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Conserved domains on  [gi|11034825|ref|NP_037415|]
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methionine adenosyltransferase 2 subunit beta isoform 1 [Homo sapiens]

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; ...
30-316 3.10e-132

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: 377.74  E-value: 3.10e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARpkFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRAS--LFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESDPELA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEV 189
Cdd:cd05254  79 YRVNVLAPENLARAAKEVGARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVLNANPRYLILRTSWLYGEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 190 eKLEESAVTVMFDKVQFsNKSANMDHWQQRFPTHVKDVATVCRQLAEKRmldpSIKGTFHWSGNEQMTKYEMACAIADAF 269
Cdd:cd05254 159 -KNGENFVEWMLRLAAE-RKEVNVVHDQIGSPTYAADLADAILELIERN----SLTGIYHLSNSGPISKYEFAKLIADAL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 11034825 270 NLPSSHLRPITDS-PVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIK 316
Cdd:cd05254 233 GLPDVEIKPITSSeYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 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; ...
30-316 3.10e-132

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: 377.74  E-value: 3.10e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARpkFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRAS--LFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESDPELA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEV 189
Cdd:cd05254  79 YRVNVLAPENLARAAKEVGARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVLNANPRYLILRTSWLYGEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 190 eKLEESAVTVMFDKVQFsNKSANMDHWQQRFPTHVKDVATVCRQLAEKRmldpSIKGTFHWSGNEQMTKYEMACAIADAF 269
Cdd:cd05254 159 -KNGENFVEWMLRLAAE-RKEVNVVHDQIGSPTYAADLADAILELIERN----SLTGIYHLSNSGPISKYEFAKLIADAL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 11034825 270 NLPSSHLRPITDS-PVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIK 316
Cdd:cd05254 233 GLPDVEIKPITSSeYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
31-323 2.45e-119

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: 345.41  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    31 VLVTGATGLLGRAVHKEFQQNNWHAVGCgFRRarpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAAS 110
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGIEVVAL-TRA------ELDLTDPEAVARLLREIKPDVVVNAAAYTAVDKAESEPDLAY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   111 QLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEV 189
Cdd:pfam04321  74 AINALAPANLAEACAAVGAPLIHISTDYVFDGTKPrPYEEDDETNPLNVYGRTKLAGEQAVRAAGPRHLILRTSWVYGEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   190 EKleeSAVTVMFDKVqFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAF 269
Cdd:pfam04321 154 GN---NFVKTMLRLA-AEREELKVVDDQFGRPTWARDLADVLLQLLERLAADPPYWGVYHLSNSGQTSWYEFARAIFDEA 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11034825   270 NLPSSHLRPI-TDSPVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIKESLWPFL 323
Cdd:pfam04321 230 GADPSEVRPItTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLDELL 284
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
30-319 6.79e-88

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 265.07  E-value: 6.79e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRrarpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:COG1091   1 RILVTGANGQLGRALVRLLAERGYEVVALDRS-------ELDITDPEAVAALLEEVRPDVVINAAAYTAVDKAESEPELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGE 188
Cdd:COG1091  74 YAVNATGPANLAEACAELGARLIHISTDYVFDGTKGtPYTEDDPPNPLNVYGRSKLAGEQAVRAAGPRHLILRTSWVYGP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 189 VEKleeSAVTVMFDKVQfSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRmldpsIKGTFHWSGNEQMTKYEMACAIADA 268
Cdd:COG1091 154 HGK---NFVKTMLRLLK-EGEELRVVDDQIGSPTYAADLARAILALLEKD-----LSGIYHLTGSGETSWYEFARAIAEL 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 11034825 269 FNLPsSHLRPI-TDSPVLGAQRPRNAQLDCSKLE-TLGIGQRtPFRIGIKESL 319
Cdd:COG1091 225 AGLD-ALVEPItTAEYPTPAKRPANSVLDNSKLEaTLGIKPP-DWREALAELL 275
rmlD TIGR01214
dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making ...
30-319 1.76e-54

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273505 [Multi-domain]  Cd Length: 287  Bit Score: 179.90  E-value: 1.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    30 RVLVTGATGLLGRAVHKEFQQNNWhaVGCGFRRArpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:TIGR01214   1 RILITGANGQLGRELVQQLSPEGR--VVVALTRS-----QLDLTDPEALERLLRAIRPDAVVNTAAYTDVDGAESDPEKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGE 188
Cdd:TIGR01214  74 FAVNALAPQNLARAAARHGARLVHISTDYVFDGEGKrPYREDDATNPLNVYGQSKLAGEQAVRAAGPNALIVRTSWLYGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   189 ----------VEKLEESA-VTVMFDkvQFSNksanmdhwqqrfPTHVKDVATVCRQLAEKRmldPSIKGTFHWSGNEQMT 257
Cdd:TIGR01214 154 gggrnfvrtmLRLAGRGEeLRVVDD--QIGS------------PTYAGDLARVIAALLQRL---ARARGVYHLANSGQVS 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11034825   258 KYEMACAI-----ADAFNLPSSHLRPITDS--PVLgAQRPRNAQLDCSKLETLGIGQRTPFRIGIKESL 319
Cdd:TIGR01214 217 WYEFAQAIfeeagADGLLLHPQEVKPISSKeyPRP-ARRPAYSVLDNTKLVKTLGLPLPHWREALRRYL 284
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
74-301 3.33e-24

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 99.98  E-value: 3.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   74 DSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDI 152
Cdd:PRK09987  42 NPEGVAETVRKIRPDVIVNAAAHTAVDKAESEPEFAQLLNATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDiPWQETDA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  153 PAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGevEKLEESAVTVMfdkvQFSNKSANMDHWQQRF--PTHVKDVATV 230
Cdd:PRK09987 122 TAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYA--GKGNNFAKTML----RLAKEREELSVINDQFgaPTGAELLADC 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11034825  231 CRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIAD-----AFNLPSSHLRPI-TDSPVLGAQRPRNAQLDCSKLE 301
Cdd:PRK09987 196 TAHAIRVALNKPEVAGLYHLVASGTTTWHDYAALVFEearkaGITLALNKLNAVpTSAYPTPARRPHNSRLNTEKFQ 272
 
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; ...
30-316 3.10e-132

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: 377.74  E-value: 3.10e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARpkFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRAS--LFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESDPELA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEV 189
Cdd:cd05254  79 YRVNVLAPENLARAAKEVGARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVLNANPRYLILRTSWLYGEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 190 eKLEESAVTVMFDKVQFsNKSANMDHWQQRFPTHVKDVATVCRQLAEKRmldpSIKGTFHWSGNEQMTKYEMACAIADAF 269
Cdd:cd05254 159 -KNGENFVEWMLRLAAE-RKEVNVVHDQIGSPTYAADLADAILELIERN----SLTGIYHLSNSGPISKYEFAKLIADAL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 11034825 270 NLPSSHLRPITDS-PVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIK 316
Cdd:cd05254 233 GLPDVEIKPITSSeYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
31-323 2.45e-119

