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Conserved domains on  [gi|1720410125|ref|XP_030109702|]
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UDP-glucose 4-epimerase isoform X2 [Mus musculus]

Protein Classification

NAD-dependent epimerase/dehydratase family protein( domain architecture ID 10787209)

NAD-dependent epimerase/dehydratase family protein such as UDP-glucose 4-epimerase GalE, which catalyzes the NAD-dependent interconversion of UDP-galactose and UDP-glucose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
1-228 5.06e-155

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


:

Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 432.90  E-value: 5.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGgCTNPYGKSKFFIEEMIRDLCRADtAWNAVLLRYFNPIGAHASGRIG 80
Cdd:COG1087   104 MREAGVKRFVFSSSAAVYGEPESVPITEDAPTN-PTNPYGRSKLMVEQILRDLARAY-GLRYVALRYFNPAGAHPSGRIG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDpQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:COG1087   182 ED-HGPPTHLIPLVLQVALGKREKLSVFGDDYPTPDGTCVRDYIHVVDLADAHVLALEYLLAGGGSEVFNLGTGRGYSVL 260
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGFGA 228
Cdd:COG1087   261 EVIDAFERVTGRPIPYEIAPRRPGDPAALVADSEKARRELGWKPKYDLEDIIADAWRWQQKNPNGYRD 328
 
Name Accession Description Interval E-value
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
1-228 5.06e-155

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 432.90  E-value: 5.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGgCTNPYGKSKFFIEEMIRDLCRADtAWNAVLLRYFNPIGAHASGRIG 80
Cdd:COG1087   104 MREAGVKRFVFSSSAAVYGEPESVPITEDAPTN-PTNPYGRSKLMVEQILRDLARAY-GLRYVALRYFNPAGAHPSGRIG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDpQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:COG1087   182 ED-HGPPTHLIPLVLQVALGKREKLSVFGDDYPTPDGTCVRDYIHVVDLADAHVLALEYLLAGGGSEVFNLGTGRGYSVL 260
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGFGA 228
Cdd:COG1087   261 EVIDAFERVTGRPIPYEIAPRRPGDPAALVADSEKARRELGWKPKYDLEDIIADAWRWQQKNPNGYRD 328
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
1-220 3.49e-148

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: 415.40  E-value: 3.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGgCTNPYGKSKFFIEEMIRDLCRADTaWNAVLLRYFNPIGAHASGRIG 80
Cdd:cd05247   107 MRAHGVKNFVFSSSAAVYGEPETVPITEEAPLN-PTNPYGRTKLMVEQILRDLAKAPG-LNYVILRYFNPAGAHPSGLIG 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQgIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:cd05247   185 EDPQ-IPNNLIPYVLQVALGRREKLAIFGDDYPTPDGTCVRDYIHVVDLADAHVLALEKLENGGGSEIYNLGTGRGYSVL 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQK 220
Cdd:cd05247   264 EVVEAFEKVSGKPIPYEIAPRRAGDPASLVADPSKAREELGWKPKRDLEDMCEDAWNWQS 323
PLN02240 PLN02240
UDP-glucose 4-epimerase
1-230 6.93e-147

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 413.21  E-value: 6.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIG 80
Cdd:PLN02240  119 MAKHGCKKLVFSSSATVYGQPEEVPCTEEFPLSA-TNPYGRTKLFIEEICRDIHASDPEWKIILLRYFNPVGAHPSGRIG 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQC--GCRTYNLGTGTGYS 158
Cdd:PLN02240  198 EDPKGIPNNLMPYVQQVAVGRRPELTVFGNDYPTKDGTGVRDYIHVMDLADGHIAALRKLFTDPdiGCEAYNLGTGKGTS 277
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720410125 159 VLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGFGAQA 230
Cdd:PLN02240  278 VLEMVAAFEKASGKKIPLKLAPRRPGDAEEVYASTEKAEKELGWKAKYGIDEMCRDQWNWASKNPYGYGSSP 349
galE TIGR01179
UDP-glucose-4-epimerase GalE; Alternate name: UDPgalactose 4-epimerase This enzyme ...
1-222 5.74e-114

