NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6136118|sp|O70199|]
View 

RecName: Full=UDP-glucose 6-dehydrogenase; Short=UDP-Glc dehydrogenase; Short=UDP-GlcDH; Short=UDPGDH

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
4-464 0e+00

probable UDP-glucose 6-dehydrogenase


:

Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 781.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     4 IKKICCIGAGYVGGPTCSVIARMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREAD 83
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCES 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   395 VTISKDPYEACDGAHALVICTEWDMFKELDYERIHKRMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 464
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
4-464 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 781.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     4 IKKICCIGAGYVGGPTCSVIARMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREAD 83
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCES 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   395 VTISKDPYEACDGAHALVICTEWDMFKELDYERIHKRMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 464
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-465 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 558.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    6 KICCIGAGYVGGPTCSVIARMCPEirVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIREADL 84
Cdd:COG1004   2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004  80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPKE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  243 STGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREqivvdlshpgvsADDQVSRLVTISKDPY 402
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMEN------------ARRLLPDDITYADDAY 376
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6136118  403 EACDGAHALVICTEWDMFKELDYERIHKRMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 465
Cdd:COG1004 377 EALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
5-443 1.51e-114

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: 343.82  E-value: 1.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118      5 KKICCIGAGYVGGPTCSVIARMcpEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIREAD 83
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026  79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    162 FLAEGTAIKDLKNPDRVLIGGDEtpegqRAVQALCAVYEHWVpKEKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGGETE-----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    242 ESTGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvsaddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 6136118    402 YEACDGAHALVICTEWDMFKELDYERIhKRMLKPAFIFDGRR 443
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
5-191 8.64e-71

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: 223.28  E-value: 8.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118      5 KKICCIGAGYVGGPTCSVIARMCpeIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADL 84
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721  79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
                         170       180
                  ....*....|....*....|....*....
gi 6136118    163 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 191
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
332-446 8.09e-33

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: 120.30  E-value: 8.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvsaddqvSRLVTISKDPYEACDGAHAL 411
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6136118     412 VICTEWDMFKELDYERIHKRMLKPaFIFDGRRVLD 446
Cdd:smart00984  66 VIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
4-464 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 781.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     4 IKKICCIGAGYVGGPTCSVIARMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREAD 83
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCES 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   395 VTISKDPYEACDGAHALVICTEWDMFKELDYERIHKRMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 464
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-465 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 558.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    6 KICCIGAGYVGGPTCSVIARMCPEirVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIREADL 84
Cdd:COG1004   2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004  80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPKE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  243 STGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREqivvdlshpgvsADDQVSRLVTISKDPY 402
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMEN------------ARRLLPDDITYADDAY 376
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6136118  403 EACDGAHALVICTEWDMFKELDYERIHKRMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 465
Cdd:COG1004 377 EALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
5-443 1.51e-114

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: 343.82  E-value: 1.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118      5 KKICCIGAGYVGGPTCSVIARMcpEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIREAD 83
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026  79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    162 FLAEGTAIKDLKNPDRVLIGGDEtpegqRAVQALCAVYEHWVpKEKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGGETE-----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    242 ESTGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvsaddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 6136118    402 YEACDGAHALVICTEWDMFKELDYERIhKRMLKPAFIFDGRR 443
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
5-191 8.64e-71

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: 223.28  E-value: 8.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118      5 KKICCIGAGYVGGPTCSVIARMCpeIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADL 84
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721  79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
                         170       180
                  ....*....|....*....|....*....
gi 6136118    163 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 191
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-446 1.52e-53

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 185.65  E-value: 1.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    6 KICCIGAGYVGGPTCSVIARMCpeIRVTVVDVNEARINAWNSPTLPIYEPG---LKEVVESCRgknLFFSTNIDdAIREA 82
Cdd:COG0677   1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGdelLAEAVAAGR---LRATTDPE-ALAEA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   83 DLVFISVNTPTKtygmgKGRAADLKYIEACARRIVQN-SNGYKIVTEkSTVPVRAAESI-RRIFDANT--KPNLNLQVLS 158
Cdd:COG0677  75 DVVIIAVPTPLD-----EDKEPDLSYLESASETIAPHlKPGDLVVLE-STVYPGTTEEVcVPILEKRSglKAGEDFFLAY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  159 NPEFLAEGTAIKDLKNPDRVlIGGDeTPEGQRAVQALcavYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSIS 238
Cdd:COG0677 149 SPERINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  239 ALCESTGADVEEVATAIGMDQRignkFLKASVGFG-GG-CFQKDVLNLVYLCEALNLP----EVARywqqviDMNDYQRR 312
Cdd:COG0677 224 LICDRLGIDVWEVIEAANTKPG----FLIFYPGPGvGGhCIPVDPYYLTWKARELGYHprliLAAR------EINDSMPE 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118  313 RFASRIIDSLFN---TVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQivvdlshpgvsADD 389
Cdd:COG0677 294 YVVERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEE-----------VEG 362
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6136118  390 QVSRLVTISkdpyEACDGAHALVICTEWDMFKELDYERIhkRMLKPAFIFDGRRVLD 446
Cdd:COG0677 363 EYGELVDLE----EALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
215-308 5.53e-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: 144.44  E-value: 5.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    215 SSELSKLAANAFLAQRISSINSISALCESTGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEALNLP 294
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|....
gi 6136118    295 evARYWQQVIDMND 308
Cdd:pfam00984  81 --ARLLEAAREVNE 92
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
332-446 2.27e-37

