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Conserved domains on  [gi|960513905|ref|NP_001304712|]
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GDP-L-fucose synthase isoform 1 [Homo sapiens]

Protein Classification

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

GDP-L-fucose synthase family protein such as GDP-L-fucose synthase that catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction; belongs to the extended (e) SDR (short-chain dehydrogenase/reductase) family; in addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
15-318 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: 502.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQKVVADGAGlpgEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWR 94
Cdd:cd05239    1 KILVTGHRGLVGSAIVRVLARRGY---ENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  95 KNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAV 174
Cdd:cd05239   78 DNLLINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 175 IPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGS-ALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNevEPIILSVGEE 253
Cdd:cd05239  158 MPTNLYGPHDNFDPENSHVIPALIRKFHEAKLRGGkEVTVWGSGTPRREFLYSDDLARAIVFLLENYD--EPIIVNVGSG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513905 254 DEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTyLPDFRFTPFKQAVKETCAWF 318
Cdd:cd05239  236 VEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRA-LGWFPFTPLEQGIRETYEWY 299
 
Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
15-318 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: 502.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQKVVADGAGlpgEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWR 94
Cdd:cd05239    1 KILVTGHRGLVGSAIVRVLARRGY---ENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  95 KNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAV 174
Cdd:cd05239   78 DNLLINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 175 IPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGS-ALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNevEPIILSVGEE 253
Cdd:cd05239  158 MPTNLYGPHDNFDPENSHVIPALIRKFHEAKLRGGkEVTVWGSGTPRREFLYSDDLARAIVFLLENYD--EPIIVNVGSG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513905 254 DEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTyLPDFRFTPFKQAVKETCAWF 318
Cdd:cd05239  236 VEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRA-LGWFPFTPLEQGIRETYEWY 299
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
17-327 4.80e-159

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


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 446.45  E-value: 4.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  17 LVTGGSGLVGKAIQKVVAdgaGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKN 96
Cdd:PLN02725   1 FVAGHRGLVGSAIVRKLE---ALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIREN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  97 VHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIP 176
Cdd:PLN02725  78 LQIQTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 177 TNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALT-VWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIilSVGEEDE 255
Cdd:PLN02725 158 TNLYGPHDNFHPENSHVIPALIRRFHEAKANGAPEVvVWGSGSPLREFLHVDDLADAVVFLMRRYSGAEHV--NVGSGDE 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513905 256 VSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFtPFKQAVKETCAWFTDNYEQARK 327
Cdd:PLN02725 236 VTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKF-SLKDGLQETYKWYLENYETGGK 306
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
16-251 2.13e-59

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 190.59  E-value: 2.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   16 ILVTGGSGLVGKAIQKVVADgaglPGEDWVFVSSK---------------DADLTDTAQTRALFEKVQPTHVIHLAAmVG 80
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLE----KGYEVIGLDRLtsasntarladlrfvEGDLTDRDALEKLLADVRPDAVIHLAA-VG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   81 GLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETmIHNGPPHnSNFGYSYAKRMIDVQN 160
Cdd:pfam01370  76 GVGASIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEET-TLTGPLA-PNSPYAAAKLAGEWLV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  161 RAYFQQYGCTFTAVIPTNVFGPHDNfNIEDGHVLPGLIHKVHLAKSsgsaLTVWGTGNPRRQFIYSLDLAQLFIWVLREY 240
Cdd:pfam01370 154 LAYAAAYGLRAVILRLFNVYGPGDN-EGFVSRVIPALIRRILEGKP----ILLWGDGTQRRDFLYVDDVARAILLALEHG 228
                         250
                  ....*....|.
gi 960513905  241 NeVEPIILSVG 251
Cdd:pfam01370 229 A-VKGEIYNIG 238
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
15-318 5.07e-43

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 150.13  E-value: 5.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI--------QKVVA---------DGAGLPGEDWVFvsskdADLTDTAQTRALFEKVqpTHVIHLAA 77
Cdd:COG0451    1 RILVTGGAGFIGSHLarrllargHEVVGldrsppgaaNLAALPGVEFVR-----GDLRDPEALAAALAGV--DAVVHLAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  78 MVGGLFRNikyNLDFWRKNVHMNDNVLHSAFEVGARKVV--SclSTCIFPDkTTYPIDETMIHNgpPHNSnfgYSYAKRM 155
Cdd:COG0451   74 PAGVGEED---PDETLEVNVEGTLNLLEAARAAGVKRFVyaS--SSSVYGD-GEGPIDEDTPLR--PVSP---YGASKLA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 156 IDVQNRAYFQQYGCTFTAVIPTNVFGPHDNfniedgHVLPGLIHKVHlaksSGSALTVWGTGNPRRQFIYSLDLAQLFIW 235
Cdd:COG0451  143 AELLARAYARRYGLPVTILRPGNVYGPGDR------GVLPRLIRRAL----AGEPVPVFGDGDQRRDFIHVDDVARAIVL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 236 VLrEYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKtASNSKLRTYLpDFRF-TPFKQAVKET 314
Cdd:COG0451  213 AL-EAPAAPGGVYNVGGGEPVTLRELAEAIAEALGRPPEIVYPARPGDVRPRR-ADNSKARREL-GWRPrTSLEEGLRET 289

                 ....
gi 960513905 315 CAWF 318
Cdd:COG0451  290 VAWY 293
 
Name Accession Description Interval E-value
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
15-318 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: 502.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQKVVADGAGlpgEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWR 94
Cdd:cd05239    1 KILVTGHRGLVGSAIVRVLARRGY---ENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMTYPADFLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  95 KNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAV 174
Cdd:cd05239   78 DNLLINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGLKLCEAYRKQYGCDYISV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 175 IPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGS-ALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNevEPIILSVGEE 253
Cdd:cd05239  158 MPTNLYGPHDNFDPENSHVIPALIRKFHEAKLRGGkEVTVWGSGTPRREFLYSDDLARAIVFLLENYD--EPIIVNVGSG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513905 254 DEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTyLPDFRFTPFKQAVKETCAWF 318
Cdd:cd05239  236 VEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRA-LGWFPFTPLEQGIRETYEWY 299
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
17-327 4.80e-159