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


Pssm-ID: 273487 [Multi-domain]  Cd Length: 328  Bit Score: 328.92  E-value: 5.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIG 80
Cdd:TIGR01179 108 MQQAGVKKFIFSSSAAVYGEPSSIPISEDSPLGP-INPYGRSKLMSEQILRDLQKADPDWSYVILRYFNVAGAHPSGDIG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQGIPNnLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:TIGR01179 187 EDPPGITH-LIPYACQVAVGKRDKLTIFGTDYPTPDGTCVRDYIHVMDLADAHLAALEYLLNGGGSHVYNLGYGQGFSVL 265
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALG-LDRMCEDLWRWQKQN 222
Cdd:TIGR01179 266 EVIEAFKKVSGKDFPVELAPRRPGDPASLVADASKIRRELGWQPKYTdLEEIIKDAWRWESRN 328
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
1-215 4.22e-33

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 121.50  E-value: 4.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKN---LVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWnAVLLRYFNpigaHASG 77
Cdd:pfam16363 110 IRSLGLEKkvrFYQASTSEVYGKVQEVPQTETTPFYP-RSPYAAAKLYADWIVVNYRESYGLF-ACNGILFN----HESP 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  78 RIGEdpQGIPNNLMPYVSQVAIGRREALnVFGDDYATEDGTGVRDYIHVVDLAkghiaaLKKLKEqcgcRTYNLGTGTGY 157
Cdd:pfam16363 184 RRGE--RFVTRKITRGVARIKLGKQEKL-YLGNLDAKRDWGHARDYVEAMWLM------LQQDKP----DDYVIATGETH 250
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410125 158 SVLQMVQ------------------AMEKASGK-KIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDL 215
Cdd:pfam16363 251 TVREFVEkaflelgltitwegkgeiGYFKASGKvHVLIDPRYFRPGEVDRLLGDPSKAKEELGWKPKVSFEELVREM 327
 
Name Accession Description Interval E-value
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
1-228 5.06e-155

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 432.90  E-value: 5.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGgCTNPYGKSKFFIEEMIRDLCRADtAWNAVLLRYFNPIGAHASGRIG 80
Cdd:COG1087   104 MREAGVKRFVFSSSAAVYGEPESVPITEDAPTN-PTNPYGRSKLMVEQILRDLARAY-GLRYVALRYFNPAGAHPSGRIG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDpQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:COG1087   182 ED-HGPPTHLIPLVLQVALGKREKLSVFGDDYPTPDGTCVRDYIHVVDLADAHVLALEYLLAGGGSEVFNLGTGRGYSVL 260
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGFGA 228
Cdd:COG1087   261 EVIDAFERVTGRPIPYEIAPRRPGDPAALVADSEKARRELGWKPKYDLEDIIADAWRWQQKNPNGYRD 328
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
1-220 3.49e-148

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: 415.40  E-value: 3.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGgCTNPYGKSKFFIEEMIRDLCRADTaWNAVLLRYFNPIGAHASGRIG 80
Cdd:cd05247   107 MRAHGVKNFVFSSSAAVYGEPETVPITEEAPLN-PTNPYGRTKLMVEQILRDLAKAPG-LNYVILRYFNPAGAHPSGLIG 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQgIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:cd05247   185 EDPQ-IPNNLIPYVLQVALGRREKLAIFGDDYPTPDGTCVRDYIHVVDLADAHVLALEKLENGGGSEIYNLGTGRGYSVL 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQK 220
Cdd:cd05247   264 EVVEAFEKVSGKPIPYEIAPRRAGDPASLVADPSKAREELGWKPKRDLEDMCEDAWNWQS 323
PLN02240 PLN02240
UDP-glucose 4-epimerase
1-230 6.93e-147

