NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15241704|ref|NP_198748|]
View 

UDP-glucose 6-dehydrogenase family protein [Arabidopsis thaliana]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-473 0e+00

probable UDP-glucose 6-dehydrogenase


:

Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 1097.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    1 MVKICCIGAGYVGGPTMAVIALKCPDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREAD 80
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   81 IVFVSVNTPTKTTGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKFQILSNPEFLA 160
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  161 EGTAIADLFNPDRVLIGGRETPEGFKAVQTLKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEST 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  241 GADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPEVAEYWKQVIKINDYQKNRFVNRIVSSMFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  321 TVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKKFDWDHPLHLQPMSPTTVKQV 400
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQPMSPTAVKQV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241704  401 SVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAFIFDGRNIMNVNKLREIGFIVYSIGKPLDPWL 473
Cdd:PLN02353 401 SVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-473 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 1097.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    1 MVKICCIGAGYVGGPTMAVIALKCPDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREAD 80
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   81 IVFVSVNTPTKTTGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKFQILSNPEFLA 160
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  161 EGTAIADLFNPDRVLIGGRETPEGFKAVQTLKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEST 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  241 GADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPEVAEYWKQVIKINDYQKNRFVNRIVSSMFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  321 TVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKKFDWDHPLHLQPMSPTTVKQV 400
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQPMSPTAVKQV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241704  401 SVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAFIFDGRNIMNVNKLREIGFIVYSIGKPLDPWL 473
Cdd:PLN02353 401 SVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
3-468 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 568.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   3 KICCIGAGYVGGPTMAVIALKCPDieVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCR-GKNLFFSTDVEKHVREADI 81
Cdd:COG1004   2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  82 VFVSVNTPTKTTGlgagkAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKIL--MHNSKGIKFQILSNPEFL 159
Cdd:COG1004  80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaeELRGAGVDFDVVSNPEFL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 160 AEGTAIADLFNPDRVLIGGretpEGFKAVQTLKEVYANWVPEG-QIITTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGV----DSERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 239 STGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPevAEYWKQVIKINDYQKNRFVNRIVSSM 318
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 319 FNTVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQiQRDLSmkkfdwdhplhlqpmspttvK 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENA-RRLLP--------------------D 367
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 399 QVSVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAfIFDGRNIMNVNKLREIGFIVYSIGKP 468
Cdd:COG1004 368 DITYADDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
3-448 1.49e-115

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: 345.75  E-value: 1.49e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704     3 KICCIGAGYVGGPTMAVIALKcpDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLF-FSTDVEKHVREADI 81
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    82 VFVSVNTPTKTTGlgagkAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEK-ILMHNSK--GIKFQILSNPEF 158
Cdd:TIGR03026  80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpILERSGLklGEDFYLAYNPEF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   159 LAEGTAIADLFNPDRVLIGgrETPEgfkAVQTLKEVYANWVpEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:TIGR03026 155 LREGNAVHDLLHPDRIVGG--ETEE---AGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   239 STGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPevAEYWKQVIKINDYQKNRFVNRIVSSM 318
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   319 FNtVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKkfdwdhplhlqpmspttvk 398
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID------------------- 366
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15241704   399 qvsvtwDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPaFIFDGRN 448
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 ...
3-194 2.82e-81

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: 249.86  E-value: 2.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704     3 KICCIGAGYVGGPTMAVIALKCpdIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREADIV 82
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    83 FVSVNTPTKTTglgaGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAE-AIEKILMHNSK--GIKFQILSNPEFL 159
Cdd:pfam03721  80 FIAVGTPSKKG----GGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGKkvGVDFDVASNPEFL 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15241704   160 AEGTAIADLFNPDRVLIGGRETPEGfkavQTLKEV 194
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAE----AALEEL 186
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
328-451 2.72e-31