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: 345.41  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    31 VLVTGATGLLGRAVHKEFQQNNWHAVGCgFRRarpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAAS 110
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGIEVVAL-TRA------ELDLTDPEAVARLLREIKPDVVVNAAAYTAVDKAESEPDLAY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   111 QLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEV 189
Cdd:pfam04321  74 AINALAPANLAEACAAVGAPLIHISTDYVFDGTKPrPYEEDDETNPLNVYGRTKLAGEQAVRAAGPRHLILRTSWVYGEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   190 EKleeSAVTVMFDKVqFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAF 269
Cdd:pfam04321 154 GN---NFVKTMLRLA-AEREELKVVDDQFGRPTWARDLADVLLQLLERLAADPPYWGVYHLSNSGQTSWYEFARAIFDEA 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11034825   270 NLPSSHLRPI-TDSPVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIKESLWPFL 323
Cdd:pfam04321 230 GADPSEVRPItTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLDELL 284
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
30-319 6.79e-88

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 265.07  E-value: 6.79e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRrarpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:COG1091   1 RILVTGANGQLGRALVRLLAERGYEVVALDRS-------ELDITDPEAVAALLEEVRPDVVINAAAYTAVDKAESEPELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGE 188
Cdd:COG1091  74 YAVNATGPANLAEACAELGARLIHISTDYVFDGTKGtPYTEDDPPNPLNVYGRSKLAGEQAVRAAGPRHLILRTSWVYGP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 189 VEKleeSAVTVMFDKVQfSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRmldpsIKGTFHWSGNEQMTKYEMACAIADA 268
Cdd:COG1091 154 HGK---NFVKTMLRLLK-EGEELRVVDDQIGSPTYAADLARAILALLEKD-----LSGIYHLTGSGETSWYEFARAIAEL 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 11034825 269 FNLPsSHLRPI-TDSPVLGAQRPRNAQLDCSKLE-TLGIGQRtPFRIGIKESL 319
Cdd:COG1091 225 AGLD-ALVEPItTAEYPTPAKRPANSVLDNSKLEaTLGIKPP-DWREALAELL 275
rmlD TIGR01214
dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making ...
30-319 1.76e-54

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273505 [Multi-domain]  Cd Length: 287  Bit Score: 179.90  E-value: 1.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    30 RVLVTGATGLLGRAVHKEFQQNNWhaVGCGFRRArpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAA 109
Cdd:TIGR01214   1 RILITGANGQLGRELVQQLSPEGR--VVVALTRS-----QLDLTDPEALERLLRAIRPDAVVNTAAYTDVDGAESDPEKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   110 SQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGE 188
Cdd:TIGR01214  74 FAVNALAPQNLARAAARHGARLVHISTDYVFDGEGKrPYREDDATNPLNVYGQSKLAGEQAVRAAGPNALIVRTSWLYGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   189 ----------VEKLEESA-VTVMFDkvQFSNksanmdhwqqrfPTHVKDVATVCRQLAEKRmldPSIKGTFHWSGNEQMT 257
Cdd:TIGR01214 154 gggrnfvrtmLRLAGRGEeLRVVDD--QIGS------------PTYAGDLARVIAALLQRL---ARARGVYHLANSGQVS 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11034825   258 KYEMACAI-----ADAFNLPSSHLRPITDS--PVLgAQRPRNAQLDCSKLETLGIGQRTPFRIGIKESL 319
Cdd:TIGR01214 217 WYEFAQAIfeeagADGLLLHPQEVKPISSKeyPRP-ARRPAYSVLDNTKLVKTLGLPLPHWREALRRYL 284
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
30-319 5.08e-37

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 134.34  E-value: 5.08e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGcgFRRARPKFEqvNLLDSNAVHHIIHD-----------FQPHVIVHCAAerR 98
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVG--LDRSPPGAA--NLAALPGVEFVRGDlrdpealaaalAGVDAVVHLAA--P 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  99 PDVVENQPDAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVL----EN 173
Cdd:COG0451  75 AGVGEEDPDETLEVNVEGTLNLLEAARAAGVKrFVYASSSSVYGDGEGPIDEDTPLRPVSPYGASKLAAELLARayarRY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 174 NLGAAVLRIPILYGEVEKleeSAVTVMFDKVQFSNKSANMDHWQQRFP-THVKDVATVCRQLAEKrmlDPSIKGTFHWSG 252
Cdd:COG0451 155 GLPVTILRPGNVYGPGDR---GVLPRLIRRALAGEPVPVFGDGDQRRDfIHVDDVARAIVLALEA---PAAPGGVYNVGG 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11034825 253 NEQMTKYEMACAIADAFNLPSSHLRPitdspvLGAQRPRNAQLDCSKLET-LGIGQRTPFRIGIKESL 319
Cdd:COG0451 229 GEPVTLRELAEAIAEALGRPPEIVYP------ARPGDVRPRRADNSKARReLGWRPRTSLEEGLRETV 290
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
31-244 6.26e-25

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: 100.83  E-value: 6.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    31 VLVTGATGLLGRAVHKEFQQNNWHAVG--------CGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVV 102
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGldrltsasNTARLADLRFVEGDLTDRDALEKLLADVRPDAVIHLAAVGGVGAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   103 ENQPDAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVFDGTNPPYREEDI----PAPLNLYGKTKLDGEKAVL----EN 173
Cdd:pfam01370  81 IEDPEDFIEANVLGTLNLLEAARKAGVKrFLFASSSEVYGDGAEIPQEETTltgpLAPNSPYAAAKLAGEWLVLayaaAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   174 NLGAAVLRIPILYGE--VEKLEESAVTVMFDKVQ-------FSNKSANMDHwqqrfpTHVKDVATVCRQLAEKRMLDPSI 244
Cdd:pfam01370 161 GLRAVILRLFNVYGPgdNEGFVSRVIPALIRRILegkpillWGDGTQRRDF------LYVDDVARAILLALEHGAVKGEI 234
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
74-301 3.33e-24

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 99.98  E-value: 3.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   74 DSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP-PYREEDI 152
Cdd:PRK09987  42 NPEGVAETVRKIRPDVIVNAAAHTAVDKAESEPEFAQLLNATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDiPWQETDA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  153 PAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGevEKLEESAVTVMfdkvQFSNKSANMDHWQQRF--PTHVKDVATV 230
Cdd:PRK09987 122 TAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYA--GKGNNFAKTML----RLAKEREELSVINDQFgaPTGAELLADC 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11034825  231 CRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIAD-----AFNLPSSHLRPI-TDSPVLGAQRPRNAQLDCSKLE 301
Cdd:PRK09987 196 TAHAIRVALNKPEVAGLYHLVASGTTTWHDYAALVFEearkaGITLALNKLNAVpTSAYPTPARRPHNSRLNTEKFQ 272
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
30-318 3.22e-21