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


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 446.45  E-value: 4.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  17 LVTGGSGLVGKAIQKVVAdgaGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKN 96
Cdd:PLN02725   1 FVAGHRGLVGSAIVRKLE---ALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYPADFIREN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  97 VHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIP 176
Cdd:PLN02725  78 LQIQTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKMCQAYRIQYGWDAISGMP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 177 TNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALT-VWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIilSVGEEDE 255
Cdd:PLN02725 158 TNLYGPHDNFHPENSHVIPALIRRFHEAKANGAPEVvVWGSGSPLREFLHVDDLADAVVFLMRRYSGAEHV--NVGSGDE 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513905 256 VSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFtPFKQAVKETCAWFTDNYEQARK 327
Cdd:PLN02725 236 VTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGWDPKF-SLKDGLQETYKWYLENYETGGK 306
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
16-251 2.13e-59

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 190.59  E-value: 2.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   16 ILVTGGSGLVGKAIQKVVADgaglPGEDWVFVSSK---------------DADLTDTAQTRALFEKVQPTHVIHLAAmVG 80
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLE----KGYEVIGLDRLtsasntarladlrfvEGDLTDRDALEKLLADVRPDAVIHLAA-VG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   81 GLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETmIHNGPPHnSNFGYSYAKRMIDVQN 160
Cdd:pfam01370  76 GVGASIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEET-TLTGPLA-PNSPYAAAKLAGEWLV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  161 RAYFQQYGCTFTAVIPTNVFGPHDNfNIEDGHVLPGLIHKVHLAKSsgsaLTVWGTGNPRRQFIYSLDLAQLFIWVLREY 240
Cdd:pfam01370 154 LAYAAAYGLRAVILRLFNVYGPGDN-EGFVSRVIPALIRRILEGKP----ILLWGDGTQRRDFLYVDDVARAILLALEHG 228
                         250
                  ....*....|.
gi 960513905  241 NeVEPIILSVG 251
Cdd:pfam01370 229 A-VKGEIYNIG 238
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
15-318 5.07e-43

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 150.13  E-value: 5.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI--------QKVVA---------DGAGLPGEDWVFvsskdADLTDTAQTRALFEKVqpTHVIHLAA 77
Cdd:COG0451    1 RILVTGGAGFIGSHLarrllargHEVVGldrsppgaaNLAALPGVEFVR-----GDLRDPEALAAALAGV--DAVVHLAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  78 MVGGLFRNikyNLDFWRKNVHMNDNVLHSAFEVGARKVV--SclSTCIFPDkTTYPIDETMIHNgpPHNSnfgYSYAKRM 155
Cdd:COG0451   74 PAGVGEED---PDETLEVNVEGTLNLLEAARAAGVKRFVyaS--SSSVYGD-GEGPIDEDTPLR--PVSP---YGASKLA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 156 IDVQNRAYFQQYGCTFTAVIPTNVFGPHDNfniedgHVLPGLIHKVHlaksSGSALTVWGTGNPRRQFIYSLDLAQLFIW 235
Cdd:COG0451  143 AELLARAYARRYGLPVTILRPGNVYGPGDR------GVLPRLIRRAL----AGEPVPVFGDGDQRRDFIHVDDVARAIVL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 236 VLrEYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKtASNSKLRTYLpDFRF-TPFKQAVKET 314
Cdd:COG0451  213 AL-EAPAAPGGVYNVGGGEPVTLRELAEAIAEALGRPPEIVYPARPGDVRPRR-ADNSKARREL-GWRPrTSLEEGLRET 289

                 ....
gi 960513905 315 CAWF 318
Cdd:COG0451  290 VAWY 293
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
15-326 3.46e-27

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: 108.72  E-value: 3.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI-QKVVADGAGLPGEDWVFVSSKD----------ADLTDTAQTRALFEKVQptHVIHLAAMVGGLF 83
Cdd:cd05273    2 RALVTGAGGFIGSHLaERLKAEGHYVRGADWKSPEHMTqptdddefhlVDLREMENCLKATEGVD--HVFHLAADMGGMG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  84 RNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFP-----DKTTYPIDETMIHNGPPHNsnfGYSYAKRMIDV 158
Cdd:cd05273   80 YIQSNHAVIMYNNTLINFNMLEAARINGVERFLFASSACVYPefkqlETTVVRLREEDAWPAEPQD---AYGWEKLATER 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 159 QNRAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSaLTVWGTGNPRRQFIYSLDLAQLFIwVLR 238
Cdd:cd05273  157 LCQHYNEDYGIETRIVRFHNIYGPRGTWDGGREKAPAAMCRKVATAKDGDR-FEIWGDGLQTRSFTYIDDCVEGLR-RLM 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 239 EYNEVEPIILsvGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKETCAWF 318
Cdd:cd05273  235 ESDFGEPVNL--GSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVRGRNSDNTLLKEELGWEPNTPLEEGLRITYFWI 312

                 ....*...
gi 960513905 319 TDNYEQAR 326
Cdd:cd05273  313 KEQIEAEK 320
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
16-247 1.77e-21