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 413.21  E-value: 6.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIG 80
Cdd:PLN02240  119 MAKHGCKKLVFSSSATVYGQPEEVPCTEEFPLSA-TNPYGRTKLFIEEICRDIHASDPEWKIILLRYFNPVGAHPSGRIG 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQC--GCRTYNLGTGTGYS 158
Cdd:PLN02240  198 EDPKGIPNNLMPYVQQVAVGRRPELTVFGNDYPTKDGTGVRDYIHVMDLADGHIAALRKLFTDPdiGCEAYNLGTGKGTS 277
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720410125 159 VLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGFGAQA 230
Cdd:PLN02240  278 VLEMVAAFEKASGKKIPLKLAPRRPGDAEEVYASTEKAEKELGWKAKYGIDEMCRDQWNWASKNPYGYGSSP 349
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
1-226 1.91e-117

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 338.33  E-value: 1.91e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIG 80
Cdd:PRK10675  111 MRAANVKNLIFSSSATVYGDQPKIPYVESFPTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQGIPNNLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:PRK10675  191 EDPQGIPNNLMPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVAAMEKLANKPGVHIYNLGAGVGSSVL 270
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQNPSGF 226
Cdd:PRK10675  271 DVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGY 336
galE TIGR01179
UDP-glucose-4-epimerase GalE; Alternate name: UDPgalactose 4-epimerase This enzyme ...
1-222 5.74e-114

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


Pssm-ID: 273487 [Multi-domain]  Cd Length: 328  Bit Score: 328.92  E-value: 5.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIG 80
Cdd:TIGR01179 108 MQQAGVKKFIFSSSAAVYGEPSSIPISEDSPLGP-INPYGRSKLMSEQILRDLQKADPDWSYVILRYFNVAGAHPSGDIG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 EDPQGIPNnLMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:TIGR01179 187 EDPPGITH-LIPYACQVAVGKRDKLTIFGTDYPTPDGTCVRDYIHVMDLADAHLAALEYLLNGGGSHVYNLGYGQGFSVL 265
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720410125 161 QMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALG-LDRMCEDLWRWQKQN 222
Cdd:TIGR01179 266 EVIEAFKKVSGKDFPVELAPRRPGDPASLVADASKIRRELGWQPKYTdLEEIIKDAWRWESRN 328
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
1-221 6.91e-40

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 138.57  E-value: 6.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQyLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADtAWNAVLLRYFNPIGAHASGRIg 80
Cdd:COG0451   100 ARAAGVKRFVYASSSSVYGDGE-GPIDEDTPLRP-VSPYGASKLAAELLARAYARRY-GLPVTILRPGNVYGPGDRGVL- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  81 edpqgipNNLMPyvsqvAIGRREALNVFGddyateDGTGVRDYIHVVDLAKGHIAALKklKEQCGCRTYNLGTGTGYSVL 160
Cdd:COG0451   176 -------PRLIR-----RALAGEPVPVFG------DGDQRRDFIHVDDVARAIVLALE--APAAPGGVYNVGGGEPVTLR 235
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410125 161 QMVQAMEKASGKKIPYkVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQ 221
Cdd:COG0451   236 ELAEAIAEALGRPPEI-VYPARPGDVRPRRADNSKARRELGWRPRTSLEEGLRETVAWYRA 295
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
1-215 4.22e-33

