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Conserved domains on  [gi|1928416995|ref|WP_193939470|]
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MULTISPECIES: GDP-L-fucose synthase [Enterobacter]

Protein Classification

GDP-L-fucose synthase family protein( domain architecture ID 10142801)

GDP-L-fucose synthase family protein such as GDP-L-fucose synthase that catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction; belongs to the extended (e) SDR (short-chain dehydrogenase/reductase) family; 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

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0016491
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
5-313 0e+00

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: 517.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGGIVANNTYPADFIYENM 84
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  85 MIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPT 164
Cdd:cd05239    81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMEldrevwqENTEPmlSHIN 244
Cdd:cd05239   161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLE-------NYDEP--IIVN 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 245 VGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFL 313
Cdd:cd05239   232 VGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRALGWFPFTPLEQGIRETYEWYL 300
 
Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
5-313 0e+00

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: 517.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGGIVANNTYPADFIYENM 84
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  85 MIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPT 164
Cdd:cd05239    81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMEldrevwqENTEPmlSHIN 244
Cdd:cd05239   161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLE-------NYDEP--IIVN 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 245 VGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFL 313
Cdd:cd05239   232 VGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRALGWFPFTPLEQGIRETYEWYL 300
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
7-315 1.73e-156

GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 439.90  E-value: 1.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   7 FVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGGIVANNTYPADFIYENMMI 86
Cdd:PLN02725    1 FVAGHRGLVGSAIVRKLEALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIRENLQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  87 ESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNL 166
Cdd:PLN02725   81 QTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMPTNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 167 YGPHDNFHPSNSHVIPALLRRFHEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMELDREvwqentepmLSHINVG 246
Cdd:PLN02725  161 YGPHDNFHPENSHVIPALIRRFHEAKANGAPEVVVWGSGSPLREFLHVDDLADAVVFLMRRYSG---------AEHVNVG 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 247 TGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFLEN 315
Cdd:PLN02725  232 SGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKFSLKDGLQETYKWYLEN 300
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
6-226 7.35e-70

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: 217.17  E-value: 7.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRGdVDVIVRTRD---------------ELNLLDSRAVQDFFANERIDQVYLAAAkVGGIV 70
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKG-YEVIGLDRLtsasntarladlrfvEGDLTDRDALEKLLADVRPDAVIHLAA-VGGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  71 ANNTYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIaeSELLQGTLEATNEPYAIAKIAGIKLCESY 150
Cdd:pfam01370  79 ASIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQ--EETTLTGPLAPNSPYAAAKLAGEWLVLAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928416995 151 NRQYNRDYRSVMPTNLYGPHDNfHPSNSHVIPALLRRFHEataenAPDVVVWGSGTPMREFLHVDDMAAASIHVME 226
Cdd:pfam01370 157 AAAYGLRAVILRLFNVYGPGDN-EGFVSRVIPALIRRILE-----GKPILLWGDGTQRRDFLYVDDVARAILLALE 226
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-314 1.21e-49

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 167.08  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRD--------------ELNLLDSRAVQDFFanERIDQVYLAAAKVGGI 69
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGhEVVGLDRSPPgaanlaalpgvefvRGDLRDPEALAAAL--AGVDAVVHLAAPAGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  70 VANntyPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPkMAKQPIAESELLQGTleatnEPYAIAKIAGIKLCES 149
Cdd:COG0451    79 EED---PDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYG-DGEGPIDEDTPLRPV-----SPYGASKLAAELLARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 150 YNRQYNRDYRSVMPTNLYGPHDNfhpsnsHVIPALLRRFHEATAenapdVVVWGSGTPMREFLHVDDMAAASIHVMELDR 229
Cdd:COG0451   150 YARRYGLPVTILRPGNVYGPGDR------GVLPRLIRRALAGEP-----VPVFGDGDQRRDFIHVDDVARAIVLALEAPA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 230 EVWQentepmlsHINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDgTPRKLLDVTRLHQ-LGWYHEVSLEQGLAST 308
Cdd:COG0451   219 APGG--------VYNVGGGEPVTLRELAEAIAEALGRPPEIVYPARPGD-VRPRRADNSKARReLGWRPRTSLEEGLRET 289

                  ....*.
gi 1928416995 309 YQWFLE 314
Cdd:COG0451   290 VAWYRA 295
 
Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
5-313 0e+00

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: 517.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGGIVANNTYPADFIYENM 84
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  85 MIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPT 164
Cdd:cd05239    81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMEldrevwqENTEPmlSHIN 244
Cdd:cd05239   161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLE-------NYDEP--IIVN 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 245 VGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFL 313
Cdd:cd05239   232 VGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRALGWFPFTPLEQGIRETYEWYL 300
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
7-315 1.73e-156

GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 439.90  E-value: 1.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   7 FVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGGIVANNTYPADFIYENMMI 86
Cdd:PLN02725    1 FVAGHRGLVGSAIVRKLEALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIRENLQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  87 ESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNL 166
Cdd:PLN02725   81 QTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMPTNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 167 YGPHDNFHPSNSHVIPALLRRFHEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMELDREvwqentepmLSHINVG 246
Cdd:PLN02725  161 YGPHDNFHPENSHVIPALIRRFHEAKANGAPEVVVWGSGSPLREFLHVDDLADAVVFLMRRYSG---------AEHVNVG 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 247 TGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFLEN 315
Cdd:PLN02725  232 SGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKFSLKDGLQETYKWYLEN 300
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
6-226 7.35e-70

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: 217.17  E-value: 7.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRGdVDVIVRTRD---------------ELNLLDSRAVQDFFANERIDQVYLAAAkVGGIV 70
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKG-YEVIGLDRLtsasntarladlrfvEGDLTDRDALEKLLADVRPDAVIHLAA-VGGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  71 ANNTYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIaeSELLQGTLEATNEPYAIAKIAGIKLCESY 150
Cdd:pfam01370  79 ASIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQ--EETTLTGPLAPNSPYAAAKLAGEWLVLAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928416995 151 NRQYNRDYRSVMPTNLYGPHDNfHPSNSHVIPALLRRFHEataenAPDVVVWGSGTPMREFLHVDDMAAASIHVME 226
Cdd:pfam01370 157 AAAYGLRAVILRLFNVYGPGDN-EGFVSRVIPALIRRILE-----GKPILLWGDGTQRRDFLYVDDVARAILLALE 226
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
4-315 2.99e-51