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: 90.05  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKAI-QKVVADGAGLPGEDWVfvsskdadltdtaqtralfekvqpTHVIHLAAMVGGLFrNIKYNLDFWR 94
Cdd:cd08946    1 ILVTGGAGFIGSHLvRRLLERGHEVVVIDRL------------------------DVVVHLAALVGVPA-SWDNPDEDFE 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  95 KNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMihngPPHNSNFgYSYAKRMIDVQNRAYFQQYGCTFTAV 174
Cdd:cd08946   56 TNVVGTLNLLEAARKAGVKRFVYASSASVYGSPEGLPEEEET----PPRPLSP-YGVSKLAAEHLLRSYGESYGLPVVIL 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 960513905 175 IPTNVFGPHDNFNieDGHVLPGLIHKVHlaksSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPII 247
Cdd:cd08946  131 RLANVYGPGQRPR--LDGVVNDFIRRAL----EGKPLTVFGGGNQTRDFIHVDDVVRAILHALENPLEGGGVY 197
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
15-318 1.41e-20

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: 89.97  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI-QKVVADGAG-------LPGEDW---------VFVSskdADLTDTAQTRALFEKVqpTHVIHLAA 77
Cdd:cd05256    1 RVLVTGGAGFIGSHLvERLLERGHEvivldnlSTGKKEnlpevkpnvKFIE---GDIRDDELVEFAFEGV--DYVFHQAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  78 MvGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNgP--PhnsnfgYSYAKRM 155
Cdd:cd05256   76 Q-ASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDEDHPPN-PlsP------YAVSKYA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 156 IDVQNRAYFQQYGctftavIPT------NVFGPHDNFNIEDGHVLPGLIHkvhlAKSSGSALTVWGTGNPRRQFIYSLDL 229
Cdd:cd05256  148 GELYCQVFARLYG------LPTvslryfNVYGPRQDPNGGYAAVIPIFIE----RALKGEPPTIYGDGEQTRDFTYVEDV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 230 AQLFIWVLreYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFdTTKSDGQFKKT-ASNSKLRTYL---PDfrfT 305
Cdd:cd05256  218 VEANLLAA--TAGAGGEVYNIGTGKRTSVNELAELIREILGKELEPVY-APPRPGDVRHSlADISKAKKLLgwePK---V 291
                        330
                 ....*....|...
gi 960513905 306 PFKQAVKETCAWF 318
Cdd:cd05256  292 SFEEGLRLTVEWF 304
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
15-78 2.36e-14

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 72.09  E-value: 2.36e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960513905  15 RILVTGGSGLVGKAIQKVVADgaglPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAM 78
Cdd:COG1091    1 RILVTGANGQLGRALVRLLAE----RGYEVVALDRSELDITDPEAVAALLEEVRPDVVINAAAY 60
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
13-299 1.92e-13

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 70.43  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  13 SMRILVTGGSGLVGK-AIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRalFE-----KVQPT-----HVIHLAAMVGG 81
Cdd:PLN02166 120 RLRIVVTGGAGFVGShLVDKLIGRGDEVIVIDNFFTGRKENLVHLFGNPR--FElirhdVVEPIllevdQIYHLACPASP 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  82 LfrNIKYN-LDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTcIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQN 160
Cdd:PLN02166 198 V--HYKYNpVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSE-VYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 161 RAYFQQYGCTFTAVIPTNVFGPHdnFNIEDGHVLPGLIHKVhlakSSGSALTVWGTGNPRRQFIYSLDLAQLFIwVLREY 240
Cdd:PLN02166 275 MDYHRGAGVEVRIARIFNTYGPR--MCLDDGRVVSNFVAQT----IRKQPMTVYGDGKQTRSFQYVSDLVDGLV-ALMEG 347
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 960513905 241 NEVEPiiLSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYL 299
Cdd:PLN02166 348 EHVGP--FNLGNPGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAKELL 404
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
14-318 4.76e-13

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: 68.43  E-value: 4.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  14 MRILVTGGSGLVGKAI-QKVVADGAGLPGEDWVFVSSKD---------------ADLTDtaqtralFEKVQPTHVIHLAA 77
Cdd:cd05230    1 KRILITGGAGFLGSHLcDRLLEDGHEVICVDNFFTGRKRniehlighpnfefirHDVTE-------PLYLEVDQIYHLAC 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  78 MVGGLFRnIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTcIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMID 157
Cdd:cd05230   74 PASPVHY-QYNPIKTLKTNVLGTLNMLGLAKRVGARVLLASTSE-VYGDPEVHPQPESYWGNVNPIGPRSCYDEGKRVAE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 158 VQNRAYFQQYGCTFTAVIPTNVFGPHDNFNieDGHVLPGLIhkvhLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVL 237
Cdd:cd05230  152 TLCMAYHRQHGVDVRIARIFNTYGPRMHPN--DGRVVSNFI----VQALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLM 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 238 REYNEVEPIilSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYL---PDfrfTPFKQAVKET 314
Cdd:cd05230  226 NSDYFGGPV--NLGNPEEFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKELLgwePK---VPLEEGLRRT 300

                 ....
gi 960513905 315 CAWF 318
Cdd:cd05230  301 IEYF 304
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
14-323 6.31e-12