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 121.50  E-value: 4.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKN---LVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRADTAWnAVLLRYFNpigaHASG 77
Cdd:pfam16363 110 IRSLGLEKkvrFYQASTSEVYGKVQEVPQTETTPFYP-RSPYAAAKLYADWIVVNYRESYGLF-ACNGILFN----HESP 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  78 RIGEdpQGIPNNLMPYVSQVAIGRREALnVFGDDYATEDGTGVRDYIHVVDLAkghiaaLKKLKEqcgcRTYNLGTGTGY 157
Cdd:pfam16363 184 RRGE--RFVTRKITRGVARIKLGKQEKL-YLGNLDAKRDWGHARDYVEAMWLM------LQQDKP----DDYVIATGETH 250
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410125 158 SVLQMVQ------------------AMEKASGK-KIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDL 215
Cdd:pfam16363 251 TVREFVEkaflelgltitwegkgeiGYFKASGKvHVLIDPRYFRPGEVDRLLGDPSKAKEELGWKPKVSFEELVREM 327
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
1-218 2.03e-31

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: 116.65  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVF-SSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRdLCRADTAWNAVLLRYFNPIGAhasgri 79
Cdd:cd05264   100 CAAAGIGKIIFaSSGGTVYGVPEQLPISESDPTLP-ISSYGISKLAIEKYLR-LYQYLYGLDYTVLRISNPYGP------ 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  80 GEDPQGIpnnlmpyvsQVAIG-------RREALNVFGDdyatedGTGVRDYIHVVDLAKGHIAALKKLKEqcgCRTYNLG 152
Cdd:cd05264   172 GQRPDGK---------QGVIPialnkilRGEPIEIWGD------GESIRDYIYIDDLVEALMALLRSKGL---EEVFNIG 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410125 153 TGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRW 218
Cdd:cd05264   234 SGIGYSLAELIAEIEKVTGRSVQVIYTPARTTDVPKIVLDISRARAELGWSPKISLEDGLEKTWQW 299
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
1-218 5.45e-30

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: 113.08  E-value: 5.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPtGGCTNPYGKSKFFIEEMIRdlcradtAWN------AVLLRYFNPIGAh 74
Cdd:cd05256   104 ARKAGVKRFVYASSSSVYGDPPYLPKDEDHP-PNPLSPYAVSKYAGELYCQ-------VFArlyglpTVSLRYFNVYGP- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  75 asgriGEDPQGIPNNLMP-YVSQVAIGrrEALNVFGDdyatedGTGVRDYIHVVDLAKGHIAALK-KLKEQcgcrTYNLG 152
Cdd:cd05256   175 -----RQDPNGGYAAVIPiFIERALKG--EPPTIYGD------GEQTRDFTYVEDVVEANLLAATaGAGGE----VYNIG 237
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410125 153 TGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRW 218
Cdd:cd05256   238 TGKRTSVNELAELIREILGKELEPVYAPPRPGDVRHSLADISKAKKLLGWEPKVSFEEGLRLTVEW 303
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
1-152 4.99e-28

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: 105.07  E-value: 4.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTgGCTNPYGKSKFFIEEMIRDLCRADTaWNAVLLRYFNPIGAHASGRig 80
Cdd:cd08946    68 ARKAGVKRFVYASSASVYGSPEGLPEEEETPP-RPLSPYGVSKLAAEHLLRSYGESYG-LPVVILRLANVYGPGQRPR-- 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720410125  81 edpqgiPNNLMPYVSQVAIGRREaLNVFGddyateDGTGVRDYIHVVDLAKGHIAALKklKEQCGCRTYNLG 152
Cdd:cd08946   144 ------LDGVVNDFIRRALEGKP-LTVFG------GGNQTRDFIHVDDVVRAILHALE--NPLEGGGVYNIG 200
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
1-152 1.52e-25

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 99.68  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGC--TNPYGKSKFFIEEMIRDLCRADtAWNAVLLRYFNPIGAHasgr 78
Cdd:pfam01370 102 ARKAGVKRFLFASSSEVYGDGAEIPQEETTLTGPLapNSPYAAAKLAGEWLVLAYAAAY-GLRAVILRLFNVYGPG---- 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720410125  79 igeDPQGIPNNLMPYVSQvAIGRREALNVFGddyateDGTGVRDYIHVVDLAKGHIAALKKLKEQcgCRTYNLG 152
Cdd:pfam01370 177 ---DNEGFVSRVIPALIR-RILEGKPILLWG------DGTQRRDFLYVDDVARAILLALEHGAVK--GEIYNIG 238
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
5-222 1.13e-18