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: 92.03  E-value: 3.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNwHAVGCGFRRARPKFEQVNLL---DSNAVHHIIHDFQphVIVHCAAerRPDVVENQP 106
Cdd:cd05232   1 KVLVTGANGFIGRALVDKLLSRG-EEVRIAVRNAENAEPSVVLAelpDIDSFTDLFLGVD--AVVHLAA--RVHVMNDQG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 107 DAA----SQLNVDASGNLAKEAA--AVGAFlIYISSDYVF--DGTNPPYREEDIPAPLNLYGKTKLDGEKAVLE----NN 174
Cdd:cd05232  76 ADPlsdyRKVNTELTRRLARAAArqGVKRF-VFLSSVKVNgeGTVGAPFDETDPPAPQDAYGRSKLEAERALLElgasDG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 175 LGAAVLRIPILYGEVEKLEESAVTVMFDKVQ--FSNKSANmdhwqQRFPTHVKDVATVCRQLAEkrmLDPSIKGTFHWSG 252
Cdd:cd05232 155 MEVVILRPPMVYGPGVRGNFARLMRLIDRGLplPPGAVKN-----RRSLVSLDNLVDAIYLCIS---LPKAANGTFLVSD 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11034825 253 NEQMTKYEMACAIADA-------FNLPSSHLRPITDSPVLGAQRPR---NAQLDCSKLE-TLGIGQRTPFRIGIKES 318
Cdd:cd05232 227 GPPVSTAELVDEIRRAlgkptrlLPVPAGLLRFAAKLLGKRAVIQRlfgSLQYDPEKTQnELGWRPPISLEEGLQET 303
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
31-228 4.43e-18

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: 81.19  E-value: 4.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVhkefqqnnwhavgcgFRRARPKFEQVNLLDSNAvhhiihdfqphVIVHCAAERRPDVVENQPDAAS 110
Cdd:cd08946   1 ILVTGGAGFIGSHL---------------VRRLLERGHEVVVIDRLD-----------VVVHLAALVGVPASWDNPDEDF 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 111 QLNVDASGNLAKEAAAVGAF-LIYISSDYVF-DGTNPPYREEDIPAPLNLYGKTKLDGEKAVLE----NNLGAAVLRIPI 184
Cdd:cd08946  55 ETNVVGTLNLLEAARKAGVKrFVYASSASVYgSPEGLPEEEETPPRPLSPYGVSKLAAEHLLRSygesYGLPVVILRLAN 134
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 11034825 185 LYGEVEKLEESAVT-------VMFDKVQFSNKSAnmdhwQQRFPTHVKDVA 228
Cdd:cd08946 135 VYGPGQRPRLDGVVndfirraLEGKPLTVFGGGN-----QTRDFIHVDDVV 180
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
31-189 1.23e-13

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: 68.20  E-value: 1.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNWHAVGCGfRRARPK---------FEQVNLLDSNAVHHIIHDfqPHVIVHCAAERRPDv 101
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLLV-RNTKRLskedqepvaVVEGDLRDLDSLSDAVQG--VDVVIHLAGAPRDT- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 102 venqpDAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVFDGTnppyREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL 180
Cdd:cd05226  77 -----RDFCEVDVEGTRNVLEAAKEAGVKhFIFISSLGAYGDL----HEETEPSPSSPYLAVKAKTEAVLREASLPYTIV 147

                ....*....
gi 11034825 181 RIPILYGEV 189
Cdd:cd05226 148 RPGVIYGDL 156
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
30-263 3.60e-11

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: 63.22  E-value: 3.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCgFRRARP------------KFEQVNLLDSNAVHHIIHDFQphVIVHCAAER 97
Cdd:cd05241   1 SVLVTGGSGFFGERLVKQLLERGGTYVRS-FDIAPPgealsawqhpniEFLKGDITDRNDVEQALSGAD--CVFHTAAIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  98 RPdvvENQPDAASQLNVDASGNLAKEAAAVGA-FLIYISSDYVFDGTNPPYRE-EDIPAP---LNLYGKTKLDGEKAVLE 172
Cdd:cd05241  78 PL---AGPRDLYWEVNVGGTQNVLDACQRCGVqKFVYTSSSSVIFGGQNIHNGdETLPYPpldSDMYAETKAIAEIIVLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 173 NN----LGAAVLRIPILYGE-----VEKLEESAVTVMFdKVQFSNKSANMDhwqqrfPTHVKDVATVCRQLAEKRMLDPS 243
Cdd:cd05241 155 ANgrddLLTCALRPAGIFGPgdqglVPILFEWAEKGLV-KFVFGRGNNLVD------FTYVHNLAHAHILAAAALVKGKT 227
                       250       260
                ....*....|....*....|.
gi 11034825 244 IKGTFHWSGN-EQMTKYEMAC 263
Cdd:cd05241 228 ISGQTYFITDaEPHNMFELLR 248
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
31-319 4.75e-11

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: 62.69  E-value: 4.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNWHAvgcgfrRA--RPKfEQVNLLDSNAVHHIIHDF-----------QPHVIVHCAAer 97
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLAQGYRV------RAlvRSG-SDAVLLDGLPVEVVEGDLtdaaslaaamkGCDRVFHLAA-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  98 rpDVVENQPDAAS--QLNVDASGNLAKEAAAVGA-FLIYISSDYVFDGTNP-------PYREEDIPaplNLYGKTKLDGE 167
Cdd:cd05228  72 --FTSLWAKDRKElyRTNVEGTRNVLDAALEAGVrRVVHTSSIAALGGPPDgridettPWNERPFP---NDYYRSKLLAE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 168 KAVLE---NNLGAAVLRIPILYGeveKLEESAVTVMFDKVqfsnksanmDHWQQRFP---------THVKDVATVCRQLA 235
Cdd:cd05228 147 LEVLEaaaEGLDVVIVNPSAVFG---PGDEGPTSTGLDVL---------DYLNGKLPayppggtsfVDVRDVAEGHIAAM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 236 EK-----RML----DPSIKGTFHW----SGNEQ---MTKYEMACAIAdAFNLPSSHL--RPITDSPVLGAQRPRNAQLDC 297
Cdd:cd05228 215 EKgrrgeRYIlggeNLSFKQLFETlaeiTGVKPprrTIPPWLLKAVA-ALSELKARLtgKPPLLTPRTARVLRRNYLYSS 293
                       330       340
                ....*....|....*....|...
gi 11034825 298 SKLET-LGIGQRtPFRIGIKESL 319
Cdd:cd05228 294 DKARReLGYSPR-PLEEALRDTL 315
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
29-270 2.47e-09

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: 56.92  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRAVHKEFQQNNWHaVGCGFRRARPKFeqvnllDSNAVHHIIHDFqpHVIVHC---AAERRPDVVenq 105
Cdd:cd05265   1 MKILIIGGTRFIGKALVEELLAAGHD-VTVFNRGRTKPD------LPEGVEHIVGDR--NDRDALeelLGGEDFDVV--- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 106 pdaasqlnVDASGNLAKEAAAVGAFL-------IYISSDYVFDGTNP------PYREEDIPAPLNL--YGKTKLDGEKAV 170
Cdd:cd05265  69 --------VDTIAYTPRQVERALDAFkgrvkqyIFISSASVYLKPGRvitestPLREPDAVGLSDPwdYGRGKRAAEDVL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 171 LEN-NLGAAVLRIPILYGEVEKLEESAvtVMFDKVQFSNK----SANMDHWQQrfpTHVKDVATVCRQLAEKrmlDPSIK 245
Cdd:cd05265 141 IEAaAFPYTIVRPPYIYGPGDYTGRLA--YFFDRLARGRPilvpGDGHSLVQF---IHVKDLARALLGAAGN---PKAIG 212
                       250       260
                ....*....|....*....|....*
gi 11034825 246 GTFHWSGNEQMTKYEMACAIADAFN 270
Cdd:cd05265 213 GIFNITGDEAVTWDELLEACAKALG 237
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
29-172 3.42e-09