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: 65.26  E-value: 6.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  14 MRILVTGGSGLVG-----------KAIQKVVAD----GAGL-------PGEDWVFVSskdADLTDTAQTRALFEKVQPTH 71
Cdd:cd05246    1 MKILVTGGAGFIGsnfvryllnkyPDYKIINLDkltyAGNLenledvsSSPRYRFVK---GDICDAELVDRLFEEEKIDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  72 VIHLAAM--VGglfRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVScLSTcifpD------KTTYPIDETMIHNgpPH 143
Cdd:cd05246   78 VIHFAAEshVD---RSISDPEPFIRTNVLGTYTLLEAARKYGVKRFVH-IST----DevygdlLDDGEFTETSPLA--PT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 144 NSnfgYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDnfNIEDghvlpgLIHKVHLAKSSGSALTVWGTGNPRRQF 223
Cdd:cd05246  148 SP---YSASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQ--FPEK------LIPLFILNALDGKPLPIYGDGLNVRDW 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 224 IYSLDLAQLFIWVLREYNEVEpiILSVGEEDEVSIKEAAEAVVEAMD-FHGEVTFDTTKSDGQFKKTASNSKLRTYLPDF 302
Cdd:cd05246  217 LYVEDHARAIELVLEKGRVGE--IYNIGGGNELTNLELVKLILELLGkDESLITYVKDRPGHDRRYAIDSSKIRRELGWR 294
                        330       340
                 ....*....|....*....|.
gi 960513905 303 RFTPFKQAVKETCAWFTDNYE 323
Cdd:cd05246  295 PKVSFEEGLRKTVRWYLENRW 315
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
14-318 2.35e-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: 63.68  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  14 MRILVTGGSGLVGKAIQKVVadgagLPGEDWVFV------------------SSKDADLTDTAQTRALFEKVQPTHVIHL 75
Cdd:cd08957    1 MKVLITGGAGQIGSHLIEHL-----LERGHQVVVidnfatgrrehlpdhpnlTVVEGSIADKALVDKLFGDFKPDAVVHT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  76 AAmvgglfrniKY-NLDFW----RKNVHMNDNVLHSAFEVGARKVVSCLST-CIFPDKTTYPIdeTMIHNGPPHNSNFGY 149
Cdd:cd08957   76 AA---------AYkDPDDWyedtLTNVVGGANVVQAAKKAGVKRLIYFQTAlCYGLKPMQQPI--RLDHPRAPPGSSYAI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 150 SyakrmiDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNiedghVLPGLIHKVhlakSSGSALTVWGTgnpRRQFIYSLDL 229
Cdd:cd08957  145 S------KTAGEYYLELSGVDFVTFRLANVTGPRNVIG-----PLPTFYQRL----KAGKKCFVTDT---RRDFVFVKDL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 230 AQLfiwVLREYNEVEP---IILSVGEedEVSIKEAAEAVVEAMDFHGE---------------VTFDTTKSDGQFKKTAs 291
Cdd:cd08957  207 ARV---VDKALDGIRGhgaYHFSSGE--DVSIKELFDAVVEALDLPLRpevevvelgpddvpsILLDPSRTFQDFGWKE- 280
                        330       340
                 ....*....|....*....|....*..
gi 960513905 292 nsklrtylpdfrFTPFKQAVKETCAWF 318
Cdd:cd08957  281 ------------FTPLSETVSAALAWY 295
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
15-321 3.96e-11

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: 63.09  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI-QKVVADGAGLPGED---------WVFVSSKD------ADLTDTAQTRALFEKVQPthVIHLAAM 78
Cdd:cd05257    1 NVLVTGADGFIGSHLtERLLREGHEVRALDiynsfnswgLLDNAVHDrfhfisGDVRDASEVEYLVKKCDV--VFHLAAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  79 VGglfrnIKYN----LDFWRKNVHMNDNVLHSAFEVGARKVVScLSTC-IFPDKTTYPIDETmiH-NGPPHNSNFGYSYA 152
Cdd:cd05257   79 IA-----IPYSytapLSYVETNVFGTLNVLEAACVLYRKRVVH-TSTSeVYGTAQDVPIDED--HpLLYINKPRSPYSAS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 153 KRMIDVQNRAYFQQYGCTFTAVIPTNVFGP-HDNFNiedghVLPGLIhkvhLAKSSGSALTVWGTGNPRRQFIYSLDLAQ 231
Cdd:cd05257  151 KQGADRLAYSYGRSFGLPVTIIRPFNTYGPrQSARA-----VIPTII----SQRAIGQRLINLGDGSPTRDFNFVKDTAR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 232 LFIWVLREYNEVEPIIlSVGEEDEVSIKEAA-EAVVEAMDFHGEVTFDTTKS-----DGQFKKTASNSKLRTYLpDFR-F 304
Cdd:cd05257  222 GFIDILDAIEAVGEII-NNGSGEEISIGNPAvELIVEELGEMVLIVYDDHREyrpgySEVERRIPDIRKAKRLL-GWEpK 299
                        330
                 ....*....|....*..
gi 960513905 305 TPFKQAVKETCAWFTDN 321
Cdd:cd05257  300 YSLRDGLRETIEWFKDQ 316
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
16-184 5.71e-11

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 62.30  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVG--------------KAIQKVVADGAGLPGEDWVFVsskDADLTDTAQTRALFEKVQptHVIHLAAmvgg 81
Cdd:cd05228    1 ILVTGATGFLGsnlvrallaqgyrvRALVRSGSDAVLLDGLPVEVV---EGDLTDAASLAAAMKGCD--RVFHLAA---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  82 LFR-NIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNfgYSYAKRMIDVQN 160
Cdd:cd05228   72 FTSlWAKDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWNERPFPND--YYRSKLLAELEV 149
                        170       180
                 ....*....|....*....|....
gi 960513905 161 RAYFQQyGCTFTAVIPTNVFGPHD 184
Cdd:cd05228  150 LEAAAE-GLDVVIVNPSAVFGPGD 172
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
15-241 1.31e-10

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: 61.10  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQKVvadgagLPGEDW--VFVSSKDA-----DLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIK 87
Cdd:cd05254    1 KILITGATGMLGRALVRL------LKERGYevIGTGRSRAslfklDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  88 YNLDFwRKNVHMNDNVLHSAFEVGARKVVscLST-CIFpDKTTYPIDETMIHNgpPHNSnfgYSYAKRMIDVQNRAYFQQ 166
Cdd:cd05254   75 PELAY-RVNVLAPENLARAAKEVGARLIH--ISTdYVF-DGKKGPYKEEDAPN--PLNV---YGKSKLLGEVAVLNANPR 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 960513905 167 YgctftAVIPTNVFGPHDNFNIedghvlpGLIHKV-HLAKSSGSALTV-WGTGNPrrqfIYSLDLAQLFIWVLREYN 241
Cdd:cd05254  146 Y-----LILRTSWLYGELKNGE-------NFVEWMlRLAAERKEVNVVhDQIGSP----TYAADLADAILELIERNS 206
PLN02206 PLN02206
UDP-glucuronate decarboxylase
7-303 7.15e-10