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: 82.73  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   5 GVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTN---PYGKSKFFIEEMIRDLCRADTAwNAVLLRYFNPIGAHASGRige 81
Cdd:cd05257   110 YRKRVVHTSTSEVYGTAQDVPIDEDHPLLYINKprsPYSASKQGADRLAYSYGRSFGL-PVTIIRPFNTYGPRQSAR--- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  82 dpQGIPNnlmpYVSQVAIGRREALNVfgddyateDGTGVRDYIHVVDLAKGHIAALkkLKEQCGCRTYNLGTGTGYSV-- 159
Cdd:cd05257   186 --AVIPT----IISQRAIGQRLINLG--------DGSPTRDFNFVKDTARGFIDIL--DAIEAVGEIINNGSGEEISIgn 249
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410125 160 -LQMVQAMEKASGKKIPYKVVAR-REG--DVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQN 222
Cdd:cd05257   250 pAVELIVEELGEMVLIVYDDHREyRPGysEVERRIPDIRKAKRLLGWEPKYSLRDGLRETIEWFKDQ 316
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
1-222 1.34e-18

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


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 82.77  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMirdlcrADT-----AWNAVLLRYFNPIGaha 75
Cdd:cd05253   114 CRHFGVKHLVYASSSSVYGLNTKMPFSEDDRVDHPISLYAATKKANELM------AHTyshlyGIPTTGLRFFTVYG--- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  76 sgrigedPQGIPNnlMPYVSQV-AIGRREALNVFGddyateDGTGVRDYIHVVDLAKGHIAALKKLKEQCGC-------- 146
Cdd:cd05253   185 -------PWGRPD--MALFLFTkAILEGKPIDVFN------DGNMSRDFTYIDDIVEGVVRALDTPAKPNPNwdaeapdp 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125 147 -------RTYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAAL----GLDRMCEdl 215
Cdd:cd05253   250 stssapyRVYNIGNNSPVKLMDFIEALEKALGKKAKKNYLPMQKGDVPETYADISKLQRLLGYKPKTsleeGVKRFVE-- 327

                  ....*..
gi 1720410125 216 wrWQKQN 222
Cdd:cd05253   328 --WYKEN 332
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
2-224 1.82e-15

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 73.97  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   2 RAHGV--KNLVFSSSATVYGN-PQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRdlcradtAW------NAVLLRYFNPIG 72
Cdd:COG1088   114 RKYWVegFRFHHVSTDEVYGSlGEDGPFTETTPLDP-SSPYSASKAASDHLVR-------AYhrtyglPVVITRCSNNYG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  73 AHASgrigedpqgiPNNLMPYVSQVAI-GRReaLNVFGDdyatedGTGVRDYIHVVDLAKGHIAALKKLKeqCGcRTYNL 151
Cdd:COG1088   186 PYQF----------PEKLIPLFITNALeGKP--LPVYGD------GKQVRDWLYVEDHCRAIDLVLEKGR--PG-ETYNI 244
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720410125 152 GTGTGYSVLQMVQAMEKASGK-KIPYKVVARREGDVaACYA-NPSLAHEELGWTAALGLDRMCEDLWRWQKQNPS 224
Cdd:COG1088   245 GGGNELSNLEVVELICDLLGKpESLITFVKDRPGHD-RRYAiDASKIRRELGWKPKVTFEEGLRKTVDWYLDNRD 318
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
1-177 8.35e-15