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 56.75  E-value: 3.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRA-VHKEFQQNNWHaVGC---------GFRRARPKFEQVNLLDSNAVHHII---------------H 83
Cdd:COG3320   1 RTVLLTGATGFLGAHlLRELLRRTDAR-VYClvrasdeaaARERLEALLERYGLWLELDASRVVvvagdltqprlglseA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  84 DFQPH-----VIVHCAAerrpDVVENQP-DAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVFDGTNPP--YREEDIPA 154
Cdd:COG3320  80 EFQELaeevdAIVHLAA----LVNLVAPySELRAVNVLGTREVLRLAATGRLKpFHYVSTIAVAGPADRSgvFEEDDLDE 155
                       170       180
                ....*....|....*....|.
gi 11034825 155 PLNL---YGKTKLDGEKAVLE 172
Cdd:COG3320 156 GQGFangYEQSKWVAEKLVRE 176
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
31-174 5.05e-09

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 56.37  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    31 VLVTGATGLLGRAV----------------HKEFQQNNW-HAVGCGFRRARPKFEQVNLL----DSNAVHHIIHDFQPHV 89
Cdd:pfam02719   1 VLVTGGGGSIGSELcrqilkfnpkkiilfsRDELKLYEIrQELREKFNDPKLRFFIVPVIgdvrDRERLERAMEQYGVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    90 IVHCAAERRPDVVENQPDAASQLNVDASGNLAKEA--AAVGAFlIYISSDYVFDgtnppyreedipaPLNLYGKTKLDGE 167
Cdd:pfam02719  81 VFHAAAYKHVPLVEYNPMEAIKTNVLGTENVADAAieAGVKKF-VLISTDKAVN-------------PTNVMGATKRLAE 146

                  ....*..
gi 11034825   168 KAVLENN 174
Cdd:pfam02719 147 KLFQAAN 153
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
29-317 6.10e-09

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: 56.40  E-value: 6.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRAVHKEFQQN--NWHAVG------CGFRRA--------RPKFEQVNLLDSNAVHHIIHDFQPHVIVH 92
Cdd:cd05246   1 MKILVTGGAGFIGSNFVRYLLNKypDYKIINldkltyAGNLENledvssspRYRFVKGDICDAELVDRLFEEEKIDAVIH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  93 CAAERRPDVVENQPDAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVFD--GTNPPYREEDIPAPLNLYGKTKLDGEKA 169
Cdd:cd05246  81 FAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGVKrFVHISTDEVYGdlLDDGEFTETSPLAPTSPYSASKAAADLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 170 VL---------------ENNLGaavlriPilYGEVEKLEESAVTVMFD--KVQFSNKSANMDHWqqrfpTHVKDVATVCR 232
Cdd:cd05246 161 VRayhrtyglpvvitrcSNNYG------P--YQFPEKLIPLFILNALDgkPLPIYGDGLNVRDW-----LYVEDHARAIE 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 233 QLAEK-RMLDpsikgTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDspvlgaqRP---RNAQLDCSKLE-TLGIGQ 307
Cdd:cd05246 228 LVLEKgRVGE-----IYNIGGGNELTNLELVKLILELLGKDESLITYVKD-------RPghdRRYAIDSSKIRrELGWRP 295
                       330
                ....*....|
gi 11034825 308 RTPFRIGIKE 317
Cdd:cd05246 296 KVSFEEGLRK 305
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
29-188 7.73e-09

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: 56.14  E-value: 7.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRAVHKEFQQNNWHAVGC------GFRRARPKFE-QVNLLDSNAVHHIIHD--------FQPHVIVHC 93
Cdd:cd05258   1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFdnlmrrGSFGNLAWLKaNREDGGVRFVHGDIRNrndledlfEDIDLIIHT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  94 AAErrPDVVENQPDAASQLNVDASGNL-AKEAA---AVGAFLIYISSDYVF--DGTNPPYREED---------------- 151
Cdd:cd05258  81 AAQ--PSVTTSASSPRLDFETNALGTLnVLEAArqhAPNAPFIFTSTNKVYgdLPNYLPLEELEtryelapegwspagis 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 11034825 152 ----IPAPLNLYGKTKLDGEKAVLEN----NLGAAVLRIPILYGE 188
Cdd:cd05258 159 esfpLDFSHSLYGASKGAADQYVQEYgrifGLKTVVFRCGCLTGP 203
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
31-188 1.92e-08

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: 54.68  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQN----------------NWHAVGCGFRRARPKFE-----QVNL-LDSNAVHHIIHDfQPH 88
Cdd:cd05263   1 VFVTGGTGFLGRHLVKRLLENgfkvlvlvrseslgeaHERIEEAGLEADRVRVLegdltQPNLgLSAAASRELAGK-VDH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  89 VIvHCAAERRPdvvENQPDAASQLNVDASGNLAKEAAAVGA-FLIYISSDYVfDGTNPP-YREEDIPAP---LNLYGKTK 163
Cdd:cd05263  80 VI-HCAASYDF---QAPNEDAWRTNIDGTEHVLELAARLDIqRFHYVSTAYV-AGNREGnIRETELNPGqnfKNPYEQSK 154
                       170       180
                ....*....|....*....|....*..
gi 11034825 164 LDGEKAVLE--NNLGAAVLRIPILYGE 188
Cdd:cd05263 155 AEAEQLVRAaaTQIPLTVYRPSIVVGD 181
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
31-230 5.07e-08

ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-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: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 53.46  E-value: 5.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNWHAVGC--GFRRARpKFeqVNLLDSNAVHHI----------IHDFQPHV--IVHCAAe 96
Cdd:cd05248   2 IIVTGGAGFIGSNLVKALNERGITDILVvdNLSNGE-KF--KNLVGLKIADYIdkddfkdwvrKGDENFKIeaIFHQGA- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  97 rRPDVVENQPDAASQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPA---PLNLYGKTKLDGEKAVL-- 171
Cdd:cd05248  78 -CSDTTETDGKYMMDNNYQYTKELLHYCLEKKIRFIYASSAAVYGNGSLGFAEDIETPnlrPLNVYGYSKLLFDQWARrh 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11034825 172 --ENNLGAAVLRIPILYGEVEKLEE---SAVTVMFDKVQ-------FSNKSANMDHWQQRFPTHVKDVATV 230
Cdd:cd05248 157 gkEVLSQVVGLRYFNVYGPREYHKGrmaSVVFHLFNQIKagekvklFKSSDGYADGEQLRDFVYVKDVVKV 227
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
30-167 6.31e-08