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: 116.07  E-value: 2.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    328 AILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEqiqrdlsMKKFDwdhplhlqpmspttvkqVSVTWDAY 407
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEE-------AREYG-----------------LTYVSDLE 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 15241704    408 EATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPaFIFDGRNIMN 451
Cdd:smart00984  57 EALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-473 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 1097.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    1 MVKICCIGAGYVGGPTMAVIALKCPDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREAD 80
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   81 IVFVSVNTPTKTTGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKFQILSNPEFLA 160
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  161 EGTAIADLFNPDRVLIGGRETPEGFKAVQTLKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEST 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  241 GADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPEVAEYWKQVIKINDYQKNRFVNRIVSSMFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  321 TVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKKFDWDHPLHLQPMSPTTVKQV 400
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQPMSPTAVKQV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241704  401 SVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAFIFDGRNIMNVNKLREIGFIVYSIGKPLDPWL 473
Cdd:PLN02353 401 SVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
3-468 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 568.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   3 KICCIGAGYVGGPTMAVIALKCPDieVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCR-GKNLFFSTDVEKHVREADI 81
Cdd:COG1004   2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  82 VFVSVNTPTKTTGlgagkAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKIL--MHNSKGIKFQILSNPEFL 159
Cdd:COG1004  80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaeELRGAGVDFDVVSNPEFL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 160 AEGTAIADLFNPDRVLIGGretpEGFKAVQTLKEVYANWVPEG-QIITTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGV----DSERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 239 STGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPevAEYWKQVIKINDYQKNRFVNRIVSSM 318
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 319 FNTVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQiQRDLSmkkfdwdhplhlqpmspttvK 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENA-RRLLP--------------------D 367
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 399 QVSVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAfIFDGRNIMNVNKLREIGFIVYSIGKP 468
Cdd:COG1004 368 DITYADDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
3-448 1.49e-115

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: 345.75  E-value: 1.49e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704     3 KICCIGAGYVGGPTMAVIALKcpDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLF-FSTDVEKHVREADI 81
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    82 VFVSVNTPTKTTGlgagkAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEK-ILMHNSK--GIKFQILSNPEF 158
Cdd:TIGR03026  80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpILERSGLklGEDFYLAYNPEF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   159 LAEGTAIADLFNPDRVLIGgrETPEgfkAVQTLKEVYANWVpEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:TIGR03026 155 LREGNAVHDLLHPDRIVGG--ETEE---AGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   239 STGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPevAEYWKQVIKINDYQKNRFVNRIVSSM 318
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   319 FNtVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKkfdwdhplhlqpmspttvk 398
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID------------------- 366
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15241704   399 qvsvtwDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPaFIFDGRN 448
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 ...
3-194 2.82e-81

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: 249.86  E-value: 2.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704     3 KICCIGAGYVGGPTMAVIALKCpdIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREADIV 82
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    83 FVSVNTPTKTTglgaGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAE-AIEKILMHNSK--GIKFQILSNPEFL 159
Cdd:pfam03721  80 FIAVGTPSKKG----GGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGKkvGVDFDVASNPEFL 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15241704   160 AEGTAIADLFNPDRVLIGGRETPEGfkavQTLKEV 194
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAE----AALEEL 186
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
3-451 4.90e-57

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 194.51  E-value: 4.90e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   3 KICCIGAGYVGGPTMAVIALKcpDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKhVREADIV 82
Cdd:COG0677   1 KIAVIGLGYVGLPLAVAFAKA--GFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPEA-LAEADVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  83 FVSVNTPtkttgLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKFqilsNPEF-LA- 160
Cdd:COG0677  78 IIAVPTP-----LDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKA----GEDFfLAy 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 161 ------EGTAIADLFNPDRVlIGGReTPEGFKAVqtlKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMS 234
Cdd:COG0677 149 sperinPGNKLHELRNIPKV-VGGI-TPESAERA---AALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 235 ALCESTGADVTQVSYAVGTdsRIGSKFLNASVGFGGSCFQKDILNLVYicqcnGLPEVaEYWKQVI----KINDYQKNRF 310
Cdd:COG0677 224 LICDRLGIDVWEVIEAANT--KPGFLIFYPGPGVGGHCIPVDPYYLTW-----KAREL-GYHPRLIlaarEINDSMPEYV 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704 311 VNRIVSSMFN---TVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRdlsmkkfdwdhpl 387
Cdd:COG0677 296 VERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEG------------- 362
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241704 388 hlqpmspTTVKQVSVTwdayEATKDAHAVCVLTEWDEFKSLDYQKIfdNMQKPAFIFDGRNIMN 451
Cdd:COG0677 363 -------EYGELVDLE----EALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
211-304 1.96e-42

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: 145.60  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   211 SAELSKLAANAFLAQRISSVNAMSALCESTGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLP 290
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|....
gi 15241704   291 evAEYWKQVIKIND 304
Cdd:pfam00984  81 --ARLLEAAREVNE 92
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
328-451 5.12e-35

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: 126.15  E-value: 5.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   328 AILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLsmkkfdwdhplhlqpmspttvKQVSVTWDAY 407
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALG---------------------DGVTLVDDLE 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15241704   408 EATKDAHAVCVLTEWDEFKSLDYQKIFDNMqKPAFIFDGRNIMN 451
Cdd:pfam03720  60 EALKGADAIVILTDHDEFKSLDWEKLKKLM-KPPVVFDGRNVLD 102
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
328-451 2.72e-31