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


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 71.95  E-value: 8.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCRAD--TAWnavLLRYFNPIGAHASGR 78
Cdd:cd05234   105 MRANGVKRIVFASSSTVYGEAKVIPTPEDYPPLP-ISVYGASKLAAEALISAYAHLFgfQAW---IFRFANIVGPRSTHG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  79 IGEDpqgipnnlmpYVSQVAiGRREALNVFGddyateDGTGVRDYIHVVDLAKGHIAALKKLKEqcGCRTYNLGTGTGYS 158
Cdd:cd05234   181 VIYD----------FINKLK-RNPNELEVLG------DGRQRKSYLYVSDCVDAMLLAWEKSTE--GVNIFNLGNDDTIS 241
                         170
                  ....*....|....*....
gi 1720410125 159 VLQMVQAMEKASGKKIPYK 177
Cdd:cd05234   242 VNEIAEIVIEELGLKPRFK 260
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
1-219 3.84e-13

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


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 67.31  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVK-NLVFSSSATVYGN-PQYLPL-------------------DEAHPTGGCTNPYGKSKFFIEEMIRDLCRAdTA 59
Cdd:cd05258   111 ARQHAPNaPFIFTSTNKVYGDlPNYLPLeeletryelapegwspagiSESFPLDFSHSLYGASKGAADQYVQEYGRI-FG 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  60 WNAVLLRYFNPIGAHASGRigEDpQGIPNNLMpyvsQVAIgRREALNVFGDDyatedGTGVRDYIHVVDLAKGHIAALKK 139
Cdd:cd05258   190 LKTVVFRCGCLTGPRQFGT--ED-QGWVAYFL----KCAV-TGKPLTIFGYG-----GKQVRDVLHSADLVNLYLRQFQN 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125 140 LKEQCGcRTYNLGTGTGYSV--LQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWR 217
Cdd:cd05258   257 PDRRKG-EVFNIGGGRENSVslLELIALCEEITGRKMESYKDENRPGDQIWYISDIRKIKEKPGWKPERDPREILAEIYA 335

                  ..
gi 1720410125 218 WQ 219
Cdd:cd05258   336 WI 337
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
2-173 6.98e-12

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: 63.48  E-value: 6.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   2 RAHGVKnLVFSSSATVYGN--PQYLPlDEAHPTGGCTNPYGKSKFFIEEMIRDLCRADTaWNAVLLRYFNPIGAHA--SG 77
Cdd:cd05248   105 LEKKIR-FIYASSAAVYGNgsLGFAE-DIETPNLRPLNVYGYSKLLFDQWARRHGKEVL-SQVVGLRYFNVYGPREyhKG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  78 RIGEdpqgipnnlMPYVSQVAIGRREALNVFGDDYATEDGTGVRDYIHVVDLAKghiAALKKLKEQCGCRTYNLGTGTGY 157
Cdd:cd05248   182 RMAS---------VVFHLFNQIKAGEKVKLFKSSDGYADGEQLRDFVYVKDVVK---VNLFFLENPSVSGIFNVGTGRAR 249
                         170
                  ....*....|....*.
gi 1720410125 158 SVLQMVQAMEKASGKK 173
Cdd:cd05248   250 SFNDLASATFKALGKE 265
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
1-219 1.91e-10

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: 59.53  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVK-NLVFSSSATVYGNPQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRdLCRADTAWNAVLLRYFNpigaHASGRI 79
Cdd:cd05260   110 IRILGLDaRFYQASSSEEYGKVQELPQSETTPFRP-RSPYAVSKLYADWITR-NYREAYGLFAVNGRLFN----HEGPRR 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  80 GED--PQGIpnnlmpyVSQVA---IGRREAL---NVfgddyatedgTGVRDYIHVVDLAKGHIAALKKLKEQcgcrTYNL 151
Cdd:cd05260   184 GETfvTRKI-------TRQVArikAGLQPVLklgNL----------DAKRDWGDARDYVEAYWLLLQQGEPD----DYVI 242
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720410125 152 GTGTGYSVLQMV-QAMEKASGKKIPYKVV--AR-REGDVAACYANPSLAHEELGWTAALGLdrmcEDLWRWQ 219
Cdd:cd05260   243 ATGETHSVREFVeLAFEESGLTGDIEVEIdpRYfRPTEVDLLLGDPSKAREELGWKPEVSF----EELVREM 310
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
2-222 5.85e-09