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: 53.49  E-value: 6.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQ-----------NNWHAVGCGFRRA-------RPKFEQVNLLDSNAVHHIIHDFQPHVIV 91
Cdd:cd05253   2 KILVTGAAGFIGFHVAKRLLErgdevvgidnlNDYYDVRLKEARLellgksgGFKFVKGDLEDREALRRLFKDHEFDAVI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  92 HCAAerRPDV---VENqPDAASQLNVDASGNLAKEAAAVG-AFLIYISSDYVFDG-TNPPYREED-IPAPLNLYGKTKLD 165
Cdd:cd05253  82 HLAA--QAGVrysLEN-PHAYVDSNIVGFLNLLELCRHFGvKHLVYASSSSVYGLnTKMPFSEDDrVDHPISLYAATKKA 158

                ..
gi 11034825 166 GE 167
Cdd:cd05253 159 NE 160
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
30-261 6.92e-08

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: 53.02  E-value: 6.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNwHAVGCGFRRarpkfeqvnllDSNAVHHI-IHDFQPHVIVHC---------AAERRP 99
Cdd:cd05271   2 VVTVFGATGFIGRYVVNRLAKRG-SQVIVPYRC-----------EAYARRLLvMGDLGQVLFVEFdlrddesirKALEGS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 100 DVV--------ENQPDAASQLNVDASGNLAKEAAAVGAF-LIYISS---DyvfdgTNPPYReedipaplnlYGKTKLDGE 167
Cdd:cd05271  70 DVVinlvgrlyETKNFSFEDVHVEGPERLAKAAKEAGVErLIHISAlgaD-----ANSPSK----------YLRSKAEGE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 168 KAVLENNLGAAVLRIPILYGEveklEESAVTvmfdkvQFSNKSANM------DHWQQRF-PTHVKDVA-TVCRQLaekrm 239
Cdd:cd05271 135 EAVREAFPEATIVRPSVVFGR----EDRFLN------RFAKLLAFLpfppliGGGQTKFqPVYVGDVAeAIARAL----- 199
                       250       260
                ....*....|....*....|...
gi 11034825 240 LDPSIKG-TFHWSGNEQMTKYEM 261
Cdd:cd05271 200 KDPETEGkTYELVGPKVYTLAEL 222
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
30-188 8.31e-08

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: 53.13  E-value: 8.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRA-VHKEFQQNNW--HA--VGCGF-----RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAerrP 99
Cdd:cd09813   1 SCLVVGGSGFLGRHlVEQLLRRGNPtvHVfdIRPTFeldpsSSGRVQFHTGDLTDPQDLEKAFNEKGPNVVFHTAS---P 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 100 DVVENqPDAASQLNVDASGNLAKEAAAVGA-FLIYISS-DYVFDGTNPPYREEDIPAP---LNLYGKTKLDGEKAVL--- 171
Cdd:cd09813  78 DHGSN-DDLYYKVNVQGTRNVIEACRKCGVkKLVYTSSaSVVFNGQDIINGDESLPYPdkhQDAYNETKALAEKLVLkan 156
                       170
                ....*....|....*....
gi 11034825 172 --ENNLGAAVLRIPILYGE 188
Cdd:cd09813 157 dpESGLLTCALRPAGIFGP 175
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
32-164 1.51e-07

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 52.16  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    32 LVTGATG---------LL--GRAVH------KEFQQNNWHAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCA 94
Cdd:pfam16363   1 LITGITGqdgsylaelLLekGYEVHgivrrsSSFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQPDEIYNLA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11034825    95 AERRPDVVENQPDAASQLNVDASGNL---AKEAAAVGAFLIY-ISSDYVFdGT--NPPYREEDIPAPLNLYGKTKL 164
Cdd:pfam16363  81 AQSHVDVSFEQPEYTADTNVLGTLRLleaIRSLGLEKKVRFYqASTSEVY-GKvqEVPQTETTPFYPRSPYAAAKL 155
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
30-193 1.79e-07

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: 51.93  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGcgFRRARPKFEQ----VNLLDSNA-----VHHIIHDFQphVIVHCAAERRPD 100
Cdd:cd05264   1 RVLIVGGNGFIGSHLVDALLEEGPQVRV--FDRSIPPYELplggVDYIKGDYenradLESALVGID--TVIHLASTTNPA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 101 VVENQPDAASQLNVDASGNLAKEAAAVG-AFLIYISSDyvfdGT------NPPYREEDIPAPLNLYGKTKLDGEKAV--- 170
Cdd:cd05264  77 TSNKNPILDIQTNVAPTVQLLEACAAAGiGKIIFASSG----GTvygvpeQLPISESDPTLPISSYGISKLAIEKYLrly 152
                       170       180
                ....*....|....*....|....
gi 11034825 171 -LENNLGAAVLRIPILYGEVEKLE 193
Cdd:cd05264 153 qYLYGLDYTVLRISNPYGPGQRPD 176
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
28-171 1.95e-07

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: 51.47  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  28 NRRVLVTGATGLLGRAVHKE-----------FQQNNW------HAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVI 90
Cdd:cd05237   2 GKTILVTGGAGSIGSELVRQilkfgpkklivFDRDENklhelvRELRSRFPHDKLRFIIGDVRDKERLRRAFKERGPDIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  91 VHCAAERRPDVVENQPDAASQLNVDASGNLAKEAAAVG-AFLIYISSDYVFDgtnppyreedipaPLNLYGKTKLDGEKA 169
Cdd:cd05237  82 FHAAALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIENGvEKFVCISTDKAVN-------------PVNVMGATKRVAEKL 148

                ..
gi 11034825 170 VL 171
Cdd:cd05237 149 LL 150
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
30-181 5.77e-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: 50.23  E-value: 5.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAV-----GCGFRRA-------RPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAer 97
Cdd:cd05247   1 KVLVTGGAGYIGSHTVVELLEAGYDVVvldnlSNGHREAlpriekiRIEFYEGDIRDRAALDKVFAEHKIDAVIHFAA-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  98 RPDVVEN--QPDAASQLNVDASGNLAKEAAAVGAF-LIYISSDYVF-DGTNPPYREEDIPAPLNLYGKTKLDGEKAVLE- 172
Cdd:cd05247  79 LKAVGESvqKPLKYYDNNVVGTLNLLEAMRAHGVKnFVFSSSAAVYgEPETVPITEEAPLNPTNPYGRTKLMVEQILRDl 158
                       170
                ....*....|..
gi 11034825 173 ---NNLGAAVLR 181
Cdd:cd05247 159 akaPGLNYVILR 170
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
30-319 7.46e-07