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. 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: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 172.28  E-value: 2.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   4 QRIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTR-----------DELNLLDSRAVQDFF-ANERIDQVYLAAAKVGGIVA 71
Cdd:cd05273     1 QRALVTGAGGFIGSHLAERLKAEGHYVRGADWKspehmtqptddDEFHLVDLREMENCLkATEGVDHVFHLAADMGGMGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  72 NNTYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPkmakQPIAESELLQGTLE------ATNEPYAIAKIAGIK 145
Cdd:cd05273    81 IQSNHAVIMYNNTLINFNMLEAARINGVERFLFASSACVYP----EFKQLETTVVRLREedawpaEPQDAYGWEKLATER 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 146 LCESYNRQYNRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRfhEATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVM 225
Cdd:cd05273   157 LCQHYNEDYGIETRIVRFHNIYGPRGTWDGGREKAPAAMCRK--VATAKDGDRFEIWGDGLQTRSFTYIDDCVEGLRRLM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 226 ELDrevwqeNTEPmlshINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQ-LGWYHEVSLEQG 304
Cdd:cd05273   235 ESD------FGEP----VNLGSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVRGRNSDNTLLKEeLGWEPNTPLEEG 304
                         330
                  ....*....|.
gi 1928416995 305 LASTYQWFLEN 315
Cdd:cd05273   305 LRITYFWIKEQ 315
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-314 1.21e-49

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 167.08  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRD--------------ELNLLDSRAVQDFFanERIDQVYLAAAKVGGI 69
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGhEVVGLDRSPPgaanlaalpgvefvRGDLRDPEALAAAL--AGVDAVVHLAAPAGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  70 VANntyPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPkMAKQPIAESELLQGTleatnEPYAIAKIAGIKLCES 149
Cdd:COG0451    79 EED---PDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYG-DGEGPIDEDTPLRPV-----SPYGASKLAAELLARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 150 YNRQYNRDYRSVMPTNLYGPHDNfhpsnsHVIPALLRRFHEATAenapdVVVWGSGTPMREFLHVDDMAAASIHVMELDR 229
Cdd:COG0451   150 YARRYGLPVTILRPGNVYGPGDR------GVLPRLIRRALAGEP-----VPVFGDGDQRRDFIHVDDVARAIVLALEAPA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 230 EVWQentepmlsHINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDgTPRKLLDVTRLHQ-LGWYHEVSLEQGLAST 308
Cdd:COG0451   219 APGG--------VYNVGGGEPVTLRELAEAIAEALGRPPEIVYPARPGD-VRPRRADNSKARReLGWRPRTSLEEGLRET 289

                  ....*.
gi 1928416995 309 YQWFLE 314
Cdd:COG0451   290 VAWYRA 295
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-231 2.85e-41

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: 142.44  E-value: 2.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRGDvDVIVRTRDelnlldsravqdffaneriDQVYLAAAKVGGIVANNtYPADFIYENMM 85
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLERGH-EVVVIDRL-------------------DVVVHLAALVGVPASWD-NPDEDFETNVV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  86 IESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGTleatnEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTN 165
Cdd:cd08946    60 GTLNLLEAARKAGVKRFVYASSASVYGSPEGLPEEEETPPRPL-----SPYGVSKLAAEHLLRSYGESYGLPVVILRLAN 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928416995 166 LYGPHDnfHPSNSHVIPALLRRfheatAENAPDVVVWGSGTPMREFLHVDDMAAASIHVMELDREV 231
Cdd:cd08946   135 VYGPGQ--RPRLDGVVNDFIRR-----ALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALENPLEG 193
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
5-311 2.03e-28

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: 111.26  E-value: 2.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVR--TRDELNLLDSRAVQDFFAN--------ERIDQV-YLAAAKVGGIVAN 72
Cdd:cd05264     1 RVLIVGGNGFIGSHLVDALLEEGpQVRVFDRsiPPYELPLGGVDYIKGDYENradlesalVGIDTViHLASTTNPATSNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  73 NtyPADFIYENMMIESNIIHAAHLHNVNKLLFLGSS-CIYPKMAKQPIAESELLqgtleATNEPYAIAKIAGIKLCESYN 151
Cdd:cd05264    81 N--PILDIQTNVAPTVQLLEACAAAGIGKIIFASSGgTVYGVPEQLPISESDPT-----LPISSYGISKLAIEKYLRLYQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 152 RQYNRDYRSVMPTNLYGPHDNfHPSNSHVIPALLRRfheaTAENAPdVVVWGSGTPMREFLHVDDMAAASIHVMELDREv 231
Cdd:cd05264   154 YLYGLDYTVLRISNPYGPGQR-PDGKQGVIPIALNK----ILRGEP-IEIWGDGESIRDYIYIDDLVEALMALLRSKGL- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 232 wqENTepmlshINVGTGVDCTIRELAQTIAQVVGYKgrVVFDATKPDGT--PRKLLDVTRLH-QLGWYHEVSLEQGLAST 308
Cdd:cd05264   227 --EEV------FNIGSGIGYSLAELIAEIEKVTGRS--VQVIYTPARTTdvPKIVLDISRARaELGWSPKISLEDGLEKT 296

                  ...
gi 1928416995 309 YQW 311
Cdd:cd05264   297 WQW 299
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
146-312 7.00e-23

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 96.17  E-value: 7.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 146 LCESYNRQYNRDYRSVMPTNLYGPHdnFHPSNSHVIPALLRRfheatAENAPDVVVWGSGTPMREFLHVDDMAAASIHVM 225
Cdd:cd05230   153 LCMAYHRQHGVDVRIARIFNTYGPR--MHPNDGRVVSNFIVQ-----ALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLM 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 226 ELDREvwqenTEPmlshINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLH-QLGWYHEVSLEQG 304
Cdd:cd05230   226 NSDYF-----GGP----VNLGNPEEFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKeLLGWEPKVPLEEG 296

                  ....*...
gi 1928416995 305 LASTYQWF 312
Cdd:cd05230   297 LRRTIEYF 304
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
4-317 1.61e-22

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: 95.31  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   4 QRIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTrDEL-------NLLDSRAVQDF----------------FANERIDQVY 60
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNKYPDYKIINL-DKLtyagnleNLEDVSSSPRYrfvkgdicdaelvdrlFEEEKIDAVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  61 LAAAK--VGGIVANntyPADFIYENMMIESNIIHAAHLHNVNKLLFL------GSSCIYPKMAkqpiaESELLqgtleAT 132
Cdd:cd05246    80 HFAAEshVDRSISD---PEPFIRTNVLGTYTLLEAARKYGVKRFVHIstdevyGDLLDDGEFT-----ETSPL-----AP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 133 NEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNLYGPHDnfHPSNshVIPALLRRfheaTAENAPdVVVWGSGTPMREFL 212
Cdd:cd05246   147 TSPYSASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQ--FPEK--LIPLFILN----ALDGKP-LPIYGDGLNVRDWL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 213 HVDDMAAASIHVME--LDREVWqentepmlshiNVGTGVDCTIRELAQTIAQVVG-YKGRVVFDATKPDGTPRKLLDVTR 289
Cdd:cd05246   218 YVEDHARAIELVLEkgRVGEIY-----------NIGGGNELTNLELVKLILELLGkDESLITYVKDRPGHDRRYAIDSSK 286
                         330       340
                  ....*....|....*....|....*....
gi 1928416995 290 LH-QLGWYHEVSLEQGLASTYQWFLENQH 317
Cdd:cd05246   287 IRrELGWRPKVSFEEGLRKTVRWYLENRW 315
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
5-312 9.68e-22