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: 55.18  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   2 RAHGVKNLVFSSSATVYgnPQYL-------PLDE-----AHPTGGctnpYGKSKFFIEEmirdLCRA---DTAWNAVLLR 66
Cdd:cd05273   104 RINGVERFLFASSACVY--PEFKqlettvvRLREedawpAEPQDA----YGWEKLATER----LCQHyneDYGIETRIVR 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  67 YFN---PIGAHASGRigedpqgipnNLMPyvsqVAIGRREALNVFGDDYAT-EDGTGVRDYIHVVDLAKGhiaaLKKLKE 142
Cdd:cd05273   174 FHNiygPRGTWDGGR----------EKAP----AAMCRKVATAKDGDRFEIwGDGLQTRSFTYIDDCVEG----LRRLME 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125 143 QCGCRTYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGWTAALGLDRMCEDLWRWQKQN 222
Cdd:cd05273   236 SDFGEPVNLGSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVRGRNSDNTLLKEELGWEPNTPLEEGLRITYFWIKEQ 315
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
2-208 3.76e-08

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: 52.50  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   2 RAHGVKNLVFSSSATVYGNP---QYLPLDeaHPTGGCTNPYGKSKFFIEE--MIRDLcradtawNAVLLRYFNPIGahas 76
Cdd:cd08957   104 KKAGVKRLIYFQTALCYGLKpmqQPIRLD--HPRAPPGSSYAISKTAGEYylELSGV-------DFVTFRLANVTG---- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  77 grigedPQGIPNNLMPYVSQVAIGRrealNVFGDDyatedgtGVRDYIHVVDLAKghiAALKKLKEQCGCRTYNLGTGTG 156
Cdd:cd08957   171 ------PRNVIGPLPTFYQRLKAGK----KCFVTD-------TRRDFVFVKDLAR---VVDKALDGIRGHGAYHFSSGED 230
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410125 157 YSVLQM----VQAMEKASGKKIPykVVARREGDVAACYANPSLAHEELGWTAALGL 208
Cdd:cd08957   231 VSIKELfdavVEALDLPLRPEVE--VVELGPDDVPSILLDPSRTFQDFGWKEFTPL 284
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
2-224 7.22e-08

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: 51.78  E-value: 7.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   2 RAHGVKNLVFSSSATVYGN-PQYLPLDEAHPTGGcTNPYGKSKFFIEEMIRdlcradtAW------NAVLLRYFNPIGah 74
Cdd:cd05246   113 RKYGVKRFVHISTDEVYGDlLDDGEFTETSPLAP-TSPYSASKAAADLLVR-------AYhrtyglPVVITRCSNNYG-- 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  75 asgrigedPQGIPNNLMP-YVSQVAIGRReaLNVFGDdyatedGTGVRDYIHVVDLAKGHIAALKKLKEqcGcRTYNLGT 153
Cdd:cd05246   183 --------PYQFPEKLIPlFILNALDGKP--LPIYGD------GLNVRDWLYVEDHARAIELVLEKGRV--G-EIYNIGG 243
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410125 154 GTGYSVLQMVQAMEKASGKKIPY-KVVARREG-DVAacYA-NPSLAHEELGWTAAL----GLDRMCedlwRWQKQNPS 224
Cdd:cd05246   244 GNELTNLELVKLILELLGKDESLiTYVKDRPGhDRR--YAiDSSKIRRELGWRPKVsfeeGLRKTV----RWYLENRW 315
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
1-75 2.80e-07