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 59.61  E-value: 7.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   7 MGEPQGSMRILVTGGSGLVGK-AIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRalFEK-----VQPT-----HVIHL 75
Cdd:PLN02206 113 LGLKRKGLRVVVTGGAGFVGShLVDRLMARGDSVIVVDNFFTGRKENVMHHFSNPN--FELirhdvVEPIllevdQIYHL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  76 AAMVGGLfrNIKYN-LDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTcIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKR 154
Cdd:PLN02206 191 ACPASPV--HYKFNpVKTIKTNVVGTLNMLGLAKRVGARFLLTSTSE-VYGDPLQHPQVETYWGNVNPIGVRSCYDEGKR 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 155 MIDVQNRAYFQQYGCTFTAVIPTNVFGPHdnFNIEDGHVLPGLIHKVhLAKssgSALTVWGTGNPRRQFIYSLDLAQLFI 234
Cdd:PLN02206 268 TAETLTMDYHRGANVEVRIARIFNTYGPR--MCIDDGRVVSNFVAQA-LRK---EPLTVYGDGKQTRSFQFVSDLVEGLM 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 235 wVLREYNEVEPiiLSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSK------------LRTYLP-- 300
Cdd:PLN02206 342 -RLMEGEHVGP--FNLGNPGEFTMLELAKVVQETIDPNAKIEFRPNTEDDPHKRKPDITKakellgwepkvsLRQGLPlm 418

                 ....*
gi 960513905 301 --DFR 303
Cdd:PLN02206 419 vkDFR 423
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
15-238 9.39e-10

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: 58.87  E-value: 9.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQkvvadgAGLPGEDW---VFVSSKDADLTDTA---------QTRALFEK--VQPTHVIHLAA--M 78
Cdd:cd05264    1 RVLIVGGNGFIGSHLV------DALLEEGPqvrVFDRSIPPYELPLGgvdyikgdyENRADLESalVGIDTVIHLASttN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  79 VGGLFRNIkyNLDFwRKNVHMNDNVLHSAFEVGARKVV--SCLSTcIFPDKTTYPIDETmiHNGPPHNSnfgYSYAKRMI 156
Cdd:cd05264   75 PATSNKNP--ILDI-QTNVAPTVQLLEACAAAGIGKIIfaSSGGT-VYGVPEQLPISES--DPTLPISS---YGISKLAI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 157 DVQNRAYFQQYGCTFTAVIPTNVFGPHDNfnIEDGHvlpGLIhKVHLAK-SSGSALTVWGTGNPRRQFIYSLDLAQLFIW 235
Cdd:cd05264  146 EKYLRLYQYLYGLDYTVLRISNPYGPGQR--PDGKQ---GVI-PIALNKiLRGEPIEIWGDGESIRDYIYIDDLVEALMA 219

                 ...
gi 960513905 236 VLR 238
Cdd:cd05264  220 LLR 222
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
15-277 9.52e-10

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: 58.85  E-value: 9.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSG-----LVGKAIQK----VVAD--GAGLPGEDWVFVSSKDADL--TDTAQTRALFEKVQPTHVIHLAAMVGG 81
Cdd:cd05234    1 RILVTGGAGfigshLVDRLLEEgnevVVVDnlSSGRRENIEPEFENKAFRFvkRDLLDTADKVAKKDGDTVFHLAANPDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  82 LFRNIKYNLDFwRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDEtmihNGPPHNSNFgYSYAKRMIDVQNR 161
Cdd:cd05234   81 RLGATDPDIDL-EENVLATYNVLEAMRANGVKRIVFASSSTVYGEAKVIPTPE----DYPPLPISV-YGASKLAAEALIS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 162 AYFQQYGCTFTAVIPTNVFGPHDNfniedgH-VLPGLIHKVhlaKSSGSALTVWGTGNPRRQFIYSLDL--AQLFIWvlr 238
Cdd:cd05234  155 AYAHLFGFQAWIFRFANIVGPRST------HgVIYDFINKL---KRNPNELEVLGDGRQRKSYLYVSDCvdAMLLAW--- 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 960513905 239 EYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTF 277
Cdd:cd05234  223 EKSTEGVNIFNLGNDDTISVNEIAEIVIEELGLKPRFKY 261
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
15-267 1.57e-08

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: 54.93  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQKVVADGAglPGEDWVF----------------------VSSKDADLTDTAQTRALFEKVQPTHV 72
Cdd:cd05237    4 TILVTGGAGSIGSELVRQILKFG--PKKLIVFdrdenklhelvrelrsrfphdkLRFIIGDVRDKERLRRAFKERGPDIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  73 IHLAAM--VgglfRNIKYN-LDFWRKNVHMNDNVLHSAFEVGARKVVsCLSTcifpDKTTYPIdetmihngpphnSNFGY 149
Cdd:cd05237   82 FHAAALkhV----PSMEDNpEEAIKTNVLGTKNVIDAAIENGVEKFV-CIST----DKAVNPV------------NVMGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 150 SyaKRMIDVQNRAYFQQYGCT-FTAVIPTNVFGphdnfniEDGHVLPGLIHKVhlakSSGSALTVwgTGNPRRQFIYSLD 228
Cdd:cd05237  141 T--KRVAEKLLLAKNEYSSSTkFSTVRFGNVLG-------SRGSVLPLFKKQI----KKGGPLTV--TDPDMTRFFMTIP 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 960513905 229 LA-QLFIWVLREYNEVEPIILSVGEedEVSIKEAAEAVVE 267
Cdd:cd05237  206 EAvDLVLQACILGDGGGIFLLDMGP--PVKILDLAEALIE 243
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
15-327 3.54e-08