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. 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: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 50.19  E-value: 7.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVG-----CGFRRARPKFEQVNLL-----DSNAVHHIIHDFQPHVIVHCAAE-RR 98
Cdd:cd08957   2 KVLITGGAGQIGSHLIEHLLERGHQVVVidnfaTGRREHLPDHPNLTVVegsiaDKALVDKLFGDFKPDAVVHTAAAyKD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  99 PDVVENQpdaaSQLNVDASGNLAKEAAAVGA-FLIYISSD--YVFDGTNPPYR-EEDIPAPLNLYGKTKLDGEKAVLENN 174
Cdd:cd08957  82 PDDWYED----TLTNVVGGANVVQAAKKAGVkRLIYFQTAlcYGLKPMQQPIRlDHPRAPPGSSYAISKTAGEYYLELSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 175 LGAAVLRIPILYGevEKLEESAVTVMFDKVQFSNKSANMDhwQQRFPTHVKDVATVC-RQLAEKRMldpsiKGTFHWSGN 253
Cdd:cd08957 158 VDFVTFRLANVTG--PRNVIGPLPTFYQRLKAGKKCFVTD--TRRDFVFVKDLARVVdKALDGIRG-----HGAYHFSSG 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11034825 254 EQMTKYEMACAIADAFNLPSSHLRPITDspvLGAQRPRNAQLDCSKLET-LGIGQRTPFRIGIKESL 319
Cdd:cd08957 229 EDVSIKELFDAVVEALDLPLRPEVEVVE---LGPDDVPSILLDPSRTFQdFGWKEFTPLSETVSAAL 292
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
30-268 1.10e-06

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 48.69  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARPKFE--------QVNLLDSNAVHHIIHDFqpHVIVHCAAERRPDV 101
Cdd:COG0702   1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALaaagvevvQGDLDDPESLAAALAGV--DAVFLLVPSGPGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 102 VENQPDAAsqlnvdasGNLAKEAAAVG-AFLIYISSDYVFDGTNPPyreedipaplnlYGKTKLDGEKAVLENNLGAAVL 180
Cdd:COG0702  79 FAVDVEGA--------RNLADAAKAAGvKRIVYLSALGADRDSPSP------------YLRAKAAVEEALRASGLPYTIL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 181 RIPILYG----EVEKLEESAVTVMFD---KVQfsnksanmdhwqqrfPTHVKDVATVCRQLAEkrmlDPSIKG-TFHWSG 252
Cdd:COG0702 139 RPGWFMGnllgFFERLRERGVLPLPAgdgRVQ---------------PIAVRDVAEAAAAALT----DPGHAGrTYELGG 199
                       250
                ....*....|....*.
gi 11034825 253 NEQMTKYEMACAIADA 268
Cdd:COG0702 200 PEALTYAELAAILSEA 215
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
30-167 1.38e-06

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: 49.30  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNnwhavgcgfrrarPKFEQVNLLD-------SNAVHHIIH--DFQPHVIVHCAAERRPD 100
Cdd:cd05238   2 KVLITGASGFVGQRLAERLLSD-------------VPNERLILIDvvspkapSGAPRVTQIagDLAVPALIEALANGRPD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 101 VV-----------ENQPDAASQLNVDASGNL--AKEAAAVGAFLIYISSDYVFdGTNPPYREED--IPAPLNLYGKTKLD 165
Cdd:cd05238  69 VVfhlaaivsggaEADFDLGYRVNVDGTRNLleALRKNGPKPRFVFTSSLAVY-GLPLPNPVTDhtALDPASSYGAQKAM 147

                ..
gi 11034825 166 GE 167
Cdd:cd05238 148 CE 149
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
29-163 2.33e-06

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 48.54  E-value: 2.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRA-VHKEFQQNNWHAVGC-------GFRR--------ARPKFEQVNLLDSNAVHHIIHDFQPHVIVH 92
Cdd:COG1088   2 MRILVTGGAGFIGSNfVRYLLAKYPGAEVVVldkltyaGNLEnladleddPRYRFVKGDIRDRELVDELFAEHGPDAVVH 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11034825  93 CAAErrPDV---VENqPDAASQLNVDASGNL---AKEAAAVGAFLIYISSDYVFD--GTNPPYREEDIPAPLNLYGKTK 163
Cdd:COG1088  82 FAAE--SHVdrsIDD-PAAFVETNVVGTFNLleaARKYWVEGFRFHHVSTDEVYGslGEDGPFTETTPLDPSSPYSASK 157
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
29-170 3.13e-06

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 48.49  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   29 RRVLVTGATGLLGRAVHKEFQQN---------------NWHAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHC 93
Cdd:PRK10217   2 RKILITGGAGFIGSALVRYIINEtsdavvvvdkltyagNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   94 AAERRPDVVENQPDAASQLNVDASGNLAKEAAAVGAFLI----------YISSDYVF---DGTNPPYREEDIPAPLNLYG 160
Cdd:PRK10217  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTedkksafrfhHISTDEVYgdlHSTDDFFTETTPYAPSSPYS 161
                        170
                 ....*....|
gi 11034825  161 KTKLDGEKAV 170
Cdd:PRK10217 162 ASKASSDHLV 171
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
30-95 3.33e-06

GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, 5-epimerase-4-reductase) acts in the NADP-dependent synthesis of GDP-fucose from GDP-mannose. Two activities have been proposed for the same active site: epimerization and reduction. Proteins in this subgroup are extended SDRs, which have a characteristic active site tetrad and an NADP-binding motif, [AT]GXXGXXG, that is a close match to the archetypical form. 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: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 47.96  E-value: 3.33e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVgcGFRRARpkfeQVNLLDSNAVHHIIHDFQPHVIVHCAA 95
Cdd:cd05239   1 KILVTGHRGLVGSAIVRVLARRGYENV--VFRTSK----ELDLTDQEAVRAFFEKEKPDYVIHLAA 60
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
30-187 1.96e-05

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an 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: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 45.72  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQN-------------NWHAVGCGFRRARP--KFEQVNLLDSNAVHHIIHDF-QPH----- 88
Cdd:cd05235   1 TVLLTGATGFLGAYLLRELLKRknvskiyclvrakDEEAALERLIDNLKeyGLNLWDELELSRIKVVVGDLsKPNlglsd 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  89 -----------VIVHCAAerrpDVVENQPDAAS-QLNVDASGNLAKeAAAVG--AFLIYISSDYVFDGTNPP----YREE 150
Cdd:cd05235  81 ddyqelaeevdVIIHNGA----NVNWVYPYEELkPANVLGTKELLK-LAATGklKPLHFVSTLSVFSAEEYNalddEESD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 11034825 151 DIPAPLNL----YGKTKLDGEKAVLE-NNLG--AAVLRIPILYG 187
Cdd:cd05235 156 DMLESQNGlpngYIQSKWVAEKLLREaANRGlpVAIIRPGNIFG 199
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
31-170 2.83e-05

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended 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. 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: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 45.05  E-value: 2.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNW-HAVGCGFRRARPK------FEQVNLLDSNAVHHiIHDFQPHVIVHCAAerrpdVVE 103
Cdd:cd05240   1 ILVTGAAGGLGRLLARRLAASPRvIGVDGLDRRRPPGsppkveYVRLDIRDPAAADV-FREREADAVVHLAF-----ILD 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11034825 104 NQPDAAS--QLNVDASGNL--AKEAAAVGAfLIYISSDYVFD--GTNPPYREEDIP---APLNLYGKTKLDGEKAV 170
Cdd:cd05240  75 PPRDGAErhRINVDGTQNVldACAAAGVPR-VVVTSSVAVYGahPDNPAPLTEDAPlrgSPEFAYSRDKAEVEQLL 149
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
30-228 3.38e-05

