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Conserved domains on  [gi|224009534|ref|XP_002293725|]
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udp-d-glucose 6-dehydrogenase [Thalassiosira pseudonana CCMP1335]

Protein Classification

UDP-glucose 6-dehydrogenase( domain architecture ID 11476687)

UDP-glucose 6-dehydrogenase is involved in the biosynthesis of glycosaminoglycans, hyaluronan, chondroitin sulfate, and heparan sulfate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
6-472 0e+00

probable UDP-glucose 6-dehydrogenase


:

Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 906.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   6 DLKICCMGAGYVGGPTMAVIAANCPKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSEIKKAD 85
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  86 IIFISVNTPTKTMGIGAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLDCNEKGLKFQVLSNPEFLA 165
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 166 EGTAIPDLMKPDRVLIGGVQSPEGLAAAETLVSVYANWVPREQIITTNLWSSELSKLVANAFLAQRVSSINSISALCEAT 245
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 246 GADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNECAKYWNQVIVMNDYQKKRFSEKMVSHMFN 325
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 326 TVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEM-------DYTVQMSESThPGLEAA 398
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLsmnkfdwDHPRHLQPMS-PTAVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224009534 399 VTTSPDAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPAFVFDGRNILDHEKLRGMGFEVHAIGKPDPNKF 472
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
6-472 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 906.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   6 DLKICCMGAGYVGGPTMAVIAANCPKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSEIKKAD 85
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  86 IIFISVNTPTKTMGIGAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLDCNEKGLKFQVLSNPEFLA 165
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 166 EGTAIPDLMKPDRVLIGGVQSPEGLAAAETLVSVYANWVPREQIITTNLWSSELSKLVANAFLAQRVSSINSISALCEAT 245
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 246 GADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNECAKYWNQVIVMNDYQKKRFSEKMVSHMFN 325
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 326 TVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEM-------DYTVQMSESThPGLEAA 398
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLsmnkfdwDHPRHLQPMS-PTAVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224009534 399 VTTSPDAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPAFVFDGRNILDHEKLRGMGFEVHAIGKPDPNKF 472
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
8-467 0e+00

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 539.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   8 KICCMGAGYVGGPTMAVIAANCPKVrVCVvDLSQKQIDAWNSPNLPIYEPGLPAVVDQCR-NKNLFFSTDIDSEIKKADI 86
Cdd:COG1004    2 KIAVIGTGYVGLVTAACLAELGHEV-TCV-DIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  87 IFISVNTPTKTMGigagrAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLD--CNEKGLKFQVLSNPEFL 164
Cdd:COG1004   80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAeeLRGAGVDFDVVSNPEFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 165 AEGTAIPDLMKPDRVLIGGvqspEGLAAAETLVSVYANWVPRE-QIITTNLWSSELSKLVANAFLAQRVSSINSISALCE 243
Cdd:COG1004  155 REGSAVEDFLRPDRIVIGV----DSERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 244 ATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNecAKYWNQVIVMNDYQKKRFSEKMVSHM 323
Cdd:COG1004  231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 324 FNTVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVsredmfsemdytvqmSESTHPGLEAAVTTSP 403
Cdd:COG1004  309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVA---------------MENARRLLPDDITYAD 373
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224009534 404 DAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPAfVFDGRNILDHEKLRGMGFEVHAIGKP 467
Cdd:COG1004  374 DAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
8-447 1.08e-106

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 323.02  E-value: 1.08e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534    8 KICCMGAGYVGGPTMAVIAANcpKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLF-FSTDIDSEIKKADI 86
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   87 IFISVNTPTKTMGigagrAANVKNCELCARKIAEVSESGKIVVEKSTVPVRT-AQAVRRVLDCNEK--GLKFQVLSNPEF 163
Cdd:TIGR03026  80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTtEEVVKPILERSGLklGEDFYLAYNPEF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  164 LAEGTAIPDLMKPDRVlIGGVQSpeglAAAETLVSVYANWVpREQIITTNLWSSELSKLVANAFLAQRVSSINSISALCE 243
Cdd:TIGR03026 155 LREGNAVHDLLHPDRI-VGGETE----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  244 ATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNecAKYWNQVIVMNDYQKKRFSEKMVSHM 323
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  324 FNtVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEMDYtvqmsesthpgleaavttsP 403
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSI-------------------D 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 224009534  404 DAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPaFVFDGRN 447
Cdd:TIGR03026 367 DLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
8-194 1.60e-64