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: 53.97  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQK----------VVADGAGLPGEDWVF----VSSKDADLTDTAQTRALFEKVqpTHVIHLAAMVG 80
Cdd:cd05241    1 SVLVTGGSGFFGERLVKqllerggtyvRSFDIAPPGEALSAWqhpnIEFLKGDITDRNDVEQALSGA--DCVFHTAAIVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  81 GL-FRNIkynldFWRKNVHMNDNVLHSAFEVGARKVV-SCLSTCIFPDKTTYPIDETMihngP-PHNSNFGYSYAKRMID 157
Cdd:cd05241   79 LAgPRDL-----YWEVNVGGTQNVLDACQRCGVQKFVyTSSSSVIFGGQNIHNGDETL----PyPPLDSDMYAETKAIAE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 158 VQNRAYFQQYGCTFTAVIPTNVFGPHDNFniedghVLPGLIHKVHLakssGSALTVWGTGNPRRQFIYSLDLAQLFIwvL 237
Cdd:cd05241  150 IIVLEANGRDDLLTCALRPAGIFGPGDQG------LVPILFEWAEK----GLVKFVFGRGNNLVDFTYVHNLAHAHI--L 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 238 REYNEVEPIILS-----VGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFkqAVK 312
Cdd:cd05241  218 AAAALVKGKTISgqtyfITDAEPHNMFELLRPVWKALGFGSRPKIRLSGPLAYCAALLSELVSFMLGPYFVFSPF--YVR 295
                        330
                 ....*....|....*
gi 960513905 313 ETCAWFTDNYEQARK 327
Cdd:cd05241  296 ALVTPMYFSIAKAQK 310
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
15-230 8.86e-08

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


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 52.92  E-value: 8.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVG----KAIQK-----VVADG------AGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAM- 78
Cdd:cd05247    1 KVLVTGGAGYIGshtvVELLEagydvVVLDNlsnghrEALPRIEKIRIEFYEGDIRDRAALDKVFAEHKIDAVIHFAALk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  79 -VGglfRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVV-SclSTC-IFPDKTTYPIDETMIHNgpPHNSnfgYSYAKRM 155
Cdd:cd05247   81 aVG---ESVQKPLKYYDNNVVGTLNLLEAMRAHGVKNFVfS--SSAaVYGEPETVPITEEAPLN--PTNP---YGRTKLM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 156 IDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNI-ED----GHVLPgLIHKVHLAKSSGsaLTVWGT------GNPRRQFI 224
Cdd:cd05247  151 VEQILRDLAKAPGLNYVILRYFNPAGAHPSGLIgEDpqipNNLIP-YVLQVALGRREK--LAIFGDdyptpdGTCVRDYI 227

                 ....*.
gi 960513905 225 YSLDLA 230
Cdd:cd05247  228 HVVDLA 233
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
16-77 1.09e-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: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 52.28  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960513905   16 ILVTGGSGLVGKAIQKVVAdgaglpGEDWVFV--SSKDADLTDTAQTRALFEKVQPTHVIHLAA 77
Cdd:pfam04321   1 ILITGANGQLGTELRRLLA------ERGIEVValTRAELDLTDPEAVARLLREIKPDVVVNAAA 58
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
17-238 1.77e-07

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 51.60  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   17 LVTGGSGLVGKAI----------QKV-VADGAGLPGEDWVFVSSKDA-----DLTDTAQTRALFEKVQPthVIHLAA--M 78
Cdd:pfam01073   1 VVTGGGGFLGRHIikllvregelKEVrVFDLRESPELLEDFSKSNVIkyiqgDVTDKDDLDNALEGVDV--VIHTASavD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   79 VGGLFRNIKYnldfWRKNVHMNDNVLHSAFEVGARKVVSCLS-TCIFPDKTTYPidetmIHNG---PPHNSNFG--YSYA 152
Cdd:pfam01073  79 VFGKYTFDEI----MKVNVKGTQNVLEACVKAGVRVLVYTSSaEVVGPNSYGQP-----ILNGdeeTPYESTHQdaYPRS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  153 KRM----IDVQNRAYFQQYGCTFT-AVIPTNVFGPHDNFniedghVLPGLIHkvhlAKSSGSALTVWGTGNPRRQFIYSL 227
Cdd:pfam01073 150 KAIaeklVLKANGRPLKNGGRLYTcALRPAGIYGEGDRL------LVPFIVN----LAKLGLAKFKTGDDNNLSDRVYVG 219
                         250
                  ....*....|.
gi 960513905  228 DLAQLFIWVLR 238
Cdd:pfam01073 220 NVAWAHILAAR 230
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
16-132 4.00e-06

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


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 47.51  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   16 ILVTGGSGLVGKAIQKVVAD-----------------------GAGLPGED-WVFVSSKDADLTDTAQTRALFEKVQPTH 71
Cdd:pfam02719   1 VLVTGGGGSIGSELCRQILKfnpkkiilfsrdelklyeirqelREKFNDPKlRFFIVPVIGDVRDRERLERAMEQYGVDV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960513905   72 VIHLAAMvgglfrniK------YN-LDFWRKNVHMNDNVLHSAFEVGARKVVsCLSTcifpDKTTYPI 132
Cdd:pfam02719  81 VFHAAAY--------KhvplveYNpMEAIKTNVLGTENVADAAIEAGVKKFV-LIST----DKAVNPT 135
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
16-318 9.83e-06