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: 132.70  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHpgvsaddqvsrlVTISKDPYEACDGAHAL 411
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG------------VTLVDDLEEALKGADAI 68
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 6136118    412 VICTEWDMFKELDYERIHKRMlKPAFIFDGRRVLD 446
Cdd:pfam03720  69 VILTDHDEFKSLDWEKLKKLM-KPPVVFDGRNVLD 102
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
332-446 8.09e-33

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: 120.30  E-value: 8.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvsaddqvSRLVTISKDPYEACDGAHAL 411
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6136118     412 VICTEWDMFKELDYERIHKRMLKPaFIFDGRRVLD 446
Cdd:smart00984  66 VIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
6-369 9.36e-30

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 120.13  E-value: 9.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     6 KICCIGAGYVGGPTCSVIARmcpEIRVTVVDVNEARINAWNSPTLPIYEpglKEVVESCRGKNLFFSTNID--DAIREAD 83
Cdd:PRK15057   2 KITISGTGYVGLSNGLLIAQ---NHEVVALDILPSRVAMLNDRISPIVD---KEIQQFLQSDKIHFNATLDknEAYRDAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    84 LVFISvnTPTKtYGmGKGRAADLKYIEACARRIVQnSNGYKIVTEKSTVPVRAAESIRRIFdaNTKpnlnlQVLSNPEFL 163
Cdd:PRK15057  76 YVIIA--TPTD-YD-PKTNYFNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKY--RTE-----NIIFSPEFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   164 AEGTAIKDLKNPDRVLIGgdetPEGQRAvQALCAVYEHWVPKEKILT--TNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:PRK15057 144 REGKALYDNLHPSRIVIG----ERSERA-ERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   242 ESTGADVEEVATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLvyLCEALNLPEvaRYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:PRK15057 219 ESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVPN--NLISAIVDANRTRKDFIADAILSR 294
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 6136118   322 lfntvTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDP 369
Cdd:PRK15057 295 -----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
5-359 6.78e-22

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 97.75  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     5 KKICCIGAGYVGGPTCSVIARMcpEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAireADL 84
Cdd:PRK11064   4 ETISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEP---ADA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    85 VFISVNTPTKtygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFdANTKPNL----------NL 154
Cdd:PRK11064  79 FLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWL-AEARPDLtfpqqageqaDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   155 QVLSNPEFLAEGTAIKDLKNPDRVlIGGdETPE-GQRAVqalcAVYEHWVPKEKILTtNTWSSELSKLAANAFLAQRISS 233
Cdd:PRK11064 153 NIAYCPERVLPGQVMVELIKNDRV-IGG-MTPVcSARAS----ELYKIFLEGECVVT-NSRTAEMCKLTENSFRDVNIAF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   234 INSISALCESTGADVEEVAtaigmdqRIGNK-----FLKASVGFGGGCFQKDVLNLVYLCealnlPEVARYWQQVIDMND 308
Cdd:PRK11064 226 ANELSLICADQGINVWELI-------RLANRhprvnILQPGPGVGGHCIAVDPWFIVAQN-----PQQARLIRTAREVND 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6136118   309 ----YQRRRFASRIIDSLFNT---VTDKKIAILGFAFKKDTGDTRESSSIYISKYLMD 359
Cdd:PRK11064 294 gkphWVIDQVKAAVADCLAATdkrASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
6-376 1.15e-10

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 63.55  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118     6 KICCIGAGYVGGPTCSVIARmcpEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVEScrgKNLFFSTNIDDaIREADLV 85
Cdd:PRK15182   8 KIAIIGLGYVGLPLAVEFGK---SRQVVGFDVNKKRILELKNGVDVNLETTEEELREA---RYLKFTSEIEK-IKECNFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118    86 FISVNTPTKTYgmgkgRAADLKYIEACARRI----------VQNSNGYKIVTEKSTVPVRAAESirrifdaNTKPNLNLQ 155
Cdd:PRK15182  81 IITVPTPINTY-----KQPDLTPLIKASETVgtvlnrgdivVYESTVYPGCTEEECVPILARMS-------GMTFNQDFY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   156 VLSNPEFLAEGTAIKDLKNPDRVLIGGDetpegQRAVQALCAVYEhwvpkeKILTTNTWSSELSKLAANAFL---AQR-- 230
Cdd:PRK15182 149 VGYSPERINPGDKKHRLTNIKKITSGST-----AQIAELIDEVYQ------QIISAGTYKAESIKVAEAAKVienTQRdl 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   231 -ISSINSISALCESTGADVEEVATAIGMDQrignKFLKASVGF-GGGCFQKDVLNLVYLCEALNL-PEVARYWQQVID-M 306
Cdd:PRK15182 218 nIALVNELAIIFNRLNIDTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYyPEIILAGRRLNDnM 293
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6136118   307 NDYQRRRFASRIIDSLFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQI 376
Cdd:PRK15182 294 GNYVSEQLIKAMIKKGIN-VEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
 
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