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 206.33  E-value: 1.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534    8 KICCMGAGYVGGPTMAVIAANCPKVrVCVvDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSEIKKADII 87
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIGHDV-IGV-DIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   88 FISVNTPTKTmgigAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAV--RRVLDCNEK-GLKFQVLSNPEFL 164
Cdd:pfam03721  80 FIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKvGVDFDVASNPEFL 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 224009534  165 AEGTAIPDLMKPDRVLIGGVQSPEGLAAAE 194
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
333-450 5.03e-29

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 109.52  E-value: 5.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   333 AVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMfsemdytvqmsesthpglEAAVTTSPDAYAACDGA 412
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR------------------EYGLTYVSDLEEALKGA 62
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 224009534   413 HAFAVLTEWDEFKDLDFERIYKSMAKPaFVFDGRNILD 450
Cdd:smart00984  63 DAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
6-472 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 906.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   6 DLKICCMGAGYVGGPTMAVIAANCPKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSEIKKAD 85
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  86 IIFISVNTPTKTMGIGAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLDCNEKGLKFQVLSNPEFLA 165
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 166 EGTAIPDLMKPDRVLIGGVQSPEGLAAAETLVSVYANWVPREQIITTNLWSSELSKLVANAFLAQRVSSINSISALCEAT 245
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 246 GADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNECAKYWNQVIVMNDYQKKRFSEKMVSHMFN 325
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 326 TVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEM-------DYTVQMSESThPGLEAA 398
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLsmnkfdwDHPRHLQPMS-PTAVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224009534 399 VTTSPDAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPAFVFDGRNILDHEKLRGMGFEVHAIGKPDPNKF 472
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
8-467 0e+00

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 539.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   8 KICCMGAGYVGGPTMAVIAANCPKVrVCVvDLSQKQIDAWNSPNLPIYEPGLPAVVDQCR-NKNLFFSTDIDSEIKKADI 86
Cdd:COG1004    2 KIAVIGTGYVGLVTAACLAELGHEV-TCV-DIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  87 IFISVNTPTKTMGigagrAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLD--CNEKGLKFQVLSNPEFL 164
Cdd:COG1004   80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAeeLRGAGVDFDVVSNPEFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 165 AEGTAIPDLMKPDRVLIGGvqspEGLAAAETLVSVYANWVPRE-QIITTNLWSSELSKLVANAFLAQRVSSINSISALCE 243
Cdd:COG1004  155 REGSAVEDFLRPDRIVIGV----DSERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 244 ATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNecAKYWNQVIVMNDYQKKRFSEKMVSHM 323
Cdd:COG1004  231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 324 FNTVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVsredmfsemdytvqmSESTHPGLEAAVTTSP 403
Cdd:COG1004  309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVA---------------MENARRLLPDDITYAD 373
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224009534 404 DAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPAfVFDGRNILDHEKLRGMGFEVHAIGKP 467
Cdd:COG1004  374 DAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
8-447 1.08e-106

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 323.02  E-value: 1.08e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534    8 KICCMGAGYVGGPTMAVIAANcpKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLF-FSTDIDSEIKKADI 86
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   87 IFISVNTPTKTMGigagrAANVKNCELCARKIAEVSESGKIVVEKSTVPVRT-AQAVRRVLDCNEK--GLKFQVLSNPEF 163
Cdd:TIGR03026  80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTtEEVVKPILERSGLklGEDFYLAYNPEF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  164 LAEGTAIPDLMKPDRVlIGGVQSpeglAAAETLVSVYANWVpREQIITTNLWSSELSKLVANAFLAQRVSSINSISALCE 243
Cdd:TIGR03026 155 LREGNAVHDLLHPDRI-VGGETE----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  244 ATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLNecAKYWNQVIVMNDYQKKRFSEKMVSHM 323
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  324 FNtVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEMDYtvqmsesthpgleaavttsP 403
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSI-------------------D 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 224009534  404 DAYAACDGAHAFAVLTEWDEFKDLDFERIYKSMAKPaFVFDGRN 447
Cdd:TIGR03026 367 DLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
8-194 1.60e-64