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: 93.05  E-value: 9.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDvDVIVRtrDEL------NLLDSRAVQDF------------FANERIDQVYLAAAkV 66
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGH-EVIVL--DNLstgkkeNLPEVKPNVKFiegdirddelveFAFEGVDYVFHQAA-Q 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  67 GGIVANNTYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAEsellqgTLEATNE-PYAIAKIAGIK 145
Cdd:cd05256    77 ASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDE------DHPPNPLsPYAVSKYAGEL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 146 LCESYNRQYNRDYRSVMPTNLYGPHDNFHPSNSHVIPallrRFHEATAENAPdVVVWGSGTPMREFLHVDDMAAASIHVM 225
Cdd:cd05256   151 YCQVFARLYGLPTVSLRYFNVYGPRQDPNGGYAAVIP----IFIERALKGEP-PTIYGDGEQTRDFTYVEDVVEANLLAA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 226 E--LDREVwqentepmlshINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQ-LGWYHEVSLE 302
Cdd:cd05256   226 TagAGGEV-----------YNIGTGKRTSVNELAELIREILGKELEPVYAPPRPGDVRHSLADISKAKKlLGWEPKVSFE 294
                         330
                  ....*....|
gi 1928416995 303 QGLASTYQWF 312
Cdd:cd05256   295 EGLRLTVEWF 304
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
10-315 5.04e-20

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 88.51  E-value: 5.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  10 GHRGMVGSAIVRQLE-QRGDVdvivRTRDELNlldsRAVQDffanerIDQVYLAAAKVGGIVANNTyPADFIYENMMIES 88
Cdd:cd05257    36 NSWGLLDNAVHDRFHfISGDV----RDASEVE----YLVKK------CDVVFHLAALIAIPYSYTA-PLSYVETNVFGTL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  89 NIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQgTLEATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNLYG 168
Cdd:cd05257   101 NVLEAACVLYRKRVVHTSTSEVYGTAQDVPIDEDHPLL-YINKPRSPYSASKQGADRLAYSYGRSFGLPVTIIRPFNTYG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 169 PHDnfhpSNSHVIPALLrrfhEATAENAPDVVVwGSGTPMREFLHVDDMAAASIHVMELDREVWQENTEPMLSHINVG-T 247
Cdd:cd05257   180 PRQ----SARAVIPTII----SQRAIGQRLINL-GDGSPTRDFNFVKDTARGFIDILDAIEAVGEIINNGSGEEISIGnP 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 248 GVDCTIRELAQTIAQVvgYKGRVVFDATKPDGTpRKLLDVTRLH-QLGWYHEVSLEQGLASTYQWFLEN 315
Cdd:cd05257   251 AVELIVEELGEMVLIV--YDDHREYRPGYSEVE-RRIPDIRKAKrLLGWEPKYSLRDGLRETIEWFKDQ 316
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
3-314 1.26e-19

GDP-D-mannose-3',5'-epimerase


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 88.33  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   3 KQRIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTR-----------DELNLLDSRAVQDFF-ANERIDQVYLAAAKVGG-- 68
Cdd:PLN02695   21 KLRICITGAGGFIASHIARRLKAEGHYIIASDWKknehmsedmfcHEFHLVDLRVMENCLkVTKGVDHVFNLAADMGGmg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  69 -IVANNTYpadFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKmAKQPIAESELLQGTLEATnEP---YAIAKIAGI 144
Cdd:PLN02695  101 fIQSNHSV---IMYNNTMISFNMLEAARINGVKRFFYASSACIYPE-FKQLETNVSLKESDAWPA-EPqdaYGLEKLATE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 145 KLCESYNRQYNRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAEnapdVVVWGSGTPMREFLHVDDMAAASIHV 224
Cdd:PLN02695  176 ELCKHYTKDFGIECRIGRFHNIYGPFGTWKGGREKAPAAFCRKALTSTDE----FEMWGDGKQTRSFTFIDECVEGVLRL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 225 MELDRevwqenTEPmlshINVGTGVDCTIRELAQTIaqvVGYKGR--VVFDATKPDGTPRKLLDVTR-LHQLGWYHEVSL 301
Cdd:PLN02695  252 TKSDF------REP----VNIGSDEMVSMNEMAEIA---LSFENKklPIKHIPGPEGVRGRNSDNTLiKEKLGWAPTMRL 318
                         330
                  ....*....|...
gi 1928416995 302 EQGLASTYQWFLE 314
Cdd:PLN02695  319 KDGLRITYFWIKE 331
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
5-315 6.15e-18

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: 82.77  E-value: 6.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGD----VDVI-----VRTRD---------------ELNLLDSRAVQDFFANERIDQVY 60
Cdd:cd05253     2 KILVTGAAGFIGFHVAKRLLERGDevvgIDNLndyydVRLKEarlellgksggfkfvKGDLEDREALRRLFKDHEFDAVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  61 LAAAKvGGIVANNTYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESellqgtlEATNEP---YA 137
Cdd:cd05253    82 HLAAQ-AGVRYSLENPHAYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLNTKMPFSED-------DRVDHPislYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 138 IAKIAGIKLCESYNRQYNRDYRSVMPTNLYGPHDnfHPSNShvipalLRRFHEATAENAPdVVVWGSGTPMREFLHVDDM 217
Cdd:cd05253   154 ATKKANELMAHTYSHLYGIPTTGLRFFTVYGPWG--RPDMA------LFLFTKAILEGKP-IDVFNDGNMSRDFTYIDDI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 218 AAASI----HVMELDREVWQENTEPMLSH-----INVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVT 288
Cdd:cd05253   225 VEGVVraldTPAKPNPNWDAEAPDPSTSSapyrvYNIGNNSPVKLMDFIEALEKALGKKAKKNYLPMQKGDVPETYADIS 304
                         330       340
                  ....*....|....*....|....*...
gi 1928416995 289 RLH-QLGWYHEVSLEQGLASTYQWFLEN 315
Cdd:cd05253   305 KLQrLLGYKPKTSLEEGVKRFVEWYKEN 332
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
5-308 1.37e-15

UDP-glucose 4 epimerase, subgroup 2, 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 archaeal and bacterial proteins, and 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: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 75.80  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQL-EQRGDVDVI---------------VRTRDELNLLDSRAVQDFFANERIDQVYLAAAKVGg 68
Cdd:cd05234     1 RILVTGGAGFIGSHLVDRLlEEGNEVVVVdnlssgrreniepefENKAFRFVKRDLLDTADKVAKKDGDTVFHLAANPD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  69 iVANNTYPADFIYE-NMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAEsellqgtlEATNEP---YAIAKIAGI 144
Cdd:cd05234    80 -VRLGATDPDIDLEeNVLATYNVLEAMRANGVKRIVFASSSTVYGEAKVIPTPE--------DYPPLPisvYGASKLAAE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 145 KLCESYNRQYnrDYRSVMP--TNLYGPHdnfhpSNSHVIPALLRRFHeataENAPDVVVWGSGTPMREFLHVDDMAAASI 222
Cdd:cd05234   151 ALISAYAHLF--GFQAWIFrfANIVGPR-----STHGVIYDFINKLK----RNPNELEVLGDGRQRKSYLYVSDCVDAML 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 223 HvmeldreVWQENTEPmLSHINVGTGVDCTIRELAQTIAQVVGYKGRVVFDATK---PDGTPRKLLDVTRLHQLGWYHEV 299
Cdd:cd05234   220 L-------AWEKSTEG-VNIFNLGNDDTISVNEIAEIVIEELGLKPRFKYSGGDrgwKGDVPYMRLDIEKLKALGWKPRY 291

                  ....*....
gi 1928416995 300 SLEQGLAST 308
Cdd:cd05234   292 NSEEAVRKT 300
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
5-311 1.28e-14

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: 73.34  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGdVDVIV----------------RTRDEL---NLLDSRAVQDFFANERIDQV-YLAAA 64
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLEAG-YDVVVldnlsnghrealprieKIRIEFyegDIRDRAALDKVFAEHKIDAViHFAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  65 K-VGGIVANntyPADFiYENMMIES-NIIHAAHLHNVNKLLFLGSSCIY--PKMAkqPIAESELLQgtleATNePYAIAK 140
Cdd:cd05247    80 KaVGESVQK---PLKY-YDNNVVGTlNLLEAMRAHGVKNFVFSSSAAVYgePETV--PITEEAPLN----PTN-PYGRTK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 141 IAGIKLCESYNRQYNRDYRSVMPTNLYGPHDNF-----HPSNSHVIPALLrrfhEATAENAPDVVVWGS------GTPMR 209
Cdd:cd05247   149 LMVEQILRDLAKAPGLNYVILRYFNPAGAHPSGligedPQIPNNLIPYVL----QVALGRREKLAIFGDdyptpdGTCVR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 210 EFLHVDDMAAAsiHVMELDRevwqENTEPMLSHINVGTGVDCTIRELAQTIAQVVGYKGRVVFdatkpdgTPRKLLDVTR 289
Cdd:cd05247   225 DYIHVVDLADA--HVLALEK----LENGGGSEIYNLGTGRGYSVLEVVEAFEKVSGKPIPYEI-------APRRAGDPAS 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 1928416995 290 L--------HQLGWYHEVSLEQGLASTYQW 311
Cdd:cd05247   292 LvadpskarEELGWKPKRDLEDMCEDAWNW 321
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
4-316 2.54e-13

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 69.68  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   4 QRIFVAGHRGMVGSAIVRQL-EQRGDVDVIVrtrDEL----NL--LDSRAVQDFFANERIDQVYLAAAK----------V 66
Cdd:PRK10217    2 RKILITGGAGFIGSALVRYIiNETSDAVVVV---DKLtyagNLmsLAPVAQSERFAFEKVDICDRAELArvftehqpdcV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  67 GGIVANNTY------PADFIYENMMIESNIIHAAH-----LHNVNKLLF----LGSSCIYPKMAKqpiAESELLQGTLEA 131
Cdd:PRK10217   79 MHLAAESHVdrsidgPAAFIETNIVGTYTLLEAARaywnaLTEDKKSAFrfhhISTDEVYGDLHS---TDDFFTETTPYA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 132 TNEPYAIAKIAGIKLCESYNRQYNrdyrsvMPTNLYGPHDNFHPSN--SHVIPALLrrfheATAENAPDVVVWGSGTPMR 209
Cdd:PRK10217  156 PSSPYSASKASSDHLVRAWLRTYG------LPTLITNCSNNYGPYHfpEKLIPLMI-----LNALAGKPLPVYGNGQQIR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 210 EFLHVDDMAAASIHVMELDR--EVWQENTEPMLSHINVGTGVDCTIRELAQTIAQ-VVGYKGRVVFDATKPDGTPRKLLD 286
Cdd:PRK10217  225 DWLYVEDHARALYCVATTGKvgETYNIGGHNERKNLDVVETICELLEELAPNKPQgVAHYRDLITFVADRPGHDLRYAID 304
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1928416995 287 VTRL-HQLGWYHEVSLEQGLASTYQWFLENQ 316
Cdd:PRK10217  305 ASKIaRELGWLPQETFESGMRKTVQWYLANE 335
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-308 2.38e-12

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 66.42  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   7 FVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELN----------------------LLDSRAVQDFFANERIDQVY-LA 62
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGyEVHGIVRRSSSFNtgrlehlyddhlngnlvlhygdLTDSSNLVRLLAEVQPDEIYnLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  63 AAK-VGGIVANntyPADFIyenmmiESNIIHAAHL---------HNVNKLLFLGSSCIYPKMAKQPIAESELLQgtleaT 132
Cdd:pfam16363  81 AQShVDVSFEQ---PEYTA------DTNVLGTLRLleairslglEKKVRFYQASTSEVYGKVQEVPQTETTPFY-----P 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 133 NEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNLYGPH--DNFHPSNshVIPALLRrfheaTAENAPDVVVWGSGTPMRE 210
Cdd:pfam16363 147 RSPYAAAKLYADWIVVNYRESYGLFACNGILFNHESPRrgERFVTRK--ITRGVAR-----IKLGKQEKLYLGNLDAKRD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 211 FLHVDDmaaasiHVMELDREVWQENTEPMlshiNVGTGVDCTIRELAQTIAQVVG----YKGRVVFDATKPDGTPRKLLD 286
Cdd:pfam16363 220 WGHARD------YVEAMWLMLQQDKPDDY----VIATGETHTVREFVEKAFLELGltitWEGKGEIGYFKASGKVHVLID 289
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1928416995 287 --------VTRLH--------QLGWYHEVSLEQGLAST 308
Cdd:pfam16363 290 pryfrpgeVDRLLgdpskakeELGWKPKVSFEELVREM 327
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
5-306 2.17e-11

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 63.23  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGdVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAA--KVGGIVAN-------NTY 75
Cdd:COG1091     1 RILVTGANGQLGRALVRLLAERG-YEVVALDRSELDITDPEAVAALLEEVRPDVVINAAAytAVDKAESEpelayavNAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  76 -PAdfiyenmmiesNIIHAAHLHNVnKLLFLGSSCIYPKMAKQPIAESellqgtlEATNeP---YAIAKIAGiklcESYN 151
Cdd:COG1091    80 gPA-----------NLAEACAELGA-RLIHISTDYVFDGTKGTPYTED-------DPPN-PlnvYGRSKLAG----EQAV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 152 RQYNRDY---RsvmpTN-LYGPH-DNFhpsnshvipalLRRFHEATAENAPDVVV---WGSGTPmreflhVDDMAAASIH 223
Cdd:COG1091   136 RAAGPRHlilR----TSwVYGPHgKNF-----------VKTMLRLLKEGEELRVVddqIGSPTY------AADLARAILA 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 224 VMELDRE-VWqentepmlsHInVGTGVdCTIRELAQTIAQVVGYKGRV--VFDATKPDGTPRKL---LDVTRLHQLGWYH 297
Cdd:COG1091   195 LLEKDLSgIY---------HL-TGSGE-TSWYEFARAIAELAGLDALVepITTAEYPTPAKRPAnsvLDNSKLEATLGIK 263

                  ....*....
gi 1928416995 298 EVSLEQGLA 306
Cdd:COG1091   264 PPDWREALA 272
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
121-315 5.73e-11

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 63.23  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 121 ESELLQGTLEA-----TNePYAIAKIAGIKLCESYNRQYNRDYRSVMPTNLYGPHDnfHPSNshVIPALLrrfheATAEN 195
Cdd:PLN02260  140 DEDADVGNHEAsqllpTN-PYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQ--FPEK--LIPKFI-----LLAMQ 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 196 APDVVVWGSGTPMREFLHVDDMAAASihvmeldrEVWQENTEpmLSHI-NVGTGVDCTIRELAQTIAQVVG--YKGRVVF 272
Cdd:PLN02260  210 GKPLPIHGDGSNVRSYLYCEDVAEAF--------EVVLHKGE--VGHVyNIGTKKERRVIDVAKDICKLFGldPEKSIKF 279
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1928416995 273 DATKPDGTPRKLLDVTRLHQLGWYHEVSLEQGLASTYQWFLEN 315
Cdd:PLN02260  280 VENRPFNDQRYFLDDQKLKKLGWQERTSWEEGLKKTMEWYTSN 322
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
5-305 1.86e-10

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 61.57  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDvDVIVRTrdelNLLDSRA--VQDFFANER---------------IDQVYLAAAKVG 67
Cdd:PLN02166  122 RIVVTGGAGFVGSHLVDKLIGRGD-EVIVID----NFFTGRKenLVHLFGNPRfelirhdvvepilleVDQIYHLACPAS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  68 GiVANNTYPADFIYENMMIESNIIHAAHLHNVnKLLFLGSSCIYPKMAKQPiaESELLQGTLEATNEP--YAIAKIAGIK 145
Cdd:PLN02166  197 P-VHYKYNPVKTIKTNVMGTLNMLGLAKRVGA-RFLLTSTSEVYGDPLEHP--QKETYWGNVNPIGERscYDEGKRTAET 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 146 LCESYNRQYNRDYRSVMPTNLYGPH---DNFHPSNSHVIPALLRRfheataenapDVVVWGSGTPMREFLHVDDMAAASI 222
Cdd:PLN02166  273 LAMDYHRGAGVEVRIARIFNTYGPRmclDDGRVVSNFVAQTIRKQ----------PMTVYGDGKQTRSFQYVSDLVDGLV 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 223 HVMEldrevwQENTEPMlshiNVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRL-HQLGWYHEVSL 301
Cdd:PLN02166  343 ALME------GEHVGPF----NLGNPGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAkELLNWEPKISL 412

                  ....
gi 1928416995 302 EQGL 305
Cdd:PLN02166  413 REGL 416
PLN02206 PLN02206
UDP-glucuronate decarboxylase
5-305 4.39e-10

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 60.38  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIVRtrdelNLLDSRA--VQDFFANER---------------IDQVYLAAAKVG 67
Cdd:PLN02206  121 RVVVTGGAGFVGSHLVDRLMARGDSVIVVD-----NFFTGRKenVMHHFSNPNfelirhdvvepilleVDQIYHLACPAS 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  68 GiVANNTYPADFIYENMMIESNIIHAAHLHNVnKLLFLGSSCIYPKMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLC 147
Cdd:PLN02206  196 P-VHYKFNPVKTIKTNVVGTLNMLGLAKRVGA-RFLLTSTSEVYGDPLQHPQVETYWGNVNPIGVRSCYDEGKRTAETLT 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 148 ESYNRQYNRDYRSVMPTNLYGPH---DNFHPSNSHVIPALLRRfheataenapDVVVWGSGTPMREFLHVDDMAAASIHV 224
Cdd:PLN02206  274 MDYHRGANVEVRIARIFNTYGPRmciDDGRVVSNFVAQALRKE----------PLTVYGDGKQTRSFQFVSDLVEGLMRL 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 225 MEldrevwQENTEPMlshiNVGTGVDCTIRELAQTIAQVVGYKGRVVFDATKPDGTPRKLLDVTRLHQ-LGWYHEVSLEQ 303
Cdd:PLN02206  344 ME------GEHVGPF----NLGNPGEFTMLELAKVVQETIDPNAKIEFRPNTEDDPHKRKPDITKAKElLGWEPKVSLRQ 413

                  ..
gi 1928416995 304 GL 305
Cdd:PLN02206  414 GL 415
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
5-312 5.63e-10

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: 59.44  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIVRT-----RDEL-----------NLLDSRAVQDFFANERIDQVYLAAAkvgg 68
Cdd:cd08957     2 KVLITGGAGQIGSHLIEHLLERGHQVVVIDNfatgrREHLpdhpnltvvegSIADKALVDKLFGDFKPDAVVHTAA---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  69 ivannTY--PADFIYE---NMMIESNIIHAAHLHNVNKLLFLGSSCIY--PKMaKQPIAeselLQGTLEATNEPYAIAKI 141
Cdd:cd08957    78 -----AYkdPDDWYEDtltNVVGGANVVQAAKKAGVKRLIYFQTALCYglKPM-QQPIR----LDHPRAPPGSSYAISKT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 142 AGiklcESYNRQYNRDYRSVMPTNLYGPHDNFHPsnshvIPALLRRFHEATAENAPDVVvwgsgtpmREFLHVDDMAAAS 221
Cdd:cd08957   148 AG----EYYLELSGVDFVTFRLANVTGPRNVIGP-----LPTFYQRLKAGKKCFVTDTR--------RDFVFVKDLARVV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 222 IHVMELDREVwqentepmlSHINVGTGVDCTIRELAQTIAQVVGYKGR--VVFDATKPDGTPRKLLDVTRLHQ-LGWYHE 298
Cdd:cd08957   211 DKALDGIRGH---------GAYHFSSGEDVSIKELFDAVVEALDLPLRpeVEVVELGPDDVPSILLDPSRTFQdFGWKEF 281
                         330
                  ....*....|....
gi 1928416995 299 VSLEQGLASTYQWF 312
Cdd:cd08957   282 TPLSETVSAALAWY 295
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
5-303 2.06e-09

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: 57.61  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELN--------------------LLDSRAVQDFFANERIDQVYLAA 63
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKGyEVHGIVRRSSSFNtdridhlyinkdritlhygdLTDSSSLRRAIEKVRPDEIYHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  64 AK--VGGIVANNTYPADFiyeNMMIESNIIHAAHLHNVN-KLLFLGSSCIYPKMAKQPIAESELLQGTleatnEPYAIAK 140
Cdd:cd05260    81 AQshVKVSFDDPEYTAEV---NAVGTLNLLEAIRILGLDaRFYQASSSEEYGKVQELPQSETTPFRPR-----SPYAVSK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 141 IAGIKLCESYNRQYNRDYRSVMPTNLYGPH--DNFhpsnshVIPALLRRFHEATAENAPDVVVwGSGTPMREFLHVDDMA 218
Cdd:cd05260   153 LYADWITRNYREAYGLFAVNGRLFNHEGPRrgETF------VTRKITRQVARIKAGLQPVLKL-GNLDAKRDWGDARDYV 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 219 AASIHVMELDR-EVWqentepmlshiNVGTGVDCTIRELAQTIAQVVGYKG--RVVFD--ATKPDGTPRKLLDVTRLHQ- 292
Cdd:cd05260   226 EAYWLLLQQGEpDDY-----------VIATGETHSVREFVELAFEESGLTGdiEVEIDprYFRPTEVDLLLGDPSKAREe 294
                         330
                  ....*....|.
gi 1928416995 293 LGWYHEVSLEQ 303
Cdd:cd05260   295 LGWKPEVSFEE 305
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
6-314 1.14e-07

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: 52.31  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRGDVDVIVRtrDEL-------NLLDSR------------AVQDFFANERIDQVYLAAAkv 66
Cdd:cd05248     2 IIVTGGAGFIGSNLVKALNERGITDILVV--DNLsngekfkNLVGLKiadyidkddfkdWVRKGDENFKIEAIFHQGA-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  67 ggiVANNT-YPADFIYENMMIES-NIIHAAHLHNVnKLLFLGSSCIYPKMAKQPIAESELLQgtLEATNePYAIAKiagi 144
Cdd:cd05248    78 ---CSDTTeTDGKYMMDNNYQYTkELLHYCLEKKI-RFIYASSAAVYGNGSLGFAEDIETPN--LRPLN-VYGYSK---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 145 KLCESYNRQYNRDYRSVMPT----NLYGPHDNFHPSNSHVIpalLRRFHEATAENAPDVVVW----GSGTPMREFLHVDD 216
Cdd:cd05248   147 LLFDQWARRHGKEVLSQVVGlryfNVYGPREYHKGRMASVV---FHLFNQIKAGEKVKLFKSsdgyADGEQLRDFVYVKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 217 MAAASIHVMELdrevwqentePMLSHI-NVGTGVDCTIRELAQTIAQVVGYKGRVVFDAtkpdgTPRKLL---------D 286
Cdd:cd05248   224 VVKVNLFFLEN----------PSVSGIfNVGTGRARSFNDLASATFKALGKEVKIEYID-----FPEDLRgkyqsfteaD 288
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1928416995 287 VTRLHQLGW---YHevSLEQGLASTYQWFLE 314
Cdd:cd05248   289 ISKLRAAGYtkeFH--SLEEGVKDYVKNYLA 317
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
5-271 1.94e-07

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: 51.14  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELNLL-----------DSRAVQDFFANERIDQVYlaaakvggivan 72
Cdd:cd05265     2 KILIIGGTRFIGKALVEELLAAGhDVTVFNRGRTKPDLPegvehivgdrnDRDALEELLGGEDFDVVV------------ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  73 ntypaDFI-YENMMIEsnIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQG--TLEATNEPYAIAKIAgiklCES 149
Cdd:cd05265    70 -----DTIaYTPRQVE--RALDAFKGRVKQYIFISSASVYLKPGRVITESTPLREPdaVGLSDPWDYGRGKRA----AED 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 150 YNRQYNRD-YRSVMPTNLYGPHDNFHPSNSHVipallrrfhEATAENAPdVVVWGSGTPMREFLHVDDMAAASIHVMELD 228
Cdd:cd05265   139 VLIEAAAFpYTIVRPPYIYGPGDYTGRLAYFF---------DRLARGRP-ILVPGDGHSLVQFIHVKDLARALLGAAGNP 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1928416995 229 REVwqenTEPmlshINVGTGVDCTIRELAQTIAQVVGYKGRVV 271
Cdd:cd05265   209 KAI----GGI----FNITGDEAVTWDELLEACAKALGKEAEIV 243
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
5-222 2.40e-07

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 51.66  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGDVDVIV------------RTRDELNLL--DSRAVQDFFAN-ERIDQVYLAAAKVGGI 69
Cdd:cd05241     1 SVLVTGGSGFFGERLVKQLLERGGTYVRSfdiappgealsaWQHPNIEFLkgDITDRNDVEQAlSGADCVFHTAAIVPLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  70 vanntYPADFIYE-NMMIESNIIHAAHLHNVNKLLFLGSSCIYpkMAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCE 148
Cdd:cd05241    81 -----GPRDLYWEvNVGGTQNVLDACQRCGVQKFVYTSSSSVI--FGGQNIHNGDETLPYPPLDSDMYAETKAIAEIIVL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928416995 149 SYNRQYNRDYRSVMPTNLYGPHDNFHpsnshvipalLRRFHEAtAENAPDVVVWGSGTPMREFLHVDDMAAASI 222
Cdd:cd05241   154 EANGRDDLLTCALRPAGIFGPGDQGL----------VPILFEW-AEKGLVKFVFGRGNNLVDFTYVHNLAHAHI 216
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
6-312 4.38e-07

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: 50.75  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELNLLDSRAVQ---------DFFAN--ERIDQVYLAAAKVGgivANN 73
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGyRVRALVRSGSDAVLLDGLPVEvvegdltdaASLAAamKGCDRVFHLAAFTS---LWA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  74 TYPADFIYENMMIESNIIHAAHLHNVNKLLFLGSSCIYPKMAKQPIAESELLQGtlEATNEPYAIAKIAGIKLCESYNRQ 153
Cdd:cd05228    78 KDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWNE--RPFPNDYYRSKLLAELEVLEAAAE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 154 yNRDYRSVMPTNLYGPHDnFHPSNSHVIpalLRRFHEATAENAPDvvvwgSGTpmrEFLHVDDMAAASIHVMELDR--EV 231
Cdd:cd05228   156 -GLDVVIVNPSAVFGPGD-EGPTSTGLD---VLDYLNGKLPAYPP-----GGT---SFVDVRDVAEGHIAAMEKGRrgER 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 232 WqentepMLSHINVgtgvdcTIRELAQTIAQVVGYKGRVVfdaTKPDG---------------TPRK-LLDVTRLHQLGW 295
Cdd:cd05228   223 Y------ILGGENL------SFKQLFETLAEITGVKPPRR---TIPPWllkavaalselkarlTGKPpLLTPRTARVLRR 287
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1928416995 296 YHEVS--------------LEQGLASTYQWF 312
Cdd:cd05228   288 NYLYSsdkarrelgysprpLEEALRDTLAWL 318
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
5-294 4.67e-07

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: 50.32  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRGdVDVIVRTRDE-----LNLLDSRAVQDFFANERIDQVYLAAAKVGGIVAnntypADF 79
Cdd:cd05254     1 KILITGATGMLGRALVRLLKERG-YEVIGTGRSRaslfkLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKC-----ESD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  80 IYENMMIES----NIIHAAHLHNVnKLLFLGSSCIYPKmAKQPIAESellqgtlEATNeP---YAIAKIAGiklcESYNR 152
Cdd:cd05254    75 PELAYRVNVlapeNLARAAKEVGA-RLIHISTDYVFDG-KKGPYKEE-------DAPN-PlnvYGKSKLLG----EVAVL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 153 QYNRDYRsVMPTN-LYGPHDNfhpSNSHVIPALlrrfHEATAENAPDVVVWGSGTPmrefLHVDDMAAASIHVMEldrev 231
Cdd:cd05254   141 NANPRYL-ILRTSwLYGELKN---GENFVEWML----RLAAERKEVNVVHDQIGSP----TYAADLADAILELIE----- 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995 232 wqENTEPMLSHInVGTGVdCTIRELAQTIAQVVGYKG---RVVFDATKPDGTPRKL---LDVTRLHQLG 294
Cdd:cd05254   204 --RNSLTGIYHL-SNSGP-ISKYEFAKLIADALGLPDveiKPITSSEYPLPARRPAnssLDCSKLEELG 268
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
5-316 1.86e-06

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 49.02  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQ--------------------LEQRGDVDVIVR-TRDELNLLDSRAVQDFFANERIDQVYLAA 63
Cdd:PRK10084    2 KILVTGGAGFIGSAVVRHiinntqdsvvnvdkltyagnLESLADVSDSERyVFEHADICDRAELDRIFAQHQPDAVMHLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  64 AKvGGIVANNTYPADFIYENMMIESNIIHAAH-----LHNVNKLLF----LGSSCIY-----PKMAKQPIAESELLQGTL 129
Cdd:PRK10084   82 AE-SHVDRSITGPAAFIETNIVGTYVLLEAARnywsaLDEDKKNAFrfhhISTDEVYgdlphPDEVENSEELPLFTETTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 130 EATNEPYAIAKIAGIKLCESYNRQYNrdyrsvMPT------NLYGPhdnFH-PSNshVIPALLrrfheATAENAPDVVVW 202
Cdd:PRK10084  161 YAPSSPYSASKASSDHLVRAWLRTYG------LPTivtncsNNYGP---YHfPEK--LIPLVI-----LNALEGKPLPIY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 203 GSGTPMREFLHVDDMAAASIHVMeldrevwqenTEPMLSHI-NVGTGVDCTIRELAQTIAQV--------VGYKGRVVFD 273
Cdd:PRK10084  225 GKGDQIRDWLYVEDHARALYKVV----------TEGKAGETyNIGGHNEKKNLDVVLTICDLldeivpkaTSYREQITYV 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1928416995 274 ATKPDGTPRKLLDVTRLH-QLGWYHEVSLEQGLASTYQWFLENQ 316
Cdd:PRK10084  295 ADRPGHDRRYAIDASKISrELGWKPQETFESGIRKTVEWYLANT 338
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
6-64 9.24e-06

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: 46.50  E-value: 9.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRGdVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAA 64
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERG-IEVVALTRAELDLTDPEAVARLLREIKPDVVVNAAA 58
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
8-262 3.12e-05

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it 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: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 44.92  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   8 VAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELN----LLDSRAVQD----FFANERIDQVYLAAAKVGGIVANNTYPAD 78
Cdd:cd05193     3 VTGASGFVASHVVEQLLERGyKVRATVRDPSKVKkvnhLLDLDAKPGrlelAVADLTDEQSFDEVIKGCAGVFHVATPVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  79 FI--YENMMIESNI-------IHAAHLHNVNKLLFLGS--SCIYPKMAKQPIAESELLQGTLEATNEP------YAIAKI 141
Cdd:cd05193    83 FSskDPNEVIKPAIggtlnalKAAAAAKSVKRFVLTSSagSVLIPKPNVEGIVLDEKSWNLEEFDSDPkksawvYAASKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 142 AGIKLCESYNRQYNRDYRSVMPTNLYGPH-DNFHPSNSHVIPALLrrfheaTAENA--PDVVVWGSGTpmreFLHVDDMA 218
Cdd:cd05193   163 LAEKAAWKFADENNIDLITVIPTLTIGTIfDSETPSSSGWAMSLI------TGNEGvsPALALIPPGY----YVHVVDIC 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1928416995 219 AASIHVMELDREvwqentepmlSHINVGTGVDCTIRELAQTIAQ 262
Cdd:cd05193   233 LAHIGCLELPIA----------RGRYICTAGNFDWNTLLKTLRK 266
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
4-311 4.58e-05

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: 44.59  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   4 QRIFVAGHRGMVGSAIVRQLEQRG-DVDVI---VRTRDELNLLDSRAVQDFFA-----------------NERIDQVYLA 62
Cdd:cd05258     1 MRVLITGGAGFIGSNLARFFLKQGwEVIGFdnlMRRGSFGNLAWLKANREDGGvrfvhgdirnrndledlFEDIDLIIHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  63 AAKVGgIVANNTYPADFIYENMMIESNIIHAAHLHNVNK-LLFLGSSCIYPKMAKQ-PIAESE------LLQGTLEATNE 134
Cdd:cd05258    81 AAQPS-VTTSASSPRLDFETNALGTLNVLEAARQHAPNApFIFTSTNKVYGDLPNYlPLEELEtryelaPEGWSPAGISE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 135 ---------PYAIAKIAGIKLCESYNRQYNrdyrsvMPT------NLYGPhdNFHPSNSHVIPALlrrFHEATAENAPDV 199
Cdd:cd05258   160 sfpldfshsLYGASKGAADQYVQEYGRIFG------LKTvvfrcgCLTGP--RQFGTEDQGWVAY---FLKCAVTGKPLT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 200 VVWGSGTPMREFLHVDDMAAASIHVME----LDREVWqentepmlshiNVGTGVD--CTIRELAQTIAQVVGYKGRVVFD 273
Cdd:cd05258   229 IFGYGGKQVRDVLHSADLVNLYLRQFQnpdrRKGEVF-----------NIGGGREnsVSLLELIALCEEITGRKMESYKD 297
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1928416995 274 ATKPDGTPRKLLDVTRLHQ-LGWYHEVSLEQGLASTYQW 311
Cdd:cd05258   298 ENRPGDQIWYISDIRKIKEkPGWKPERDPREILAEIYAW 336
PLN02427 PLN02427
UDP-apiose/xylose synthase
73-318 5.75e-05

UDP-apiose/xylose synthase


Pssm-ID: 178047 [Multi-domain]  Cd Length: 386  Bit Score: 44.46  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  73 NTYPADFIYenmmieSNIIHA----AHLHNVNKLLFLGSSC-IYPK-----------MAKQPI------AESELLQGTLE 130
Cdd:PLN02427  103 NTRPLDTIY------SNFIDAlpvvKYCSENNKRLIHFSTCeVYGKtigsflpkdhpLRQDPAfyvlkeDESPCIFGSIE 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 131 ATNEPYAIAKIAGIKLCESYNRQYNRDYRSVMPTNLYGPHDNFHP---SNSHVIPALLRRFHEATAENAPDVVVWGsGTP 207
Cdd:PLN02427  177 KQRWSYACAKQLIERLIYAEGAENGLEFTIVRPFNWIGPRMDFIPgidGPSEGVPRVLACFSNNLLRREPLKLVDG-GQS 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 208 MREFLHVDDmAAASIHVMeldrevwQENTEPMLSHI-NVGT-GVDCTIRELAQTIAQVVG-YKGRVVFDATKP------- 277
Cdd:PLN02427  256 QRTFVYIKD-AIEAVLLM-------IENPARANGHIfNVGNpNNEVTVRQLAEMMTEVYAkVSGEPALEEPTVdvsskef 327
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1928416995 278 -----DGTPRKLLDVTRLH-QLGWYHEVSLEQGLASTyqwfLENQHR 318
Cdd:PLN02427  328 ygegyDDSDKRIPDMTIINkQLGWNPKTSLWDLLEST----LTYQHK 370
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
5-263 6.73e-05

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: 43.30  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELNLLDSRAVQDFFAN-----------ERIDQVYLaaakvggiVAN 72
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGhPVRALVRDPEKAAALAAAGVEVVQGDlddpeslaaalAGVDAVFL--------LVP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  73 NTYPADFIYENMMIEsNIIHAAHLHNVNKLLFLGSsciypkmakqpiaesellQGTLEATNEPYAIAKIAGiklcESYNR 152
Cdd:COG0702    73 SGPGGDFAVDVEGAR-NLADAAKAAGVKRIVYLSA------------------LGADRDSPSPYLRAKAAV----EEALR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 153 QYNRDYRSVMPTNLYGphdNFHPSnshvIPALLRRfheataenapDVVVWGSGTPMREFLHVDDMAAASIHVMELDRevw 232
Cdd:COG0702   130 ASGLPYTILRPGWFMG---NLLGF----FERLRER----------GVLPLPAGDGRVQPIAVRDVAEAAAAALTDPG--- 189
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1928416995 233 QENTEpmlshINVGTGVDCTIRELAQTIAQV 263
Cdd:COG0702   190 HAGRT-----YELGGPEALTYAELAAILSEA 215
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
6-174 6.73e-05

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: 42.77  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   6 IFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELNLLDSRAVQDFFANERIDQVYLAAAK----VGGIVANNTYPADFI 80
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGhEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQgvdvVIHLAGAPRDTRDFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  81 YENMMIESNIIHAAHLHNVNKLLFLGSSCIYPkmakQPIAESEllqgtlEATNEPYAIAKIAgiklCESYNRQYNRDYRS 160
Cdd:cd05226    81 EVDVEGTRNVLEAAKEAGVKHFIFISSLGAYG----DLHEETE------PSPSSPYLAVKAK----TEAVLREASLPYTI 146
                         170
                  ....*....|....
gi 1928416995 161 VMPTNLYGPHDNFH 174
Cdd:cd05226   147 VRPGVIYGDLARAI 160
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
8-312 5.86e-04

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: 41.19  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   8 VAGHRGMVGSAIVRQLEQRGDVDV----IVRTRDELNLLDSRA------------VQDFFANERIDQVYLAAAKVGGIva 71
Cdd:cd09813     4 VVGGSGFLGRHLVEQLLRRGNPTVhvfdIRPTFELDPSSSGRVqfhtgdltdpqdLEKAFNEKGPNVVFHTASPDHGS-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  72 nntypADFIYE--NMMIESNIIHAAHLHNVNKLLFLGS-SCIYpkmAKQPIAESELLQGTLEATNEPYAIAKIAGIKLCE 148
Cdd:cd09813    82 -----NDDLYYkvNVQGTRNVIEACRKCGVKKLVYTSSaSVVF---NGQDIINGDESLPYPDKHQDAYNETKALAEKLVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 149 SYNRQYNRDYR-SVMPTNLYGPHDnfhpsnSHVIPALLrrfheATAENAPDVVVWGSGTPMREFLHVDDMAAASIHVME- 226
Cdd:cd09813   154 KANDPESGLLTcALRPAGIFGPGD------RQLVPGLL-----KAAKNGKTKFQIGDGNNLFDFTYVENVAHAHILAADa 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995 227 LDREVWQE----------NTEP-----MLSHINVGTG-VDCTIRELAQTIAQVVGYKGRVVFDATK--PDGTPRK--LLD 286
Cdd:cd09813   223 LLSSSHAEtvageaffitNDEPiyfwdFARAIWEGLGyERPPSIKLPRPVALYLASLLEWTCKVLGkePTFTPFRvaLLC 302
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1928416995 287 VTRLH-------QLGWYHEVSLEQGLASTYQWF 312
Cdd:cd09813   303 STRYFniekakkRLGYTPVVTLEEGIERTLQWF 335
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
5-161 9.23e-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: 40.37  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQR-GDVDVI---VRTRDE----------LNLLDSRAVQDFFANERIDQVYLAAAKVGGIV 70
Cdd:cd05272     1 RILITGGLGQIGSELAKLLRKRyGKDNVIasdIRKPPAhvvlsgpfeyLDVLDFKSLEEIVVNHKITWIIHLAALLSAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995  71 ANNtyPADFIYENMMIESNIIHAAHLHNVNklLFLGSS--CIYPKMAKQPIAesellQGTLEATNEPYAIAKIAGIKLCE 148
Cdd:cd05272    81 EKN--PPLAWDVNMNGLHNVLELAREHNLR--IFVPSTigAFGPTTPRNNTP-----DDTIQRPRTIYGVSKVAAELLGE 151
                         170
                  ....*....|...
gi 1928416995 149 SYNRQYNRDYRSV 161
Cdd:cd05272   152 YYHHKFGVDFRSL 164
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
5-107 9.28e-04

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 39.84  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDEL------------NLLD----SRAVQDFfaneriDQVYLAAakvg 67
Cdd:COG2910     1 KIAVIGATGRVGSLIVREALARGhEVTALVRNPEKLpdehpgltvvvgDVLDpaavAEALAGA------DAVVSAL---- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1928416995  68 GIVANNTYPadfIYENMMIesNIIHAAHLHNVNKLLFLGS 107
Cdd:COG2910    71 GAGGGNPTT---VLSDGAR--ALIDAMKAAGVKRLIVVGG 105
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
2-105 4.54e-03

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: 37.98  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928416995   2 TKQRIFVAGHRGMVGSAIVRQLEQRGDVDVIVRTRDELNLL-----------------------DSRAVQDFFANERIDQ 58
Cdd:cd05237     1 KGKTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHelvrelrsrfphdklrfiigdvrDKERLRRAFKERGPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1928416995  59 VYLAAA-KvgGIVANNTYPADFIYENMMIESNIIHAAHLHNVNKLLFL 105
Cdd:cd05237    81 VFHAAAlK--HVPSMEDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCI 126
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
5-67 8.33e-03

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: 36.83  E-value: 8.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928416995   5 RIFVAGHRGMVGSAIVRQLEQRG-DVDVIVRTRDELNLLDSRAVQDFFANERIDQVyLAAAKVG 67
Cdd:cd05243     1 KVLVVGATGKVGRHVVRELLDRGyQVRALVRDPSQAEKLEAAGAEVVVGDLTDAES-LAAALEG 63
 
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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