  73 VVITAG--VPRKPGMTRLDLLNVNAK 96
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
6-92 2.64e-03

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 38.82  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677   6 KVLIVGGTGYLGQHLLQAF--AGNYggecELYdvAFTHHSSPLPARLLDafPHSPAFPVDLKSglgLNSISQDFRQPDVV 83
Cdd:cd05259   1 KIAIAGATGTLGGPIVSALlaSPGF----TVT--VLTRPSSTSSNEFQP--SGVKVVPVDYAS---HESLVAALKGVDAV 69

                ....*....
gi 30678677  84 VNCAALSVP 92
Cdd:cd05259  70 ISALGGAAI 78
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
63-171 3.31e-03

CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4,6-dehydratase, an extended SDR, which catalyzes the conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 38.84  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678677  63 DLKSGLGLNSISQDFrQPDVVVNCAALSVPRACEQDPDSAMSINVpTSLVNWLSSFETNKTL--LIHLSTDQVYQGVKSF 140
Cdd:cd05252  60 DIRDLNALREAIREY-EPEIVFHLAAQPLVRLSYKDPVETFETNV-MGTVNLLEAIRETGSVkaVVNVTSDKCYENKEWG 137
                        90       100       110
                ....*....|....*....|....*....|...
gi 30678677 141 --YKEEDETVAVNVYGKSKVAAELLIKDKCQSF 171
Cdd:cd05252 138 wgYRENDPLGGHDPYSSSKGCAELIISSYRNSF 170
 
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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