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 206.33  E-value: 1.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534    8 KICCMGAGYVGGPTMAVIAANCPKVrVCVvDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSEIKKADII 87
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIGHDV-IGV-DIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   88 FISVNTPTKTmgigAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAV--RRVLDCNEK-GLKFQVLSNPEFL 164
Cdd:pfam03721  80 FIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKvGVDFDVASNPEFL 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 224009534  165 AEGTAIPDLMKPDRVLIGGVQSPEGLAAAE 194
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
8-450 3.40e-45

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 162.92  E-value: 3.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   8 KICCMGAGYVGGPTMAVIAANcpKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIdSEIKKADII 87
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKA--GFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDP-EALAEADVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  88 FISVNTPtktmgIGAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVR-TAQAVRRVLdcnEK--GLK----FQVLSN 160
Cdd:COG0677   78 IIAVPTP-----LDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGtTEEVCVPIL---EKrsGLKagedFFLAYS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 161 PEFLAEGTAIPDLMKPDRVlIGGVqSPEGLAAAETLvsvYANWVPREQIITTNLWSSELSKLVANAF------LAqrvss 234
Cdd:COG0677  150 PERINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYrdvniaLA----- 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 235 iNSISALCEATGADVSEITRAVGMDdrigKRFLNSS--IGFGGSCFQKDILNLVYLCETYGLNEcakywnQVIVM----N 308
Cdd:COG0677  220 -NELALICDRLGIDVWEVIEAANTK----PGFLIFYpgPGVGGHCIPVDPYYLTWKARELGYHP------RLILAareiN 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 309 DYQKKRFSEKMVSHMFN---TVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDmfsemdytv 385
Cdd:COG0677  289 DSMPEYVVERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEE--------- 359
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224009534 386 qmsesthpgLEAAVTTSPDAYAACDGAHAFAVLTEWDEFKDLDFERIykSMAKPAFVFDGRNILD 450
Cdd:COG0677  360 ---------VEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
216-309 3.47e-39

UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 460015 [Multi-domain]  Cd Length: 92  Bit Score: 136.74  E-value: 3.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  216 SSELSKLVANAFLAQRVSSINSISALCEATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLVYLCETYGLN 295
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|....
gi 224009534  296 ecAKYWNQVIVMND 309
Cdd:pfam00984  81 --ARLLEAAREVNE 92
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
333-451 2.32e-31

UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 427462 [Multi-domain]  Cd Length: 103  Bit Score: 116.14  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  333 AVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSEMDytvqmsesthpgleaAVTTSPDAYAACDGA 412
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGD---------------GVTLVDDLEEALKGA 65
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 224009534  413 HAFAVLTEWDEFKDLDFERIYKsMAKPAFVFDGRNILDH 451
Cdd:pfam03720  66 DAIVILTDHDEFKSLDWEKLKK-LMKPPVVFDGRNVLDP 103
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
333-450 5.03e-29

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 109.52  E-value: 5.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   333 AVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMfsemdytvqmsesthpglEAAVTTSPDAYAACDGA 412
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR------------------EYGLTYVSDLEEALKGA 62
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 224009534   413 HAFAVLTEWDEFKDLDFERIYKSMAKPaFVFDGRNILD 450
Cdd:smart00984  63 DAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
7-286 1.45e-24

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 105.10  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   7 LKICCMGAGYVGGPTMAVIAANCpkvRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVdQCRNKNLFFSTDIDSEIKKADI 86
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQNH---EVVALDILPSRVAMLNDRISPIVDKEIQQFL-QSDKIHFNATLDKNEAYRDADY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  87 IFISvnTPT----KTmgigagRAANVKNCELCARKIAEVSESGKIVVeKSTVPVRTAQAVRRVLDCNekglkfQVLSNPE 162
Cdd:PRK15057  77 VIIA--TPTdydpKT------NYFNTSSVESVIKDVVEINPYAVMVI-KSTVPVGFTAAMHKKYRTE------NIIFSPE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 163 FLAEGTAIPDLMKPDRVLIGgvqspEGLAAAETLVSVYANWVPREQIIT--TNLWSSELSKLVANAFLAQRVSSINSISA 240
Cdd:PRK15057 142 FLREGKALYDNLHPSRIVIG-----ERSERAERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDS 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 224009534 241 LCEATGADVSEITRAVGMDDRIGKRFLNSSIGFGGSCFQKDILNLV 286
Cdd:PRK15057 217 YAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLL 262
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
1-432 2.65e-20