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: 116.07  E-value: 2.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    328 AILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEqiqrdlsMKKFDwdhplhlqpmspttvkqVSVTWDAY 407
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEE-------AREYG-----------------LTYVSDLE 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 15241704    408 EATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPaFIFDGRNIMN 451
Cdd:smart00984  57 EALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
3-353 4.60e-28

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 115.47  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    3 KICCIGAGYVGGPTMAVIALKcpDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQC-RGKNLFFSTDVEkhvrEADI 81
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATTTPE----PADA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   82 VFVSVNTPTKttglgAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKF----------Q 151
Cdd:PRK11064  79 FLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFpqqageqadiN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  152 ILSNPEFLAEGTAIADLFNPDRVlIGGReTPegfKAVQTLKEVYANWVpEGQIITTNLWSAELSKLAANAFLAQRISSVN 231
Cdd:PRK11064 154 IAYCPERVLPGQVMVELIKNDRV-IGGM-TP---VCSARASELYKIFL-EGECVVTNSRTAEMCKLTENSFRDVNIAFAN 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  232 AMSALCESTGADVTQVSYAVGTDSRIgsKFLNASVGFGGSCFQKDILNLVyiCQCnglPEVAEYWKQVIKINDYQKNRFV 311
Cdd:PRK11064 228 ELSLICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIV--AQN---PQQARLIRTAREVNDGKPHWVI 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 15241704  312 NRIVSSM--FNTVSNK-----KVAILGFAFKKDTGDTRETPAIDVCKGL 353
Cdd:PRK11064 301 DQVKAAVadCLAATDKrasevKIACFGLAFKPNIDDLRESPAMEIAELI 349
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
2-380 1.57e-27

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 113.58  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    2 VKICCIGAGYVGGPTMAVIAlkcPDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQcrgKNLFFSTDVEKHVREADI 81
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIA---QNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS---DKIHFNATLDKNEAYRDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   82 VFVSVNTPT----KTTGLGAgkaadltywESAARMIADVSV--SDKIVVEKSTVPVKTAEAIEKilMHNSKGIKFqilsN 155
Cdd:PRK15057  75 DYVIIATPTdydpKTNYFNT---------SSVESVIKDVVEinPYAVMVIKSTVPVGFTAAMHK--KYRTENIIF----S 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  156 PEFLAEGTAIADLFNPDRVLIGGR-ETPEGFKAVqtlkevyanwVPEGQI------ITTNLWSAELSKLAANAFLAQRIS 228
Cdd:PRK15057 140 PEFLREGKALYDNLHPSRIVIGERsERAERFAAL----------LQEGAIkqniptLFTDSTEAEAIKLFANTYLAMRVA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  229 SVNAMSALCESTGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQcnGLPEvaEYWKQVIKINDYQKN 308
Cdd:PRK15057 210 YFNELDSYAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQ--SVPN--NLISAIVDANRTRKD 285
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241704  309 RFVNRIVSSmfntvSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEE-----QIQRDLSMKK 380
Cdd:PRK15057 286 FIADAILSR-----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKEDsffnsRLERDLATFK 357
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
2-375 3.84e-18

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 86.28  E-value: 3.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704    2 VKICCIGAGYVGGPtMAVIALKCPdiEVAVVDISVPRINAWNSDqlpiYEPGLDDIVKQCR-GKNLFFSTDVEKhVREAD 80
Cdd:PRK15182   7 VKIAIIGLGYVGLP-LAVEFGKSR--QVVGFDVNKKRILELKNG----VDVNLETTEEELReARYLKFTSEIEK-IKECN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704   81 IVFVSVNTPTKTTglgagKAADLTYWESAARMIADVSVSDKIVVEKSTV-PVKTAEAIEKILMHNSkGIKFQ----ILSN 155
Cdd:PRK15182  79 FYIITVPTPINTY-----KQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPILARMS-GMTFNqdfyVGYS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  156 PEFLAEGTAIADLFNPDRVLIGGREtpegfKAVQTLKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSA 235
Cdd:PRK15182 153 PERINPGDKKHRLTNIKKITSGSTA-----QIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241704  236 LCESTGADVTQVSYAVGTDSrigsKFLNASVGF-GGSCFQKDILNLVYICQCNGlpevaeYWKQVI----KINDYQKNRF 310
Cdd:PRK15182 228 IFNRLNIDTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIG------YYPEIIlagrRLNDNMGNYV 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241704  311 VNRIVSSMFN---TVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRD 375
Cdd:PRK15182 298 SEQLIKAMIKkgiNVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRRE 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH