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Conserved domains on  [gi|16129992|ref|NP_416556|]
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GDP-L-fucose synthase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

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

GDP-L-fucose synthase 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

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: 520.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNM 84
Cdd:cd05239   1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  85 MIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPT 164
Cdd:cd05239  81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlentqpmLSHIN 244
Cdd:cd05239 161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLENYDE---------PIIVN 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992 245 VGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFL 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: 520.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNM 84
Cdd:cd05239   1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  85 MIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPT 164
Cdd:cd05239  81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlentqpmLSHIN 244
Cdd:cd05239 161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLENYDE---------PIIVN 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992 245 VGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFL 313
Cdd:cd05239 232 VGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRALGWFPFTPLEQGIRETYEWYL 300
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
7-315 1.60e-157

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


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 442.21  E-value: 1.60e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    7 FIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMI 86
Cdd:PLN02725   1 FVAGHRGLVGSAIVRKLEALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIRENLQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   87 ESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNL 166
Cdd:PLN02725  81 QTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMPTNL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  167 YGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlentqpmLSHINVG 246
Cdd:PLN02725 161 YGPHDNFHPENSHVIPALIRRFHEAKANGAPEVVVWGSGSPLREFLHVDDLADAVVFLMRRYSG---------AEHVNVG 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992  247 TGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLEN 315
Cdd:PLN02725 232 SGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKFSLKDGLQETYKWYLEN 300
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
6-226 1.44e-67

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: 334512 [Multi-domain]  Cd Length: 236  Bit Score: 211.00  E-value: 1.44e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992     6 VFIAGHRGMVGSAIRRQLEQRGdVELVLRTRD-------------ELNLLDSRAVHDFFASERIDQVYLAAAkVGGIVAN 72
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKG-YEVIGLDRLtsasntarpktfvEGDLTDRDALEKLFADVQPDAVIHLAA-VSGVGAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    73 NTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPmAESELLQGTLEPtNEPYAIAKIAGIKLCESYNR 152
Cdd:pfam01370  79 IEDPEDFIEANVLGTLRLLEAARKAGVKRFVFASSSEVYGDGAEIP-QEETTLTGPLAP-NSPYAASKLAGERLVRAYAA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129992   153 QYGRDYRSVMPTNLYGPHdNFHPSNSHVIPALLRRFHEataqnAPDVVVWGSGTPMREFLHVDDMAAASIHVME 226
Cdd:pfam01370 157 AYGLRAVILRLFNVYGPG-RGEGFVSRVIPALIRRILE-----GKPILLWGDGTQRRDFLYVDDVARAILLALE 224
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-318 2.34e-64

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 205.56  E-value: 2.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRG-DVELVLRTRD------------ELNLLDsRAVHDFFASERIDQVYLAAAKVGGIVA 71
Cdd:COG0451   2 RILVTGGAGFIGSHLVERLLAAGhDVRGLDRLRDgldpllsgvefvVLDLTD-RDLVDELAKGVPDAVIHLAAQSSVPDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  72 NNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGS-SCIYPKLAKQPMAESEllqGTLEPTNePYAIAKIAGIKLCESY 150
Cdd:COG0451  81 NASDPAEFLDVNVDGTLNLLEAARAAGVKRFVFASSvSVVYGDPPPLPIDEDL---GPPRPLN-PYGVSKLAAEQLLRAY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 151 NRQYGRDYRSVMPTNLYGPHDNFHpSNSHVIPALLRRFHEataqNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHE 230
Cdd:COG0451 157 ARLYGLPVVILRPFNVYGPGDKPD-LSSGVVSAFIRQLLK----GEPIIVIGGDGSQTRDFVYVDDVADALLLALENPDG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 231 VWlentqpmlshINVGTG-VDCTIRELAQTIAKVVGYKGRVVF---DASKPDGTPRKLLDVTRLHQ-LGWYHEISLEAGL 305
Cdd:COG0451 232 GV----------FNIGSGtAEITVRELAEAVAEAVGSKAPLIVyipLGRRGDLREGKLLDISKARAaLGWEPKVSLEEGL 301
                       330
                ....*....|...
gi 16129992 306 ASTYQWFLENQDR 318
Cdd:COG0451 302 ADTLEWLLKKLEL 314
dTDP_gluc_dehyt TIGR01181
dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and ...
133-317 1.76e-17

dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273489 [Multi-domain]  Cd Length: 317  Bit Score: 81.27  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   133 NEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNshVIPALLRRfheaTAQNAPdVVVWGSGTPMREFL 212
Cdd:TIGR01181 147 SSPYSASKAASDHLVRAYHRTYGLPALITRCSNNYGPYQ--FPEK--LIPLMITN----ALAGKP-LPVYGDGQQVRDWL 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   213 HVDDMAAASIHVMELAH--EVWlentqpmlshiNVGTGVDCTIRELAQTIAKVVG-YKGRVVFDASKPDGTPRKLLDVTR 289
Cdd:TIGR01181 218 YVEDHCRAIYLVLEKGRvgETY-----------NIGGGNERTNLEVVETILELLGkDEDLITHVEDRPGHDRRYAIDASK 286
                         170       180
                  ....*....|....*....|....*....
gi 16129992   290 LH-QLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:TIGR01181 287 IKrELGWAPKYTFEEGLRKTVQWYLDNEW 315
 
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: 520.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNM 84
Cdd:cd05239   1 KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLRDNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  85 MIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPT 164
Cdd:cd05239  81 LINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISVMPT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 165 NLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlentqpmLSHIN 244
Cdd:cd05239 161 NLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYSDDLARAIVFLLENYDE---------PIIVN 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992 245 VGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFL 313
Cdd:cd05239 232 VGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRALGWFPFTPLEQGIRETYEWYL 300
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
7-315 1.60e-157

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


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 442.21  E-value: 1.60e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    7 FIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMI 86
Cdd:PLN02725   1 FVAGHRGLVGSAIVRKLEALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIRENLQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   87 ESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNL 166
Cdd:PLN02725  81 QTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMPTNL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  167 YGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlentqpmLSHINVG 246
Cdd:PLN02725 161 YGPHDNFHPENSHVIPALIRRFHEAKANGAPEVVVWGSGSPLREFLHVDDLADAVVFLMRRYSG---------AEHVNVG 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992  247 TGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLEN 315
Cdd:PLN02725 232 SGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKFSLKDGLQETYKWYLEN 300
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
6-226 1.44e-67

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: 334512 [Multi-domain]  Cd Length: 236  Bit Score: 211.00  E-value: 1.44e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992     6 VFIAGHRGMVGSAIRRQLEQRGdVELVLRTRD-------------ELNLLDSRAVHDFFASERIDQVYLAAAkVGGIVAN 72
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKG-YEVIGLDRLtsasntarpktfvEGDLTDRDALEKLFADVQPDAVIHLAA-VSGVGAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    73 NTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPmAESELLQGTLEPtNEPYAIAKIAGIKLCESYNR 152
Cdd:pfam01370  79 IEDPEDFIEANVLGTLRLLEAARKAGVKRFVFASSSEVYGDGAEIP-QEETTLTGPLAP-NSPYAASKLAGERLVRAYAA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129992   153 QYGRDYRSVMPTNLYGPHdNFHPSNSHVIPALLRRFHEataqnAPDVVVWGSGTPMREFLHVDDMAAASIHVME 226
Cdd:pfam01370 157 AYGLRAVILRLFNVYGPG-RGEGFVSRVIPALIRRILE-----GKPILLWGDGTQRRDFLYVDDVARAILLALE 224
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-318 2.34e-64

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 205.56  E-value: 2.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRG-DVELVLRTRD------------ELNLLDsRAVHDFFASERIDQVYLAAAKVGGIVA 71
Cdd:COG0451   2 RILVTGGAGFIGSHLVERLLAAGhDVRGLDRLRDgldpllsgvefvVLDLTD-RDLVDELAKGVPDAVIHLAAQSSVPDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  72 NNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGS-SCIYPKLAKQPMAESEllqGTLEPTNePYAIAKIAGIKLCESY 150
Cdd:COG0451  81 NASDPAEFLDVNVDGTLNLLEAARAAGVKRFVFASSvSVVYGDPPPLPIDEDL---GPPRPLN-PYGVSKLAAEQLLRAY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 151 NRQYGRDYRSVMPTNLYGPHDNFHpSNSHVIPALLRRFHEataqNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHE 230
Cdd:COG0451 157 ARLYGLPVVILRPFNVYGPGDKPD-LSSGVVSAFIRQLLK----GEPIIVIGGDGSQTRDFVYVDDVADALLLALENPDG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 231 VWlentqpmlshINVGTG-VDCTIRELAQTIAKVVGYKGRVVF---DASKPDGTPRKLLDVTRLHQ-LGWYHEISLEAGL 305
Cdd:COG0451 232 GV----------FNIGSGtAEITVRELAEAVAEAVGSKAPLIVyipLGRRGDLREGKLLDISKARAaLGWEPKVSLEEGL 301
                       330
                ....*....|...
gi 16129992 306 ASTYQWFLENQDR 318
Cdd:COG0451 302 ADTLEWLLKKLEL 314
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
4-320 2.34e-50

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: 169.58  E-value: 2.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   4 QRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTR-----------DELNLLDSRaVHDFF--ASERIDQVYLAAAKVGGIV 70
Cdd:cd05273   1 QRALVTGAGGFIGSHLAERLKAEGHYVRGADWKspehmtqptddDEFHLVDLR-EMENClkATEGVDHVFHLAADMGGMG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  71 ANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTN--EPYAIAKIAGIKLCE 148
Cdd:cd05273  80 YIQSNHAVIMYNNTLINFNMLEAARINGVERFLFASSACVYPEFKQLETTVVRLREEDAWPAEpqDAYGWEKLATERLCQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 149 SYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRfhEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMEla 228
Cdd:cd05273 160 HYNEDYGIETRIVRFHNIYGPRGTWDGGREKAPAAMCRK--VATAKDGDRFEIWGDGLQTRSFTYIDDCVEGLRRLME-- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 229 hevwlENTQpmlSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQ-LGWYHEISLEAGLAS 307
Cdd:cd05273 236 -----SDFG---EPVNLGSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVRGRNSDNTLLKEeLGWEPNTPLEEGLRI 307
                       330
                ....*....|...
gi 16129992 308 TYQWFLENQDRFR 320
Cdd:cd05273 308 TYFWIKEQIEAEK 320
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-231 3.16e-42

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: 144.75  E-value: 3.16e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   6 VFIAGHRGMVGSAIRRQLEQRGDVELVLrtrdelnlldsravhDFFaseriDQVYLAAAKVGGIVANNtYPADFIYQNMM 85
Cdd:cd08946   1 ILVTGGAGFIGSHLVRRLLERGHEVVVI---------------DRL-----DVVVHLAALVGVPASWD-NPDEDFETNVV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  86 IESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLqgtlEPTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTN 165
Cdd:cd08946  60 GTLNLLEAARKAGVKRFVYASSASVYGSPEGLPEEEETPP----RPLS-PYGVSKLAAEHLLRSYGESYGLPVVILRLAN 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129992 166 LYGPHDnfHPSNSHVIPALLRRfheatAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEV 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 3.03e-29

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: 113.18  E-value: 3.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRG----------------DVELVLRTRDELNLLD-SRAVHDffaserIDQV-YLAAAKV 66
Cdd:cd05264   1 RVLIVGGNGFIGSHLVDALLEEGpqvrvfdrsippyelpLGGVDYIKGDYENRADlESALVG------IDTViHLASTTN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  67 GGIVANNtyPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSS-CIYPKLAKQPMAESELLqgtlEPtNEPYAIAKIAGIK 145
Cdd:cd05264  75 PATSNKN--PILDIQTNVAPTVQLLEACAAAGIGKIIFASSGgTVYGVPEQLPISESDPT----LP-ISSYGISKLAIEK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 146 LCESYNRQYGRDYRSVMPTNLYGPHDNfHPSNSHVIPALLRRfheaTAQNAPdVVVWGSGTPMREFLHVDDMAAAsihVM 225
Cdd:cd05264 148 YLRLYQYLYGLDYTVLRISNPYGPGQR-PDGKQGVIPIALNK----ILRGEP-IEIWGDGESIRDYIYIDDLVEA---LM 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 226 ELAHEVWLENTqpmlshINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLH-QLGWYHEISLEAG 304
Cdd:cd05264 219 ALLRSKGLEEV------FNIGSGIGYSLAELIAEIEKVTGRSVQVIYTPARTTDVPKIVLDISRARaELGWSPKISLEDG 292

                ....*..
gi 16129992 305 LASTYQW 311
Cdd:cd05264 293 LEKTWQW 299
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
5-312 3.05e-24

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: 99.99  E-value: 3.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLrtrDEL------NLLDSRAVHDF------------FASERIDQVYLAAAkV 66
Cdd:cd05256   1 RVLVTGGAGFIGSHLVERLLERGHEVIVL---DNLstgkkeNLPEVKPNVKFiegdirddelveFAFEGVDYVFHQAA-Q 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  67 GGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYpklakqpmAESELLqgtlePTNE--------PYAI 138
Cdd:cd05256  77 ASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVY--------GDPPYL-----PKDEdhppnplsPYAV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 139 AKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPallrRFHEATAQNAPdVVVWGSGTPMREFLHVDDMA 218
Cdd:cd05256 144 SKYAGELYCQVFARLYGLPTVSLRYFNVYGPRQDPNGGYAAVIP----IFIERALKGEP-PTIYGDGEQTRDFTYVEDVV 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 219 AASIHVME--LAHEVwlentqpmlshINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQ-LGW 295
Cdd:cd05256 219 EANLLAATagAGGEV-----------YNIGTGKRTSVNELAELIREILGKELEPVYAPPRPGDVRHSLADISKAKKlLGW 287
                       330
                ....*....|....*..
gi 16129992 296 YHEISLEAGLASTYQWF 312
Cdd:cd05256 288 EPKVSFEEGLRLTVEWF 304
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
40-317 1.04e-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: 95.69  E-value: 1.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  40 NLLDSRAVHDFFASERIDQVYLAAAK--VGGIVANntyPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQ 117
Cdd:cd05246  59 DICDAELVDRLFEEEKIDAVIHFAAEshVDRSISD---PEPFIRTNVLGTYTLLEAARKYGVKRFVHISTDEVYGDLLDD 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 118 PMAESELLqgtLEPTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNshVIPALLRRfheatAQNAP 197
Cdd:cd05246 136 GEFTETSP---LAPTS-PYSASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQ--FPEK--LIPLFILN-----ALDGK 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 198 DVVVWGSGTPMREFLHVDDMAAAsIHVmelaheVWLENTqpmLSHI-NVGTGVDCTIRELAQTIAKVVG-YKGRVVFDAS 275
Cdd:cd05246 203 PLPIYGDGLNVRDWLYVEDHARA-IEL------VLEKGR---VGEIyNIGGGNELTNLELVKLILELLGkDESLITYVKD 272
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 16129992 276 KPDGTPRKLLDVTRLH-QLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:cd05246 273 RPGHDRRYAIDSSKIRrELGWRPKVSFEEGLRKTVRWYLENRW 315
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
101-312 1.75e-22

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: 95.01  E-value: 1.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 101 KLLFLGSSCIY--PKLAKQPmaesELLQGTLEPTN--EPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHdnFHPS 176
Cdd:cd05230 108 RVLLASTSEVYgdPEVHPQP----ESYWGNVNPIGprSCYDEGKRVAETLCMAYHRQHGVDVRIARIFNTYGPR--MHPN 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 177 NSHVIPALLRRfheatAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEvwlenTQPmlshINVGTGVDCTIREL 256
Cdd:cd05230 182 DGRVVSNFIVQ-----ALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLMNSDYF-----GGP----VNLGNPEEFTILEL 247
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129992 257 AQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLH-QLGWYHEISLEAGLASTYQWF 312
Cdd:cd05230 248 AELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKeLLGWEPKVPLEEGLRRTIEYF 304
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
10-315 1.45e-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: 90.05  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  10 GHRGMVGSAIRRQLE-QRGDVelvlRTRDELNlldsRAVHDffaserIDQVYLAAAKVGGIVANNTyPADFIYQNMMIES 88
Cdd:cd05257  36 NSWGLLDNAVHDRFHfISGDV----RDASEVE----YLVKK------CDVVFHLAALIAIPYSYTA-PLSYVETNVFGTL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  89 NIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPtNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYG 168
Cdd:cd05257 101 NVLEAACVLYRKRVVHTSTSEVYGTAQDVPIDEDHPLLYINKP-RSPYSASKQGADRLAYSYGRSFGLPVTIIRPFNTYG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 169 PHDnfhpSNSHVIPALLrrfhEATAQNAPDVVVwGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVG-T 247
Cdd:cd05257 180 PRQ----SARAVIPTII----SQRAIGQRLINL-GDGSPTRDFNFVKDTARGFIDILDAIEAVGEIINNGSGEEISIGnP 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992 248 GVDCTIRELAQTIAKVVGyKGRVVFDAsKPDGTpRKLLDVTRLH-QLGWYHEISLEAGLASTYQWFLEN 315
Cdd:cd05257 251 AVELIVEELGEMVLIVYD-DHREYRPG-YSEVE-RRIPDIRKAKrLLGWEPKYSLRDGLRETIEWFKDQ 316
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
2-318 4.20e-19

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


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 86.40  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    2 SKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTR-----------DELNLLDSRAVHDFF-ASERIDQVYLAAAKVGG- 68
Cdd:PLN02695  20 EKLRICITGAGGFIASHIARRLKAEGHYIIASDWKknehmsedmfcHEFHLVDLRVMENCLkVTKGVDHVFNLAADMGGm 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   69 --IVANNTYpadFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKlAKQPMAESELLQGTLEPTnEP---YAIAKIAG 143
Cdd:PLN02695 100 gfIQSNHSV---IMYNNTMISFNMLEAARINGVKRFFYASSACIYPE-FKQLETNVSLKESDAWPA-EPqdaYGLEKLAT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  144 IKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQnapdVVVWGSGTPMREFLHVDDMAAASIH 223
Cdd:PLN02695 175 EELCKHYTKDFGIECRIGRFHNIYGPFGTWKGGREKAPAAFCRKALTSTDE----FEMWGDGKQTRSFTFIDECVEGVLR 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  224 VMElahevwLENTQPmlshINVGTGVDCTIRELAQTIakvVGYKGR--VVFDASKPDGTPRKLLDVTR-LHQLGWYHEIS 300
Cdd:PLN02695 251 LTK------SDFREP----VNIGSDEMVSMNEMAEIA---LSFENKklPIKHIPGPEGVRGRNSDNTLiKEKLGWAPTMR 317
                        330
                 ....*....|....*...
gi 16129992  301 LEAGLASTYQWFLENQDR 318
Cdd:PLN02695 318 LKDGLRITYFWIKEQIEK 335
dTDP_gluc_dehyt TIGR01181
dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and ...
133-317 1.76e-17

dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273489 [Multi-domain]  Cd Length: 317  Bit Score: 81.27  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   133 NEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNshVIPALLRRfheaTAQNAPdVVVWGSGTPMREFL 212
Cdd:TIGR01181 147 SSPYSASKAASDHLVRAYHRTYGLPALITRCSNNYGPYQ--FPEK--LIPLMITN----ALAGKP-LPVYGDGQQVRDWL 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   213 HVDDMAAASIHVMELAH--EVWlentqpmlshiNVGTGVDCTIRELAQTIAKVVG-YKGRVVFDASKPDGTPRKLLDVTR 289
Cdd:TIGR01181 218 YVEDHCRAIYLVLEKGRvgETY-----------NIGGGNERTNLEVVETILELLGkDEDLITHVEDRPGHDRRYAIDASK 286
                         170       180
                  ....*....|....*....|....*....
gi 16129992   290 LH-QLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:TIGR01181 287 IKrELGWAPKYTFEEGLRKTVQWYLDNEW 315
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
4-312 4.89e-17

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224012 [Multi-domain]  Cd Length: 329  Bit Score: 79.91  E-value: 4.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   4 QRVFIAGHRGMVGSAIRRQLEQRG-DV-----------ELVLRTRDEL---NLLDSRAVHDFFASERIDQVYLAAAK--V 66
Cdd:COG1087   1 MKVLVTGGAGYIGSHTVRQLLKTGhEVvvldnlsnghkIALLKLQFKFyegDLLDRALLTAVFEENKIDAVVHFAASisV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  67 GGIVANntyPADFiYQNMMIES-NIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLqgtlEPTNePYAIAKIAGIK 145
Cdd:COG1087  81 GESVQN---PLKY-YDNNVVGTlNLIEAMLQTGVKKFIFSSTAAVYGEPTTSPISETSPL----APIN-PYGRSKLMSEE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 146 LCESYNRQYGRDYRSVMPTNLYGPHD-----NFHPSNSHVIP-----ALLRRfheataqnaPDVVVWGS------GTPMR 209
Cdd:COG1087 152 ILRDAAKANPFKVVILRYFNVAGACPdgtlgQRYPGATLLIPvaaeaALGKR---------DKLFIFGDdydtkdGTCIR 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 210 EFLHVDDMAAAsiHVMELAhevWLENTQpmLSHI-NVGTGVDCTIRELAQTIAKVVGYKGRVVFdaskpdgTPRKLLDVT 288
Cdd:COG1087 223 DYIHVDDLADA--HVLALK---YLKEGG--SNNIfNLGSGNGFSVLEVIEAAKKVTGRDIPVEI-------APRRAGDPA 288
                       330       340       350
                ....*....|....*....|....*....|...
gi 16129992 289 RL--------HQLGWYHE-ISLEAGLASTYQWF 312
Cdd:COG1087 289 ILvadsskarQILGWQPTyDDLEDIIKDAWDWH 321
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
5-295 6.96e-16

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: 76.57  E-value: 6.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGS-AIRRQLEQRGDVELV-----LRTRD----------ELNLLDSRAVHDFFASERIDQVYLAAAKVGg 68
Cdd:cd05234   1 RILVTGGAGFIGShLVDRLLEEGNEVVVVdnlssGRRENiepefenkafRFVKRDLLDTADKVAKKDGDTVFHLAANPD- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  69 iVANNTYPADFIY-QNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAEsellQGTLEPTNEpYAIAKIAGIKLC 147
Cdd:cd05234  80 -VRLGATDPDIDLeENVLATYNVLEAMRANGVKRIVFASSSTVYGEAKVIPTPE----DYPPLPISV-YGASKLAAEALI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 148 ESYNRQYGRD---YRSVmptNLYGPHdnfhpSNSHVIPALLRRFHEataqNAPDVVVWGSGTPMREFLHVDDMAAASIHV 224
Cdd:cd05234 154 SAYAHLFGFQawiFRFA---NIVGPR-----STHGVIYDFINKLKR----NPNELEVLGDGRQRKSYLYVSDCVDAMLLA 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129992 225 melahevwLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASK---PDGTPRKLLDVTRLHQLGW 295
Cdd:cd05234 222 --------WEKSTEGVNIFNLGNDDTISVNEIAEIVIEELGLKPRFKYSGGDrgwKGDVPYMRLDIEKLKALGW 287
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
5-315 8.66e-16

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: 76.61  E-value: 8.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRG-------------DVELVLRTRDEL-----------NLLDSRAVHDFFASERIDQVY 60
Cdd:cd05253   2 KILVTGAAGFIGFHVAKRLLERGdevvgidnlndyyDVRLKEARLELLgksggfkfvkgDLEDREALRRLFKDHEFDAVI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  61 LAAAKvGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESEllqgtlePTNEP---YA 137
Cdd:cd05253  82 HLAAQ-AGVRYSLENPHAYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLNTKMPFSEDD-------RVDHPislYA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 138 IAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNShvipalLRRFHEATAQNAPdVVVWGSGTPMREFLHVDDM 217
Cdd:cd05253 154 ATKKANELMAHTYSHLYGIPTTGLRFFTVYGPWG--RPDMA------LFLFTKAILEGKP-IDVFNDGNMSRDFTYIDDI 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 218 AAASI---HVMELAHEVW-LENTQPMLSH-----INVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVT 288
Cdd:cd05253 225 VEGVVralDTPAKPNPNWdAEAPDPSTSSapyrvYNIGNNSPVKLMDFIEALEKALGKKAKKNYLPMQKGDVPETYADIS 304
                       330       340
                ....*....|....*....|....*...
gi 16129992 289 RLH-QLGWYHEISLEAGLASTYQWFLEN 315
Cdd:cd05253 305 KLQrLLGYKPKTSLEEGVKRFVEWYKEN 332
galE TIGR01179
UDP-glucose-4-epimerase GalE; Alternate name: UDPgalactose 4-epimerase This enzyme ...
5-311 2.97e-15

UDP-glucose-4-epimerase GalE; Alternate name: UDPgalactose 4-epimerase This enzyme interconverts UDP-glucose and UDP-galactose. A set of related proteins, some of which are tentatively identified as UDP-glucose-4-epimerase in Thermotoga maritima, Bacillus halodurans, and several archaea, but deeply branched from this set and lacking experimental evidence, are excluded from this model and described by a separate model. [Energy metabolism, Sugars]


Pssm-ID: 273487 [Multi-domain]  Cd Length: 328  Bit Score: 75.07  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992     5 RVFIAGHRGMVGSAIRRQLEQRGDVELVL---------------RTRD----ELNLLDSRAVHDFFASERIDQV-YLAAA 64
Cdd:TIGR01179   1 KILVTGGAGYIGSHTVRQLLESGHEVVILdnlsngsrealprgeRITPvtfvEGDLRDRELLDRLFEEHKIDAViHFAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    65 K-VGGIVANntyPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQgtlePTNePYAIAKIAG 143
Cdd:TIGR01179  81 IaVGESVQK---PLKYYRNNVVGTLNLLEAMQQAGVKKFIFSSSAAVYGEPSSIPISEDSPLG----PIN-PYGRSKLMS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   144 IKLCESYNR-QYGRDYRSVMPTNLYGPHDNF-----HPSNSHVIPALLrrfhEATAQNAPDVVVWGS------GTPMREF 211
Cdd:TIGR01179 153 EQILRDLQKaDPDWSYVILRYFNVAGAHPSGdigedPPGITHLIPYAC----QVAVGKRDKLTIFGTdyptpdGTCVRDY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   212 LHVDDMAAASIHVMElahevWLENTQPmlSHI-NVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTR- 289
Cdd:TIGR01179 229 IHVMDLADAHLAALE-----YLLNGGG--SHVyNLGYGQGFSVLEVIEAFKKVSGKDFPVELAPRRPGDPASLVADASKi 301
                         330       340
                  ....*....|....*....|...
gi 16129992   290 LHQLGWYHEI-SLEAGLASTYQW 311
Cdd:TIGR01179 302 RRELGWQPKYtDLEEIIKDAWRW 324
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
43-317 8.63e-15

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


Pssm-ID: 224013 [Multi-domain]  Cd Length: 340  Bit Score: 73.80  E-value: 8.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  43 DSRAVHDFFASERIDQVYLAAAKVGgiVANNTY-PADFIYQNMMIESNIIHAAHQNDVN-KLLFLGSSCIYPKLAKQPMA 120
Cdd:COG1088  62 DRELVDRLFKEYQPDAVVHFAAESH--VDRSIDgPAPFIQTNVVGTYTLLEAARKYWGKfRFHHISTDEVYGDLGLDDDA 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 121 ESEllQGTLEPTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNshVIPALLRRfheaTAQNAPdVV 200
Cdd:COG1088 140 FTE--TTPYNPSS-PYSASKAASDLLVRAYVRTYGLPATITRCSNNYGPYQ--FPEK--LIPLMIIN----ALLGKP-LP 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 201 VWGSGTPMREFLHVDDMAAASIHVMELAH--EVWlentqpmlshiNVGTGVDCTIRELAQTIAKVVG-----YKGRVVFD 273
Cdd:COG1088 208 VYGDGLQIRDWLYVEDHCRAIDLVLTKGKigETY-----------NIGGGNERTNLEVVKTICELLGkdkpdYRDLITFV 276
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 16129992 274 ASKPDGTPRKLLDVTRLH-QLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:COG1088 277 EDRPGHDRRYAIDASKIKrELGWRPQETFETGLRKTVDWYLDNEW 321
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
129-317 4.25e-14

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 72.47  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  129 LEPTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfHPSNshVIPALLrrfheATAQNAPDVVVWGSGTPM 208
Cdd:PLN02260 153 LLPTN-PYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQ--FPEK--LIPKFI-----LLAMQGKPLPIHGDGSNV 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  209 REFLHVDDMAAA---SIHVMELAHeVWlentqpmlshiNVGTGVDCTIRELAQTIAKVVG--YKGRVVFDASKPDGTPRK 283
Cdd:PLN02260 223 RSYLYCEDVAEAfevVLHKGEVGH-VY-----------NIGTKKERRVIDVAKDICKLFGldPEKSIKFVENRPFNDQRY 290
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16129992  284 LLDVTRLHQLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:PLN02260 291 FLDDQKLKKLGWQERTSWEEGLKKTMEWYTSNPD 324
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
4-316 1.45e-12

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 67.36  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    4 QRVFIAGHRGMVGSAIRRQL-EQRGDVELVLrtrDEL----NL--LDSRAVHDFFASERIDQVYLAAAK----------V 66
Cdd:PRK10217   2 RKILITGGAGFIGSALVRYIiNETSDAVVVV---DKLtyagNLmsLAPVAQSERFAFEKVDICDRAELArvftehqpdcV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   67 GGIVANNTY------PADFIYQNMMIESNIIHAAHQ-----NDVNKLLF----LGSSCIYPKLAKqpmAESELLQGTLEP 131
Cdd:PRK10217  79 MHLAAESHVdrsidgPAAFIETNIVGTYTLLEAARAywnalTEDKKSAFrfhhISTDEVYGDLHS---TDDFFTETTPYA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  132 TNEPYAIAKIAGIKLCESYNRQYGrdyrsvMPTNLYGPHDNFHPSN--SHVIPALLrrfheATAQNAPDVVVWGSGTPMR 209
Cdd:PRK10217 156 PSSPYSASKASSDHLVRAWLRTYG------LPTLITNCSNNYGPYHfpEKLIPLMI-----LNALAGKPLPVYGNGQQIR 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  210 EFLHVDDMAAASIHVMELAH--EVWLENTQPMLSHINVGTGVDCTIRELA-QTIAKVVGYKGRVVFDASKPDGTPRKLLD 286
Cdd:PRK10217 225 DWLYVEDHARALYCVATTGKvgETYNIGGHNERKNLDVVETICELLEELApNKPQGVAHYRDLITFVADRPGHDLRYAID 304
                        330       340       350
                 ....*....|....*....|....*....|.
gi 16129992  287 VTRL-HQLGWYHEISLEAGLASTYQWFLENQ 316
Cdd:PRK10217 305 ASKIaRELGWLPQETFESGMRKTVQWYLANE 335
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
38-311 5.57e-12

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: 65.25  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  38 ELNLLDSRAVHDFFASERIDQV-YLAAAK-VGGIVANntyPADFiYQNMMIES-NIIHAAHQNDVNKLLFLGSSCIYPKL 114
Cdd:cd05247  52 EGDIRDRAALDKVFAEHKIDAViHFAALKaVGESVQK---PLKY-YDNNVVGTlNLLEAMRAHGVKNFVFSSSAAVYGEP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 115 AKQPMAESELLQgtlePTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNF-----HPSNSHVIPALLrrfh 189
Cdd:cd05247 128 ETVPITEEAPLN----PTN-PYGRTKLMVEQILRDLAKAPGLNYVILRYFNPAGAHPSGligedPQIPNNLIPYVL---- 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 190 EATAQNAPDVVVWGS------GTPMREFLHVDDMAAAsiHVmeLAHEvWLENtQPMLSHINVGTGVDCTIRELAQTIAKV 263
Cdd:cd05247 199 QVALGRREKLAIFGDdyptpdGTCVRDYIHVVDLADA--HV--LALE-KLEN-GGGSEIYNLGTGRGYSVLEVVEAFEKV 272
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16129992 264 VGYKGRVVFdASKPDGTPRKLL-DVTRLHQ-LGWYHEISLEAGLASTYQW 311
Cdd:cd05247 273 SGKPIPYEI-APRRAGDPASLVaDPSKAREeLGWKPKRDLEDMCEDAWNW 321
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
5-312 7.82e-11

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: 61.75  E-value: 7.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRT-----RDEL-----------NLLDSRAVHDFFASERIDQVYLAAAkvgg 68
Cdd:cd08957   2 KVLITGGAGQIGSHLIEHLLERGHQVVVIDNfatgrREHLpdhpnltvvegSIADKALVDKLFGDFKPDAVVHTAA---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  69 ivannTY--PADFI---YQNMMIESNIIHAAHQNDVNKLLFLGSSCIYpklAKQPMAESELLQGTLEPTNEPYAIAKIAG 143
Cdd:cd08957  78 -----AYkdPDDWYedtLTNVVGGANVVQAAKKAGVKRLIYFQTALCY---GLKPMQQPIRLDHPRAPPGSSYAISKTAG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 144 iklcESYNRQYGRDYRSVMPTNLYGPHDNFHPsnshvIPALLRRFHEATAQNAPDVVvwgsgtpmREFLHVDDMAAASIH 223
Cdd:cd08957 150 ----EYYLELSGVDFVTFRLANVTGPRNVIGP-----LPTFYQRLKAGKKCFVTDTR--------RDFVFVKDLARVVDK 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 224 VM--ELAHEVWlentqpmlshiNVGTGVDCTIRELAQTIAKVVGYKGR--VVFDASKPDGTPRKLLDVTRLHQ-LGWYHE 298
Cdd:cd08957 213 ALdgIRGHGAY-----------HFSSGEDVSIKELFDAVVEALDLPLRpeVEVVELGPDDVPSILLDPSRTFQdFGWKEF 281
                       330
                ....*....|....
gi 16129992 299 ISLEAGLASTYQWF 312
Cdd:cd08957 282 TPLSETVSAALAWY 295
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
5-321 1.44e-10

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 61.57  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRtrdelNLLDSRA---VHdFFASER---------------IDQVYLAAAKV 66
Cdd:PLN02166 122 RIVVTGGAGFVGSHLVDKLIGRGDEVIVID-----NFFTGRKenlVH-LFGNPRfelirhdvvepilleVDQIYHLACPA 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   67 GGiVANNTYPADFIYQNMMIESNIIHAAHQNDVnKLLFLGSSCIYPKLAKQPmaESELLQGTLEPTNEP--YAIAKIAGI 144
Cdd:PLN02166 196 SP-VHYKYNPVKTIKTNVMGTLNMLGLAKRVGA-RFLLTSTSEVYGDPLEHP--QKETYWGNVNPIGERscYDEGKRTAE 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  145 KLCESYNRQYGRDYRSVMPTNLYGPH----DNFHPSNshvipallrrFHEATAQNAPdVVVWGSGTPMREFLHVDDMAAA 220
Cdd:PLN02166 272 TLAMDYHRGAGVEVRIARIFNTYGPRmcldDGRVVSN----------FVAQTIRKQP-MTVYGDGKQTRSFQYVSDLVDG 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  221 SIHVMELAHevwlentqpmLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRL-HQLGWYHEI 299
Cdd:PLN02166 341 LVALMEGEH----------VGPFNLGNPGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAkELLNWEPKI 410
                        330       340
                 ....*....|....*....|....*
gi 16129992  300 SLEAGL---ASTYQWFLENQDRFRG 321
Cdd:PLN02166 411 SLREGLplmVSDFRNRILNEDEGKG 435
EDH_00030 TIGR04180
NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family; This clade within the NAD ...
56-295 1.82e-10

NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family; This clade within the NAD dependent epimerase/dehydratase superfamily (pfam01370) is characterized by inclusion of its members within a cassette of seven distinctive enzymes. These include four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD), an aminotransferase and a nucleotidyltransferase in addition to the epimerase/dehydratase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analagous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar. Although this cassette is widely distributed in bacteria, the family nomenclature arises from the instance in Leptospira interrogans serovar Lai, str. 56601, where it appears as the 30th gene in the 91-gene lipopolysaccharide biosynthesis cluster.


Pssm-ID: 275033 [Multi-domain]  Cd Length: 297  Bit Score: 60.39  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    56 IDQVYLAAAKVGgIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGtleptNEP 135
Cdd:TIGR04180  71 CDVVFHLAALIA-IPYSYIAPDSYVDTNVTGTLNVLQAARDLGVEKVVHTSTSEVYGTAQYVPIDEKHPLQG-----QSP 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   136 YAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDnfhpSNSHVIPALLRRFHEATAQnapdvVVWGSGTPMREFLHVD 215
Cdd:TIGR04180 145 YSASKIGADQLALSFYRSFNTPVTIIRPFNTYGPRQ----SARAVIPTIITQIASGKRR-----IKLGSLSPTRDFNYVT 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   216 DMAAASIHVMELAHEVWLEntqpmlshINVGTGVDCTIRELAQTIAKVVGYKGRVVFDAS--KPDGTP--RKLLDVTRLH 291
Cdd:TIGR04180 216 DTVRGFIAIAESDKTVGEV--------INIGSNFEISIGDTVKLIAEIMGSEVEIETDEErlRPEKSEveRLWCDNSKIK 287

                  ....*
gi 16129992   292 QL-GW 295
Cdd:TIGR04180 288 ELtGW 292
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-308 6.87e-10

GDP-mannose 4,6 dehydratase;


Pssm-ID: 339714 [Multi-domain]  Cd Length: 332  Bit Score: 59.09  E-value: 6.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992     7 FIAGHRGMVGSAIRRQLEQRG-----------------------DVELVLRTRDEL---NLLDSRAVHDFFASERIDQVY 60
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGyevhgiirrsssfntgriehlydDPDAHLNPNLVLhygDLTDSSNLIRLLAEVQPDEIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    61 -LAAAK-VGGIVANntyPADFIyqnmmiESNIIHAAH-------QNDVNKLLFL--GSSCIYPKLAKQPMAESellqGTL 129
Cdd:pfam16363  81 nLAAQShVGVSFEQ---PEYTA------DTNVLGTLRlleairsLGLEKKIRFYqaSTSEVYGKVQEVPQTET----TPF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   130 EPTNePYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRrfheaTAQNAPDVVVWGSGTPMR 209
Cdd:pfam16363 148 YPRS-PYAAAKLYADWIVVNYRESYGLFACNGILFNHESPRRGERFVTRKITRGVAR-----IKLGLQEVLYLGNLDAKR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   210 EFLHVDDMAAAsihvmelaheVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVG----YKGRVVFDASKPDGTPRKLL 285
Cdd:pfam16363 222 DWGHARDYVEA----------MWLMLQQDEPDDYVIATGETHTVREFVEKAFLHLGititWEGKGEDEVGRFKATGKVHV 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 16129992   286 ----------DVTRLH--------QLGWYHEISLEAGLAST 308
Cdd:pfam16363 292 lidpryfrpgEVDRLLgdpskakeELGWKPKVSFEELVREM 332
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
5-302 5.96e-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: 56.07  E-value: 5.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGS---------------AIRRQLEQRGDVELVLRTRD------ELNLLDSRAVHDFFASERIDQVYLAA 63
Cdd:cd05260   1 RALITGITGQDGSylaefllekgyevhgIVRRSSSFNTDRIDHLYINKdritlhYGDLTDSSSLRRAIEKVRPDEIYHLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  64 AK--VGGIVANNTYPADFiyqNMMIESNIIHAAHQNDVN-KLLFLGSSCIYPKLAKQPMAESEllqgTLEPTNePYAIAK 140
Cdd:cd05260  81 AQshVKVSFDDPEYTAEV---NAVGTLNLLEAIRILGLDaRFYQASSSEEYGKVQELPQSETT----PFRPRS-PYAVSK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 141 IAGIKLCESYNRQYGRDYRSVMPTNLYGPH--DNFhpsnshVIPALLRRFHEATAQNAPDVVVwGSGTPMREFLHVDDMA 218
Cdd:cd05260 153 LYADWITRNYREAYGLFAVNGRLFNHEGPRrgETF------VTRKITRQVARIKAGLQPVLKL-GNLDAKRDWGDARDYV 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 219 AAsihvmelaheVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKG--RVVFDAS--KPDGTPRKLLDVTRLHQ-L 293
Cdd:cd05260 226 EA----------YWLLLQQGEPDDYVIATGETHSVREFVELAFEESGLTGdiEVEIDPRyfRPTEVDLLLGDPSKAREeL 295

                ....*....
gi 16129992 294 GWYHEISLE 302
Cdd:cd05260 296 GWKPEVSFE 304
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
5-310 1.80e-08

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


Pssm-ID: 224016 [Multi-domain]  Cd Length: 281  Bit Score: 54.60  E-value: 1.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVlrTRDELNLLDSRAVHDFFASERIDQVYLAAA--KVGGIVAN--NTYPADFI 80
Cdd:COG1091   2 KILITGANGQLGTELRRALPGEFEVIAT--DRAELDITDPDAVLEVIRETRPDVVINAAAytAVDKAESEpeLAFAVNAT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  81 Y-QNMMIESNIIHAahqndvnKLLFLGSSCIYPKLAKQPMAESEllqgTLEPTNEpYAIAKIAGiklcESYNRQYGRDYR 159
Cdd:COG1091  80 GaENLARAAAEVGA-------RLVHISTDYVFDGEKGGPYKETD----TPNPLNV-YGRSKLAG----EEAVRAAGPRHL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 160 SVMPTNLYGPH-DNFhpsnshVIPA--LLRRFHEATAQNApdvvVWGSGTpmreflHVDDMAAASIHVMELAHEvwlent 236
Cdd:COG1091 144 ILRTSWVYGEYgNNF------VKTMlrLAKEGKELKVVDD----QYGSPT------YTEDLADAILELLEKEKE------ 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 237 qPMLSHInVGTGVdCTIRELAQTIAKVVGYKGRVVfDASKPDGTPRKL-------LDVTRLHQLGWYHEISLEAGLASTY 309
Cdd:COG1091 202 -GGVYHL-VNSGE-CSWYEFAKAIFEEAGVDGEVI-EPIASAEYPTPAkrpanssLDTKKLEKAFGLSLPEWREALKALL 277

                .
gi 16129992 310 Q 310
Cdd:COG1091 278 D 278
PLN02206 PLN02206
UDP-glucuronate decarboxylase
5-305 3.57e-08

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 54.22  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    5 RVFIAGHRGMVGSAIRRQLEQRGDVELVLRtrdelNLLDSR---AVHDF----FASER----------IDQVYLAAAKVG 67
Cdd:PLN02206 121 RVVVTGGAGFVGSHLVDRLMARGDSVIVVD-----NFFTGRkenVMHHFsnpnFELIRhdvvepilleVDQIYHLACPAS 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   68 GiVANNTYPADFIYQNMMIESNIIHAAHQNDVnKLLFLGSSCIYPKLAKQPMAESelLQGTLEP--TNEPYAIAKIAGIK 145
Cdd:PLN02206 196 P-VHYKFNPVKTIKTNVVGTLNMLGLAKRVGA-RFLLTSTSEVYGDPLQHPQVET--YWGNVNPigVRSCYDEGKRTAET 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  146 LCESYNRQYGRDYRSVMPTNLYGPH---DNFHPSNSHVIPALLRRfheataqnapDVVVWGSGTPMREFLHVDDMAAASI 222
Cdd:PLN02206 272 LTMDYHRGANVEVRIARIFNTYGPRmciDDGRVVSNFVAQALRKE----------PLTVYGDGKQTRSFQFVSDLVEGLM 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  223 HVMELAHevwlentqpmLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQ-LGWYHEISL 301
Cdd:PLN02206 342 RLMEGEH----------VGPFNLGNPGEFTMLELAKVVQETIDPNAKIEFRPNTEDDPHKRKPDITKAKElLGWEPKVSL 411

                 ....
gi 16129992  302 EAGL 305
Cdd:PLN02206 412 RQGL 415
PLN02427 PLN02427
UDP-apiose/xylose synthase
73-310 1.89e-07

UDP-apiose/xylose synthase


Pssm-ID: 178047 [Multi-domain]  Cd Length: 386  Bit Score: 51.78  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   73 NTYPADFIYQNMMIESNIIHAAHQNdvNKLLFLGSSC-IYPK-----------LAKQPM------AESELLQGTLEPTNE 134
Cdd:PLN02427 103 NTRPLDTIYSNFIDALPVVKYCSEN--NKRLIHFSTCeVYGKtigsflpkdhpLRQDPAfyvlkeDESPCIFGSIEKQRW 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  135 PYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHP---SNSHVIPALLRRFHEATAQNAPDVVVWGsGTPMREF 211
Cdd:PLN02427 181 SYACAKQLIERLIYAEGAENGLEFTIVRPFNWIGPRMDFIPgidGPSEGVPRVLACFSNNLLRREPLKLVDG-GQSQRTF 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  212 LHVDDmAAASIHVMelahevwLENTQPMLSHI-NVGT-GVDCTIRELAQTIAKVVG-YKGRVVFD------ASKP----- 277
Cdd:PLN02427 260 VYIKD-AIEAVLLM-------IENPARANGHIfNVGNpNNEVTVRQLAEMMTEVYAkVSGEPALEeptvdvSSKEfygeg 331
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129992  278 -DGTPRKLLDVTRLH-QLGWYHEISLEAGLAST--YQ 310
Cdd:PLN02427 332 yDDSDKRIPDMTIINkQLGWNPKTSLWDLLESTltYQ 368
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
6-314 5.19e-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: 50.38  E-value: 5.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   6 VFIAGHRGMVGSAIRRQLEQRG--DVELVLRTRDE---LNLLDSR-----AVHDFFASERIDQVYLaaaKVGGIVAN--- 72
Cdd:cd05248   2 IIVTGGAGFIGSNLVKALNERGitDILVVDNLSNGekfKNLVGLKiadyiDKDDFKDWVRKGDENF---KIEAIFHQgac 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  73 -NTYPADfiyQNMMIESN------IIHAAHQNDVnKLLFLGSSCIYPKLAKQPMAESELLQgtLEPTNePYAIAKiagiK 145
Cdd:cd05248  79 sDTTETD---GKYMMDNNyqytkeLLHYCLEKKI-RFIYASSAAVYGNGSLGFAEDIETPN--LRPLN-VYGYSK----L 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 146 LCESYNRQYGRDYRSVMPT----NLYGPHDNFHPSNSHVIpalLRRFHEATAQNAPDVVVW----GSGTPMREFLHVDDM 217
Cdd:cd05248 148 LFDQWARRHGKEVLSQVVGlryfNVYGPREYHKGRMASVV---FHLFNQIKAGEKVKLFKSsdgyADGEQLRDFVYVKDV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 218 AAASIHVMELahevwlentqPMLSHI-NVGTGVDCTIRELAQTIAKVVGYKGRVVFDAskpdgTPRKLL---------DV 287
Cdd:cd05248 225 VKVNLFFLEN----------PSVSGIfNVGTGRARSFNDLASATFKALGKEVKIEYID-----FPEDLRgkyqsfteaDI 289
                       330       340       350
                ....*....|....*....|....*....|
gi 16129992 288 TRLHQLGW---YHeiSLEAGLASTYQWFLE 314
Cdd:cd05248 290 SKLRAAGYtkeFH--SLEEGVKDYVKNYLA 317
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
6-64 7.94e-07

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: 309453 [Multi-domain]  Cd Length: 283  Bit Score: 49.56  E-value: 7.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129992     6 VFIAGHRGMVGSAIRRQLEQRGdVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAA 64
Cdd:pfam04321   1 ILVTGANGQLGTELRRLLAERG-IEVLALTRPQLDLTDPEAVARLLREARPDVVVNAAA 58
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
5-317 5.24e-06

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 47.09  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    5 RVFIAGHRGMVGSAIRRQ--------------------LEQRGDVELVLR-TRDELNLLDSRAVHDFFASERIDQVYLAA 63
Cdd:PRK10084   2 KILVTGGAGFIGSAVVRHiinntqdsvvnvdkltyagnLESLADVSDSERyVFEHADICDRAELDRIFAQHQPDAVMHLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   64 AKvGGIVANNTYPADFIYQNMMIESNIIHAAHQ-----NDVNKLLF----LGSSCIYPKLAK-QPMAESELLQGTLEPT- 132
Cdd:PRK10084  82 AE-SHVDRSITGPAAFIETNIVGTYVLLEAARNywsalDEDKKNAFrfhhISTDEVYGDLPHpDEVENSEELPLFTETTa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  133 ---NEPYAIAKIAGIKLCESYNRQYGrdyrsvMPT------NLYGPhdnFH-PSNshVIPALLrrfheATAQNAPDVVVW 202
Cdd:PRK10084 161 yapSSPYSASKASSDHLVRAWLRTYG------LPTivtncsNNYGP---YHfPEK--LIPLVI-----LNALEGKPLPIY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  203 GSGTPMREFLHVDDMAAASIHVME--LAHEVWlentqpmlshiNVGTGVDCTIRELAQTIA--------KVVGYKGRVVF 272
Cdd:PRK10084 225 GKGDQIRDWLYVEDHARALYKVVTegKAGETY-----------NIGGHNEKKNLDVVLTICdlldeivpKATSYREQITY 293
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 16129992  273 DASKPDGTPRKLLDVTRLH-QLGWYHEISLEAGLASTYQWFLENQD 317
Cdd:PRK10084 294 VADRPGHDRRYAIDASKISrELGWKPQETFESGIRKTVEWYLANTE 339
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
5-271 5.25e-06

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: 46.90  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDvELVLRTRDELNLLDSRAVhDFFASERIDQVYLAAAKVGG----IVANNTY-PADf 79
Cdd:cd05265   2 KILIIGGTRFIGKALVEELLAAGH-DVTVFNRGRTKPDLPEGV-EHIVGDRNDRDALEELLGGEdfdvVVDTIAYtPRQ- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  80 iyqnmmIEsnIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEP--YAIAKIAgiklCESYNRQYGRD 157
Cdd:cd05265  79 ------VE--RALDAFKGRVKQYIFISSASVYLKPGRVITESTPLREPDAVGLSDPwdYGRGKRA----AEDVLIEAAAF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 158 -YRSVMPTNLYGPHDNFHPSNSHVipallrrfhEATAQNAPdVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVwlenT 236
Cdd:cd05265 147 pYTIVRPPYIYGPGDYTGRLAYFF---------DRLARGRP-ILVPGDGHSLVQFIHVKDLARALLGAAGNPKAI----G 212
                       250       260       270
                ....*....|....*....|....*....|....*
gi 16129992 237 QPmlshINVGTGVDCTIRELAQTIAKVVGYKGRVV 271
Cdd:cd05265 213 GI----FNITGDEAVTWDELLEACAKALGKEAEIV 243
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
6-312 1.92e-05

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: 45.35  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   6 VFIAGHRGMVGSAIRRQLEQRG-DVE-LVLRTRD------------ELNLLDSRAVHDffASERIDQVYLAAAkvggIVA 71
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLAQGyRVRaLVRSGSDavlldglpvevvEGDLTDAASLAA--AMKGCDRVFHLAA----FTS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  72 NNTYPADFIYQ-NMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGtlEPTNEPYAIAKIAGIKLCESY 150
Cdd:cd05228  75 LWAKDRKELYRtNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWNE--RPFPNDYYRSKLLAELEVLEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 151 NRQyGRDYRSVMPTNLYGPHDnFHPSNSHVIpalLRRFHEATAQNAPDvvvwgSGTpmrEFLHVDDMAAASIHVME--LA 228
Cdd:cd05228 153 AAE-GLDVVIVNPSAVFGPGD-EGPTSTGLD---VLDYLNGKLPAYPP-----GGT---SFVDVRDVAEGHIAAMEkgRR 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 229 HEVWLentqpmLSHINVgtgvdcTIRELAQTIAKVVGYK--------------GRVVFDASKPDGTPrKLLDVTRLHQLG 294
Cdd:cd05228 220 GERYI------LGGENL------SFKQLFETLAEITGVKpprrtippwllkavAALSELKARLTGKP-PLLTPRTARVLR 286
                       330       340       350
                ....*....|....*....|....*....|..
gi 16129992 295 WYHEIS--------------LEAGLASTYQWF 312
Cdd:cd05228 287 RNYLYSsdkarrelgysprpLEEALRDTLAWL 318
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
6-174 2.13e-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: 43.93  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   6 VFIAGHRGMVGSAIRRQLEQRG-DVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAK----VGGIVANNTYPADFI 80
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGhEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQgvdvVIHLAGAPRDTRDFC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  81 YQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPklakqpmaesELLQGTLEPTNEPYAIAKIAgiklCESYNRQYGRDYRS 160
Cdd:cd05226  81 EVDVEGTRNVLEAAKEAGVKHFIFISSLGAYG----------DLHEETEPSPSSPYLAVKAK----TEAVLREASLPYTI 146
                       170
                ....*....|....
gi 16129992 161 VMPTNLYGPHDNFH 174
Cdd:cd05226 147 VRPGVIYGDLARAI 160
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
5-294 4.64e-05

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: 44.15  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRG-DVELVLRTRDE---LNLLDSRAVHDFFASERIDQVYLAAAKVGGIVA----NNTYP 76
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGyEVIGTGRSRASlfkLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCesdpELAYR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  77 --ADFIYqnmmiesNIIHAAHQNDVnKLLFLGSSCIYPKlAKQPMAESEllqgTLEPTNEpYAIAKIAGiklcESYNRQY 154
Cdd:cd05254  81 vnVLAPE-------NLARAAKEVGA-RLIHISTDYVFDG-KKGPYKEED----APNPLNV-YGKSKLLG----EVAVLNA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 155 GRDYRsVMPTN-LYGPHDNfhpSNSHVIPALlrrfHEATAQNAPDVVVWGSGTPmrefLHVDDMAAASIHVMElahevwl 233
Cdd:cd05254 143 NPRYL-ILRTSwLYGELKN---GENFVEWML----RLAAERKEVNVVHDQIGSP----TYAADLADAILELIE------- 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129992 234 ENTQPMLSHInVGTGVdCTIRELAQTIAKVVGYKG---RVVFDASKPDGTPRKL---LDVTRLHQLG 294
Cdd:cd05254 204 RNSLTGIYHL-SNSGP-ISKYEFAKLIADALGLPDveiKPITSSEYPLPARRPAnssLDCSKLEELG 268
heptose_epim TIGR02197
ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ...
8-314 7.80e-05

ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ADP-L-glycero-D-mannoheptose-6-epimerase, an enzyme involved in biosynthesis of the inner core of lipopolysaccharide (LPS) for Gram-negative bacteria. This enzyme is homologous to UDP-glucose 4-epimerase (TIGR01179) and belongs to the NAD dependent epimerase/dehydratase family (pfam01370). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274028 [Multi-domain]  Cd Length: 314  Bit Score: 43.42  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992     8 IAGHRGMVGSAIRRQLEQRG--DVELVLRTRDE---LNLLDSRAVHDFFASERIDQvyLAAAKVGGIVA-------NNTY 75
Cdd:TIGR02197   3 VTGGAGFIGSNLVKALNERGitDILVVDNLRDGhkfLNLADLVIADYIDKEDFLDR--LEKGAFGKIEAifhqgacSDTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992    76 PADfiyQNMMIESN------IIHAAHQNDVnKLLFLGSSCIYPKlAKQPMAESELLQGtlePTNePYAIAKiagiKLCES 149
Cdd:TIGR02197  81 ETD---GEYMMENNyqyskrLLDWCAEKGI-PFIYASSAATYGD-GEAGFREGRELER---PLN-VYGYSK----FLFDQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   150 YNRQYGRDYRSVMPT------NLYGPHDNFHPSNSHVIpalLRRFHEATAQNAPDVVVWG----SGTPMREFLHVDDMAA 219
Cdd:TIGR02197 148 YVRRRVLPEALSAQVvglryfNVYGPREYHKGKMASVA---FHLFNQIKAGGNVKLFKSSegfkDGEQLRDFVYVKDVVD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   220 ASIHVMElahevwlentqPMLSHI-NVGTGVDCTIRELAQTIAKVVGyKGRVVFDASKPDGTPRKL-----LDVTRLHQL 293
Cdd:TIGR02197 225 VNLWLLE-----------NGVSGIfNLGTGRARSFNDLADAVFKALG-KDEKIEYIPMPEALRGRYqyftqADITKLRAA 292
                         330       340
                  ....*....|....*....|..
gi 16129992   294 GWYHE-ISLEAGLASTYQWFLE 314
Cdd:TIGR02197 293 GYYGPfTTLEEGVKDYVQWLLA 314
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
5-266 1.08e-04

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: 43.19  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   5 RVFIAGHRGMVGSAIRRQLEQRGDVELVL------------RTRDEL-----NLLDSRAVHDffASERIDQVYLAAAKVG 67
Cdd:cd05241   1 SVLVTGGSGFFGERLVKQLLERGGTYVRSfdiappgealsaWQHPNIeflkgDITDRNDVEQ--ALSGADCVFHTAAIVP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992  68 GIvanntYPADFIYQ-NMMIESNIIHAAHQNDVNKLLFLGSSCIYPKlaKQPMAESELLQGTLEPTNEPYAIAKIAGIKL 146
Cdd:cd05241  79 LA-----GPRDLYWEvNVGGTQNVLDACQRCGVQKFVYTSSSSVIFG--GQNIHNGDETLPYPPLDSDMYAETKAIAEII 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 147 CESYNRQYGRDYRSVMPTNLYGPHDNFHpsnshvipalLRRFHEAtAQNAPDVVVWGSGTPMREFLHVDDMAAASIhvme 226
Cdd:cd05241 152 VLEANGRDDLLTCALRPAGIFGPGDQGL----------VPILFEW-AEKGLVKFVFGRGNNLVDFTYVHNLAHAHI---- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 16129992 227 LAHEVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGY 266
Cdd:cd05241 217 LAAAALVKGKTISGQTYFITDAEPHNMFELLRPVWKALGF 256
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
209-311 2.72e-04

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: 41.89  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992 209 REFLHVDDMAAasihvmelAHEVWLENTQPMLSHI-NVGTGVD--CTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLL 285
Cdd:cd05258 238 RDVLHSADLVN--------LYLRQFQNPDRRKGEVfNIGGGREnsVSLLELIALCEEITGRKMESYKDENRPGDQIWYIS 309
                        90       100
                ....*....|....*....|....*..
gi 16129992 286 DVTRLHQ-LGWYHEISLEAGLASTYQW 311
Cdd:cd05258 310 DIRKIKEkPGWKPERDPREILAEIYAW 336
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
2-105 8.08e-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: 37.21  E-value: 8.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129992   2 SKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLL-----------------------DSRAVHDFFASERIDQ 58
Cdd:cd05237   1 KGKTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHelvrelrsrfphdklrfiigdvrDKERLRRAFKERGPDI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16129992  59 VYLAAA-KvgGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFL 105
Cdd:cd05237  81 VFHAAAlK--HVPSMEDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCI 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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