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: 50.06  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   1 MRAHGVKNLVFSSSATVYG----NPqyLPLDEAHPTGGCTN-PYGKSKFFIEEMIRDLCRADTAWNAVLLRYFNPIGAHA 75
Cdd:cd05240    97 CAAAGVPRVVVTSSVAVYGahpdNP--APLTEDAPLRGSPEfAYSRDKAEVEQLLAEFRRRHPELNVTVLRPATILGPGT 174
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
1-66 1.41e-05

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: 45.07  E-value: 1.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410125   1 MRAHG-VKNLVFSSSATVYG-NPQYLPLDEAHPTGgcTNPYGKSKFFIEEMIRDLCRADTAWNAVLLR 66
Cdd:cd05238   103 LRKNGpKPRFVFTSSLAVYGlPLPNPVTDHTALDP--ASSYGAQKAMCELLLNDYSRRGFVDGRTLRL 168
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
3-162 1.42e-05

Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 45.09  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   3 AHgVKNLVFSSSATVYGNPQYLPLDEAHpTGGCTNPYGKSKFfIEEMIRDLCRADTAWNAVLLRYFNPIGAHasgrigED 82
Cdd:PRK15181  131 AH-VSSFTYAASSSTYGDHPDLPKIEER-IGRPLSPYAVTKY-VNELYADVFARSYEFNAIGLRYFNVFGRR------QN 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  83 PQGIPNNLMPyvsqvaigrREALNVFGDD--YATEDGTGVRDYIHVVDLAKGHIAALKKLKEQCGCRTYNLGTGTGYSVL 160
Cdd:PRK15181  202 PNGAYSAVIP---------RWILSLLKDEpiYINGDGSTSRDFCYIENVIQANLLSATTNDLASKNKVYNVAVGDRTSLN 272

                  ..
gi 1720410125 161 QM 162
Cdd:PRK15181  273 EL 274
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
9-215 4.94e-05

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


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 43.39  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   9 LVFSSSATVYGNPqylpldEAHPTG----GCTNP------YGKSKFFIEEMIRDLCRADTAwNAVLLRYFNPIGA--HAS 76
Cdd:cd05230   109 VLLASTSEVYGDP------EVHPQPesywGNVNPigprscYDEGKRVAETLCMAYHRQHGV-DVRIARIFNTYGPrmHPN 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  77 -GRIgedpqgIPNnlmpYVSQvAIgRREALNVFGddyateDGTGVRDYIHVVDLAKGHIaALKKLKEQCGcrTYNLGTGT 155
Cdd:cd05230   182 dGRV------VSN----FIVQ-AL-RGEPITVYG------DGTQTRSFQYVSDLVEGLI-RLMNSDYFGG--PVNLGNPE 240
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720410125 156 GYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAHEELGW--TAAL--GLDRMCEDL 215
Cdd:cd05230   241 EFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKELLGWepKVPLeeGLRRTIEYF 304
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-209 1.49e-04

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 41.95  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125   3 AHGVKNLVFSSSATVYGNP-QYLPLDEAHPTGGcTNPYGKSKFFIEEMIRDLCrADTAWNAVLLRYfnPI--GAHASGRI 79
Cdd:cd05232    99 RQGVKRFVFLSSVKVNGEGtVGAPFDETDPPAP-QDAYGRSKLEAERALLELG-ASDGMEVVILRP--PMvyGPGVRGNF 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410125  80 GEDPQ----GIPnnLMPYVSQvaiGRREALNVFgddyatedgtgvrdyiHVVDLAkGHIAALKKLKEQcgcrTYNLGTGT 155
Cdd:cd05232   175 ARLMRlidrGLP--LPPGAVK---NRRSLVSLD----------------NLVDAI-YLCISLPKAANG----TFLVSDGP 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720410125 156 GYSVLQMVQAMEKASGKK--------IPYKVVARREGDVAACYA-------NPSLAHEELGWTAALGLD 209
Cdd:cd05232   229 PVSTAELVDEIRRALGKPtrllpvpaGLLRFAAKLLGKRAVIQRlfgslqyDPEKTQNELGWRPPISLE 297
 
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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