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: 44.90  E-value: 3.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNwHAVGC------GFR------RARPKFEQVNLLDSNAVHHIIHDfqPHVIVHCAAEr 97
Cdd:cd05256   1 RVLVTGGAGFIGSHLVERLLERG-HEVIVldnlstGKKenlpevKPNVKFIEGDIRDDELVEFAFEG--VDYVFHQAAQ- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  98 rPDVVE--NQPDAASQLNVDASGNL--AKEAAAVGAFlIYISSDYVFDGTNP-PYREEDIPAPLNLYGKTKLDGEKAVL- 171
Cdd:cd05256  77 -ASVPRsiEDPIKDHEVNVLGTLNLleAARKAGVKRF-VYASSSSVYGDPPYlPKDEDHPPNPLSPYAVSKYAGELYCQv 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11034825 172 ---ENNLGAAVLRIPILYG--EVEKLEESAVTVMFDKVQFSNKSA--NMDHWQQRFPTHVKDVA 228
Cdd:cd05256 155 farLYGLPTVSLRYFNVYGprQDPNGGYAAVIPIFIERALKGEPPtiYGDGEQTRDFTYVEDVV 218
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
28-151 7.15e-05

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: 43.84  E-value: 7.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  28 NRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGFR-RARPK-FEQVNL-----------LDSNAVHHIIHDFQPHVIVHCA 94
Cdd:cd05252   4 GKRVLVTGHTGFKGSWLSLWLQELGAKVIGYSLDpPTNPNlFELANLdnkisstrgdiRDLNALREAIREYEPEIVFHLA 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11034825  95 AErrPDVVE--NQPDAASQLNVDASGNL---AKEAAAVGAFLIyISSDYVFDGT--NPPYREED 151
Cdd:cd05252  84 AQ--PLVRLsyKDPVETFETNVMGTVNLleaIRETGSVKAVVN-VTSDKCYENKewGWGYREND 144
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
30-181 8.06e-05

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 42.99  E-value: 8.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHaVGCGFRRArpkfEQVNLLDSNAVHHIIHDFQ-----------PHVIVHCAAERR 98
Cdd:cd05243   1 KVLVVGATGKVGRHVVRELLDRGYQ-VRALVRDP----SQAEKLEAAGAEVVVGDLTdaeslaaalegIDAVISAAGSGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  99 pdvvenqPDAASQLNVDASGNL----AKEAAAVGAFlIYISSdyvFDGTNPPYREEDIPAplnlYGKTKLDGEKAVLENN 174
Cdd:cd05243  76 -------KGGPRTEAVDYDGNInlidAAKKAGVKRF-VLVSS---IGADKPSHPLEALGP----YLDAKRKAEDYLRASG 140

                ....*..
gi 11034825 175 LGAAVLR 181
Cdd:cd05243 141 LDYTIVR 147
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
31-295 8.16e-05

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site 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. 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: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 43.46  E-value: 8.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGAtGLLGRAVHKEFQQNNWHAVGCGFRRARPKF---EQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPD 107
Cdd:cd05266   1 VLILGC-GYLGQRLARQLLAQGWQVTGTTRSPEKLAAdrpAGVTPLAADLTQPGLLADVDHLVISLPPPAGSYRGGYDPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 108 AASQLNVDASGNLAKeaaavgaFLIYISSDYVFDGTNPPYREEDIP-APLNLYGKTKLDGEKAVLE-NNLGAAVLRIPIL 185
Cdd:cd05266  80 LRALLDALAQLPAVQ-------RVIYLSSTGVYGDQQGEWVDETSPpNPSTESGRALLEAEQALLAlGSKPTTILRLAGI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 186 YGEveklEESAVTVmfdKVQFSNKSANMDHWQQRFptHVKDVATVCRQLAEKrmldPSIKGTFHWSGNEQMTKYEMACAI 265
Cdd:cd05266 153 YGP----GRHPLRR---LAQGTGRPPAGNAPTNRI--HVDDLVGALAFALQR----PAPGPVYNVVDDLPVTRGEFYQAA 219
                       250       260       270
                ....*....|....*....|....*....|
gi 11034825 266 ADAFNLPSshLRPITDSPVLGAQRPRNAQL 295
Cdd:cd05266 220 AELLGLPP--PPFIPFAFLREGKRVSNDRL 247
PRK05865 PRK05865
sugar epimerase family protein;
30-136 8.53e-05

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 44.26  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRR-----ARPKFEQVNLLDSNAVHHIIHDfqPHVIVHCAAERRPdvven 104
Cdd:PRK05865   2 RIAVTGASGVLGRGLTARLLSQGHEVVGIARHRpdswpSSADFIAADIRDATAVESAMTG--ADVVAHCAWVRGR----- 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 11034825  105 qpdaASQLNVDASGNLAKEAAAVGAFLIYISS 136
Cdd:PRK05865  75 ----NDHINIDGTANVLKAMAETGTGRIVFTS 102
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
30-167 1.21e-04

L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad 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: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 43.07  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGR----AVHKEFQQNN----------WHAVGCGfrrarpKFEQVNLLDSNAVHHIIHDFQPHVIVHCAA 95
Cdd:cd05272   1 RILITGGLGQIGSelakLLRKRYGKDNviasdirkppAHVVLSG------PFEYLDVLDFKSLEEIVVNHKITWIIHLAA 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11034825  96 ERRPdVVENQPDAASQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNP--PYREEDIPAPLNLYGKTKLDGE 167
Cdd:cd05272  75 LLSA-VGEKNPPLAWDVNMNGLHNVLELAREHNLRIFVPSTIGAFGPTTPrnNTPDDTIQRPRTIYGVSKVAAE 147
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
32-188 1.37e-04

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 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. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 43.26  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  32 LVTGATGLLG-----------------RAVHKEFQQNNWHAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFqpHVIVHCA 94
Cdd:cd09811   3 LVTGGGGFLGqhiirlllerkeelkeiRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGV--SVVIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  95 AERRpdvVENQPDAASQLNVDASGNLAKEAAAVGA---FLIYISS----------DYVFDG-TNPPYrEEDIPAPlnlYG 160
Cdd:cd09811  81 AIVD---VFGPPNYEELEEVNVNGTQAVLEACVQNnvkRLVYTSSievagpnfkgRPIFNGvEDTPY-EDTSTPP---YA 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 11034825 161 KTKLDGEKAVLENN---------LGAAVLRIPILYGE 188
Cdd:cd09811 154 SSKLLAENIVLNANgaplkqggyLVTCALRPMYIYGE 190
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
29-168 3.16e-04