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 92.74  E-value: 2.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   1 MSdgFDlKICCMGAGYVGGPTMAVIAANcpKVRVCVVDLSQKQIDAWNSPNLPIYEPGLPAVVDQCRNKNLFFSTDIDSE 80
Cdd:PRK11064   1 MS--FE-TISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  81 ikkADIIFISVNTPTKtmgigAGRAANVKNCELCARKIAEVSESGKIVVEKSTVPVRTAQAVRRVLDCNEKGLKF----- 155
Cdd:PRK11064  76 ---ADAFLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFpqqag 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 156 -----QVLSNPEFLAEGTAIPDLMKPDRVlIGGVqSPEGLAAAetlVSVYANWVPREQIITtNLWSSELSKLVANAFLAQ 230
Cdd:PRK11064 148 eqadiNIAYCPERVLPGQVMVELIKNDRV-IGGM-TPVCSARA---SELYKIFLEGECVVT-NSRTAEMCKLTENSFRDV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 231 RVSSINSISALCEATGADVSEITRAVGMDDRIGkrFLNSSIGFGGSCFQKDILNLV-------YLCET-YGLNECAKYW- 301
Cdd:PRK11064 222 NIAFANELSLICADQGINVWELIRLANRHPRVN--ILQPGPGVGGHCIAVDPWFIVaqnpqqaRLIRTaREVNDGKPHWv 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 302 -NQV-------IVMNDyqkKRFSEKmvshmfntvtgkKIAVLGYAFKKDTGDVRETPSMFVVRDLV-LEQAKIHVYDPQV 372
Cdd:PRK11064 300 iDQVkaavadcLAATD---KRASEV------------KIACFGLAFKPNIDDLRESPAMEIAELIAqWHSGETLVVEPNI 364
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 373 srEDMFSEMDYTVQMSEsthpgLEAAVTTspdayaacdgAHAFAVLTEWDEFKDLDFERI 432
Cdd:PRK11064 365 --HQLPKKLDGLVTLVS-----LDEALAT----------ADVLVMLVDHSQFKAINGDNV 407
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
6-380 4.08e-12

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 67.79  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534   6 DLKICCMGAGYVGGPtmavIAANCPKVRVCV-VDLSQKQI-DAWNSPNLpiyepGLPAVVDQCRN-KNLFFSTDIDsEIK 82
Cdd:PRK15182   6 EVKIAIIGLGYVGLP----LAVEFGKSRQVVgFDVNKKRIlELKNGVDV-----NLETTEEELREaRYLKFTSEIE-KIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534  83 KADIIFISVNTPTKTMgigagRAANVKNCELCARKIAEVSESGKIVVEKSTV-PVRTAQAVRRVLdCNEKGLKFQ----V 157
Cdd:PRK15182  76 ECNFYIITVPTPINTY-----KQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPIL-ARMSGMTFNqdfyV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 158 LSNPEFLAEGTAIPDLMKPDRVLIGGVQSpeglaAAETLVSVYANWVPREQIITTNLWSSELSKLVANAFLAQRVSSINS 237
Cdd:PRK15182 150 GYSPERINPGDKKHRLTNIKKITSGSTAQ-----IAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009534 238 ISALCEATGADVSEITRAVGMDdrigKRFLNSSIGF-GGSCFQKDILNLVYLCETYGlnecakYWNQVIV----MNDYQK 312
Cdd:PRK15182 225 LAIIFNRLNIDTEAVLRAAGSK----WNFLPFRPGLvGGHCIGVDPYYLTHKSQGIG------YYPEIILagrrLNDNMG 294
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224009534 313 KRFSEKMVSHMFN---TVTGKKIAVLGYAFKKDTGDVRETPSMFVVRDLVLEQAKIHVYDPQVSREDMFSE 380
Cdd:PRK15182 295 NYVSEQLIKAMIKkgiNVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRRE 365
 
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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