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: 46.53  E-value: 9.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKAIQK----------VVADGAGlPGEDWV-FVSSKDADLTDT----AQTRALFEKVQPTHVIHLAAMVG 80
Cdd:cd05248    2 IIVTGGAGFIGSNLVKalnergitdiLVVDNLS-NGEKFKnLVGLKIADYIDKddfkDWVRKGDENFKIEAIFHQGACSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  81 GLFRNIKYNLDfwrKNVHMNDNVLHSAFEVGARkVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSnfgYSYAKRMIDVQN 160
Cdd:cd05248   81 TTETDGKYMMD---NNYQYTKELLHYCLEKKIR-FIYASSAAVYGNGSLGFAEDIETPNLRPLNV---YGYSKLLFDQWA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 161 RAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIH------KVHLAKSSGSaltvWGTGNPRRQFIYSLDLAQLFI 234
Cdd:cd05248  154 RRHGKEVLSQVVGLRYFNVYGPREYHKGRMASVVFHLFNqikageKVKLFKSSDG----YADGEQLRDFVYVKDVVKVNL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 235 WVLReyNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTF----DTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQA 310
Cdd:cd05248  230 FFLE--NPSVSGIFNVGTGRARSFNDLASATFKALGKEVKIEYidfpEDLRGKYQSFTEADISKLRAAGYTKEFHSLEEG 307

                 ....*...
gi 960513905 311 VKETCAWF 318
Cdd:cd05248  308 VKDYVKNY 315
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
16-184 3.17e-05

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 45.05  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKA----------IQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRaLFEKVQPTHVIHLAAMVG-GLFR 84
Cdd:cd05240    1 ILVTGAAGGLGRLlarrlaasprVIGVDGLDRRRPPGSPPKVEYVRLDIRDPAAAD-VFREREADAVVHLAFILDpPRDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  85 NIKYNLdfwrkNVHMNDNVLHSAFEVGARKVVSCLSTCIF---PDkttypiDETMIH-NGPPH-NSNFGYSYAKRMIDVQ 159
Cdd:cd05240   80 AERHRI-----NVDGTQNVLDACAAAGVPRVVVTSSVAVYgahPD------NPAPLTeDAPLRgSPEFAYSRDKAEVEQL 148
                        170       180
                 ....*....|....*....|....*.
gi 960513905 160 NRAYFQQY-GCTFTAVIPTNVFGPHD 184
Cdd:cd05240  149 LAEFRRRHpELNVTVLRPATILGPGT 174
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
16-186 1.01e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 42.39  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKAIQK-----------VVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEkvQPTHVIHLAAMVGglfr 84
Cdd:cd05226    1 ILILGATGFIGRALARelleqghevtlLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQ--GVDVVIHLAGAPR---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  85 nikYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYpidetmihnGPPHNSNFgysYAKRMIDVqnRAYF 164
Cdd:cd05226   75 ---DTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDLHEE---------TEPSPSSP---YLAVKAKT--EAVL 137
                        170       180
                 ....*....|....*....|..
gi 960513905 165 QQYGCTFTAVIPTNVFGPHDNF 186
Cdd:cd05226  138 REASLPYTIVRPGVIYGDLARA 159
PRK07578 PRK07578
short chain dehydrogenase; Provisional
14-67 1.27e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 42.49  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 960513905  14 MRILVTGGSGLVGKAIQK-------VVADGAglpgedwvfvSSKD--ADLTDTAQTRALFEKV 67
Cdd:PRK07578   1 MKILVIGASGTIGRAVVAelskrheVITAGR----------SSGDvqVDITDPASIRALFEKV 53
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
16-125 1.53e-04

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 42.74  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKA-IQKVVADGAGLpgedWVFVSSKD----------------------ADLT------DTAQTRALFEK 66
Cdd:cd05263    1 VFVTGGTGFLGRHlVKRLLENGFKV----LVLVRSESlgeaherieeagleadrvrvleGDLTqpnlglSAAASRELAGK 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960513905  67 VqpTHVIHLAAmvggLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARK--VVSCLSTCIFP 125
Cdd:cd05263   77 V--DHVIHCAA----SYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRfhYVSTAYVAGNR 131
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
14-275 2.71e-04

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: 41.89  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  14 MRILVTGGSGLVGKAI-QKVVADGAGLpgedwvfvsskdadltdTAQTRALFEKVQPTHVIHLAA------MVGGLFRNI 86
Cdd:cd05265    1 MKILIIGGTRFIGKALvEELLAAGHDV-----------------TVFNRGRTKPDLPEGVEHIVGdrndrdALEELLGGE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  87 KYN--LDFW-RKNVHMNDnvLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNG--PPHNSNFGYSYAKRMIDvqnR 161
Cdd:cd05265   64 DFDvvVDTIaYTPRQVER--ALDAFKGRVKQYIFISSASVYLKPGRVITESTPLREPdaVGLSDPWDYGRGKRAAE---D 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 162 AYFQQYGCTFTAVIPTNVFGPHDNFniedgHVLPGLIHKVHLakssGSALTVWGTGNPRRQFIYSLDLAQLFIWVLrEYN 241
Cdd:cd05265  139 VLIEAAAFPYTIVRPPYIYGPGDYT-----GRLAYFFDRLAR----GRPILVPGDGHSLVQFIHVKDLARALLGAA-GNP 208
                        250       260       270
                 ....*....|....*....|....*....|....
gi 960513905 242 EVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEV 275
Cdd:cd05265  209 KAIGGIFNITGDEAVTWDELLEACAKALGKEAEI 242
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
16-83 3.21e-04

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.03  E-value: 3.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513905  16 ILVTGGSGLVGKAiqkvVADGAGLPGEDWVFVSSKD----ADLTDTAQTRALFEKVqpTHVIHLAAMVGGLF 83
Cdd:cd11731    1 IIVIGATGTIGLA----VAQLLSAHGHEVITAGRSSgdyqVDITDEASIKALFEKV--GHFDAIVSTAGDAE 66
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
15-268 7.02e-04