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. 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: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 41.90  E-value: 3.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLG--------------------------RAVHKEFQQNNWHAVGCGFRRARPKFE-----------QVN 71
Cdd:cd05236   1 KSVLITGATGFLGkvllekllrscpdigkiyllirgksgQSAEERLRELLKDKLFDRGRNLNPLFEskivpiegdlsEPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  72 LLDSNAVHHIIHDfQPHVIVHCAAERRPDvveNQPDAASQLNVDASGN---LAKEAAAVGAFlIYISSDYVfdGTNPPYR 148
Cdd:cd05236  81 LGLSDEDLQTLIE-EVNIIIHCAATVTFD---ERLDEALSINVLGTLRlleLAKRCKKLKAF-VHVSTAYV--NGDRQLI 153
                       170       180
                ....*....|....*....|
gi 11034825 149 EEDIPAPLNLYGKTKLDGEK 168
Cdd:cd05236 154 EEKVYPPPADPEKLIDILEL 173
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
30-167 3.56e-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: 41.81  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  30 RVLVTGATGLLGRAVHKEFQQNNWHAVGCGfRRARPKFEQVN----------------LLDSNAVHHIIHDFQPHVIVHC 93
Cdd:cd05260   1 RALITGITGQDGSYLAEFLLEKGYEVHGIV-RRSSSFNTDRIdhlyinkdritlhygdLTDSSSLRRAIEKVRPDEIYHL 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11034825  94 AAERRPDVVENQPDAASQLNVDASGNL--AKEAAAVGAFLIYISSDYVF-DGTNPPYREEDIPAPLNLYGKTKLDGE 167
Cdd:cd05260  80 AAQSHVKVSFDDPEYTAEVNAVGTLNLleAIRILGLDARFYQASSSEEYgKVQELPQSETTPFRPRSPYAVSKLYAD 156
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
33-188 6.81e-04

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: 40.67  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    33 VTGATGLLG---------------------RA---------VHKEFQQN-NWHAVgcgFRRARPK-------FEQVNL-L 73
Cdd:pfam07993   1 LTGATGFLGkvllekllrstpdvkkiyllvRAkdgesalerLRQELEKYpLFDAL---LKEALERivpvagdLSEPNLgL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825    74 DSNAVHHIIHDFQphVIVHCAAerrpDVVENQP-DAASQLNVDASGN---LAKEAAAVGAFlIYISSDYV-----FDGTN 144
Cdd:pfam07993  78 SEEDFQELAEEVD--VIIHSAA----TVNFVEPyDDARAVNVLGTREvlrLAKQGKQLKPF-HHVSTAYVngergGLVEE 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 11034825   145 PPYREEDIPAPL------------NLYGKTKLDGEKAVLE---NNLGAAVLRIPILYGE 188
Cdd:pfam07993 151 KPYPEGEDDMLLdedepallgglpNGYTQTKWLAEQLVREaarRGLPVVIYRPSIITGE 209
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
31-108 8.01e-04

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 40.04  E-value: 8.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNWHaVGCGFR---------RARPKFEQVNLLDSNAVHH------IIHDFQP-HVIVHCA 94
Cdd:cd08932   3 ALVTGASRGIGIEIARALARDGYR-VSLGLRnpedlaalsASGGDVEAVPYDARDPEDAralvdaLRDRFGRiDVLVHNA 81
                        90
                ....*....|....
gi 11034825  95 AERRPDVVENQPDA 108
Cdd:cd08932  82 GIGRPTTLREGSDA 95
CC3_like_SDR_a cd05250
CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as ...
29-237 1.19e-03

CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as TIP30) which is implicated in tumor suppression. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine rich NAD(P)-binding motif that resembles the extended SDRs, and have an active site triad of the SDRs (YXXXK and upstream Ser), although the upstream Asn of the usual SDR active site is substituted with Asp. For CC3, the Tyr of the triad is displaced compared to the usual SDRs and the protein is monomeric, both these observations suggest that the usual SDR catalytic activity is not present. NADP appears to serve an important role as a ligand, and may be important in the interaction with other macromolecules. 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: 187560 [Multi-domain]  Cd Length: 214  Bit Score: 39.59  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  29 RRVLVTGATGLLGRAVHKE-FQQNNWHAVGCGFRRARPKFEQvnlldSNAVHHIIHDFQpHVIVHCAAERRPDVV----- 102
Cdd:cd05250   1 KTALVLGATGLVGKHLLRElLKSPYYSKVTAIVRRKLTFPEA-----KEKLVQIVVDFE-RLDEYLEAFQNPDVGfcclg 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825 103 ---ENQPDAASQLNVD-----ASGNLAKEaAAVGAFLIyISSdyvfDGTNPPYReedipaplNLYGKTKLDGEKAVLEnn 174
Cdd:cd05250  75 ttrKKAGSQENFRKVDhdyvlKLAKLAKA-AGVQHFLL-VSS----LGADPKSS--------FLYLKVKGEVERDLQK-- 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11034825 175 LG---AAVLRIPILYGEVEklEESAVTVMFDKVqfsNKSANMDHWQQRFPTHVKDVATVCRQLAEK 237
Cdd:cd05250 139 LGferLTIFRPGLLLGERQ--ESRPGERLAQKL---LRILSPLGFPKYKPIPAETVAKAMVKAALK 199
PRK07577 PRK07577
SDR family oxidoreductase;
27-67 1.61e-03

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 39.32  E-value: 1.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 11034825   27 PNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGfRRARPKF 67
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVIGIA-RSAIDDF 41
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
28-147 1.85e-03

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 39.38  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  28 NRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRA--------------RPKFEQVNLLD----SNAVHHIIHDFQP-H 88
Cdd:COG1028   6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEaleaaaaelraaggRALAVAADVTDeaavEALVAAAVAAFGRlD 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  89 VIVHCAAERRPDVVENQPDAA--SQLNVDASG--NLAKEAAAV-----GAFLIYISSDYVFDGT--NPPY 147
Cdd:COG1028  86 ILVNNAGITPPGPLEELTEEDwdRVLDVNLKGpfLLTRAALPHmrergGGRIVNISSIAGLRGSpgQAAY 155
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
29-76 2.48e-03

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 38.84  E-value: 2.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 11034825  29 RRVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARPKFEQVNLLDSN 76
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSD 49
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
30-156 4.39e-03

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 38.62  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825   30 RVLVTGATGLLGRAVHKEFQQN---------------NWHAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCA 94
Cdd:PRK10084   2 KILVTGGAGFIGSAVVRHIINNtqdsvvnvdkltyagNLESLADVSDSERYVFEHADICDRAELDRIFAQHQPDAVMHLA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11034825   95 AERRPDVVENQPDAASQLNVDASGNLAkEAA----------AVGAFLI-YISSDYVF-DGTNPPYREEDIPAPL 156
Cdd:PRK10084  82 AESHVDRSITGPAAFIETNIVGTYVLL-EAArnywsaldedKKNAFRFhHISTDEVYgDLPHPDEVENSEELPL 154
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
31-125 9.87e-03

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 36.88  E-value: 9.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11034825  31 VLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRA-------------RPKFEQVNLLDSNAVHHIIHDFQ-----PHVIVH 92
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEalaelaaiealggNAVAVQADVSDEEDVEALVEEALeefgrLDILVN 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 11034825  93 CAAERRPDVVENQPDAAS----QLNVDASGNLAKEAA 125
Cdd:cd05233  81 NAGIARPGPLEELTDEDWdrvlDVNLTGVFLLTRAAL 117
 
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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