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 40.21  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAI--------QKVVA--------DGAGLPGEDWVFvsskdADLTDTAQTRALFEKVqpTHVIHLAAM 78
Cdd:COG0702    1 KILVTGATGFIGRRVvrallargHPVRAlvrdpekaAALAAAGVEVVQ-----GDLDDPESLAAALAGV--DAVFLLVPS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  79 VGGlfrnikynlDFWRKNVHMNDNVLHSAFEVGARKVVsCLSTCifpdkttypidetmihnGPPHNSNFGYSYAKRMIDv 158
Cdd:COG0702   74 GPG---------GDFAVDVEGARNLADAAKAAGVKRIV-YLSAL-----------------GADRDSPSPYLRAKAAVE- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905 159 qnrAYFQQYGCTFTAVIPTNVFGPHDNFniedghvLPGLIHKVHLakssgsaltVWGTGNPRRQFIYSLDLAQLFIWVLR 238
Cdd:COG0702  126 ---EALRASGLPYTILRPGWFMGNLLGF-------FERLRERGVL---------PLPAGDGRVQPIAVRDVAEAAAAALT 186
                        250       260       270
                 ....*....|....*....|....*....|
gi 960513905 239 EyNEVEPIILSVGEEDEVSIKEAAEAVVEA 268
Cdd:COG0702  187 D-PGHAGRTYELGGPEALTYAELAAILSEA 215
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
14-81 8.15e-04

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 40.45  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  14 MRILVTGGSGLVGKAI-QKVVADGAGL------------PGEDwVFVSSKDADLTDTAQTRALFEKVqPTHVIHLAAMVG 80
Cdd:cd05238    1 MKVLITGASGFVGQRLaERLLSDVPNErlilidvvspkaPSGA-PRVTQIAGDLAVPALIEALANGR-PDVVFHLAAIVS 78

                 .
gi 960513905  81 G 81
Cdd:cd05238   79 G 79
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
15-207 1.09e-03

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


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 40.42  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKA-IQKVVADG------AGL-PGEDWVFVSSKD-----ADLTDTAQTRALFEKVQPTHVIHLAAMVGG 81
Cdd:cd09813    1 SCLVVGGSGFLGRHlVEQLLRRGnptvhvFDIrPTFELDPSSSGRvqfhtGDLTDPQDLEKAFNEKGPNVVFHTASPDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  82 LFRNIkynldFWRKNVHMNDNVLHSAFEVGARKVVSCLS-TCIFPDKTTYPIDETMihngpPHNSNFGYSY------AKR 154
Cdd:cd09813   81 SNDDL-----YYKVNVQGTRNVIEACRKCGVKKLVYTSSaSVVFNGQDIINGDESL-----PYPDKHQDAYnetkalAEK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 960513905 155 MIDVQNRAYFQQYGCtftAVIPTNVFGPHDNfniedgHVLPGLIHKVHLAKSS 207
Cdd:cd09813  151 LVLKANDPESGLLTC---ALRPAGIFGPGDR------QLVPGLLKAAKNGKTK 194
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
52-313 2.74e-03

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 39.07  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   52 ADLTDTAQTRALFEKVQPTHVIHLAAM--VGGLFRNIKYnldFWRKNVHMNDNVLHSAFEVGARKVVSCLSTC---IFPD 126
Cdd:pfam16363  56 GDLTDSSNLVRLLAEVQPDEIYNLAAQshVDVSFEQPEY---TADTNVLGTLRLLEAIRSLGLEKKVRFYQAStseVYGK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  127 KTTYPIDETmihnGP--PHNSnfgYSYAKRMIDVQNRAYFQQYG---CTftaVIPTNVFGPH--DNFnieDGHVLPGLIH 199
Cdd:pfam16363 133 VQEVPQTET----TPfyPRSP---YAAAKLYADWIVVNYRESYGlfaCN---GILFNHESPRrgERF---VTRKITRGVA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  200 KVHLAKssGSALTVwGTGNPRRQFIYSLDLAQLfIWVLREYNEVEPIILSVGEedEVSIKE----AAEAVVEAMDFHGEV 275
Cdd:pfam16363 200 RIKLGK--QEKLYL-GNLDAKRDWGHARDYVEA-MWLMLQQDKPDDYVIATGE--THTVREfvekAFLELGLTITWEGKG 273
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 960513905  276 TFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKE 313
Cdd:pfam16363 274 EIGYFKASGKVHVLIDPRYFRPGEVDRLLGDPSKAKEE 311
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
16-108 3.30e-03

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 38.42  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  16 ILVTGGSGLVGKAI-QKVVADGAglpgedWVFVSSKD---------------------ADLTDTAQTRALFEKVQPTH-- 71
Cdd:cd05233    1 ALVTGASSGIGRAIaRRLAREGA------KVVLADRNeealaelaaiealggnavavqADVSDEEDVEALVEEALEEFgr 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960513905  72 ---VIHLAAmVGGLFRNIKYNLDFWRKNVHMNdnvLHSAF 108
Cdd:cd05233   75 ldiLVNNAG-IARPGPLEELTDEDWDRVLDVN---LTGVF 110
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
15-77 4.30e-03

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: 38.35  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905  15 RILVTGGSGLVGKAIQK-VVADGA------------GLPGEDWVFVSSKD-----ADLTDTAQTRALFEKVQPTHVIHLA 76
Cdd:cd05260    1 RALITGITGQDGSYLAEfLLEKGYevhgivrrsssfNTDRIDHLYINKDRitlhyGDLTDSSSLRRAIEKVRPDEIYHLA 80

                 .
gi 960513905  77 A 77
Cdd:cd05260   81 A 81
PRK12829 PRK12829
short chain dehydrogenase; Provisional
4-68 6.24e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 37.73  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513905   4 ATDMGEPQGSMRILVTGGSGLVGKAI---------QKVVAD---------GAGLPGEDwvfVSSKDADLTDTAQTRALFE 65
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIaeafaeagaRVHVCDvseaalaatAARLPGAK---VTATVADVADPAQVERVFD 78

                 ...
gi 960513905  66 KVQ 68
Cdd:PRK12829  79 TAV 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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