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Conserved domains on  [gi|1712725799|gb|QDV44216|]
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UDP-glucose 6-dehydrogenase [Stieleria neptunia]

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
 10-468 0e+00

probable UDP-glucose 6-dehydrogenase


:

Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 772.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCPHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDQAIRAADMV 89
Cdd:PLN02353    3 KICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTFGVGAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILSNTANNASFDVLSNPEFLAEG 169
Cdd:PLN02353   83 FVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLAEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 170 TAIEDLLEPDRVLIGG-ERPE---SIEALVEIYANWVPRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:PLN02353  163 TAIEDLFKPDRVLIGGrETPEgqkAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPEVADYWEQVVRMNDYQKERFVTRMVRTMFNTV 325
Cdd:PLN02353  243 DVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNTV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 326 SDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILNDLEYVFTEGD--NKISEAKRELIEQhVT 403
Cdd:PLN02353  323 SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDhpRHLQPMSPTAVKQ-VS 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712725799 404 FASSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPAFVFDGRNRLKDLDLKAKGFEYHGIG 468
Cdd:PLN02353  402 VVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIG 466
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 10-468 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 772.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCPHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDQAIRAADMV 89
Cdd:PLN02353    3 KICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTFGVGAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILSNTANNASFDVLSNPEFLAEG 169
Cdd:PLN02353   83 FVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLAEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 170 TAIEDLLEPDRVLIGG-ERPE---SIEALVEIYANWVPRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:PLN02353  163 TAIEDLFKPDRVLIGGrETPEgqkAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPEVADYWEQVVRMNDYQKERFVTRMVRTMFNTV 325
Cdd:PLN02353  243 DVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNTV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 326 SDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILNDLEYVFTEGD--NKISEAKRELIEQhVT 403
Cdd:PLN02353  323 SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDhpRHLQPMSPTAVKQ-VS 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712725799 404 FASSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPAFVFDGRNRLKDLDLKAKGFEYHGIG 468
Cdd:PLN02353  402 VVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIG 466
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
10-468 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 573.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCPhiDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSR-GKNLTFTTEIDQAIRAADM 88
Cdd:COG1004     2 KIAVIGTGYVGLVTAACLAELGH--EVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  89 VFISVNTPTKTFGvgagrAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILSNTANNAS--FDVLSNPEFL 166
Cdd:COG1004    80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGAGvdFDVVSNPEFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 167 AEGTAIEDLLEPDRVLIGGERPESIEALVEIYANWVPR-ARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:COG1004   155 REGSAVEDFLRPDRIVIGVDSERAAEVLRELYAPFVRNgTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPevADYWEQVVRMNDYQKERFVTRMVRTMFNTV 325
Cdd:COG1004   235 DVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHLGGDL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 326 SDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEhqilndleyvftegdnkisEAKRELiEQHVTFA 405
Cdd:COG1004   313 KGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAME-------------------NARRLL-PDDITYA 372

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712725799 406 SSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPAfVFDGRNRLKDLDLKAKGFEYHGIG 468
Cdd:COG1004   373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIG 434
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 9-450 5.58e-112

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: 336.51  E-value: 5.58e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799   9 SKICCIGAGYVGGPTMAMIAHKcpHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQS-SRGKNLTFTTEIDQAIRAAD 87
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKaLKAGRLRATTDYEEAIRDAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  88 MVFISVNTPTKTfgvgaGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAV-KRIL--SNTANNASFDVLSNPE 164
Cdd:TIGR03026  79 VIIICVPTPLKE-----DGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVvKPILerSGLKLGEDFYLAYNPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 165 FLAEGTAIEDLLEPDRVlIGGERPESIEALVEIYANWVpRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATG 244
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRI-VGGETEEAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 245 ADVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPevADYWEQVVRMNDYQKERfVTRMVRTMFNT 324
Cdd:TIGR03026 232 IDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDY-VVEKIKDLLGP 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 325 VSDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILNDLEYvftegdnkiseakrelieqhvtf 404
Cdd:TIGR03026 309 LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSI----------------------- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1712725799 405 aSSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPaFVFDGRN 450
Cdd:TIGR03026 366 -DDLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 10-197 4.00e-74

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: 230.98  E-value: 4.00e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCphIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDQAIRAADMV 89
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTfgvgAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAE-AVKRILSNT--ANNASFDVLSNPEFL 166
Cdd:pfam03721  80 FIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGgkKVGVDFDVASNPEFL 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1712725799 167 AEGTAIEDLLEPDRVLIGGERPESIEALVEI 197
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEEL 186
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 331-453 5.10e-26

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: 101.43  E-value: 5.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  331 GIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEhqilndleyvftegdnkiseakrELIEQHVTFASSAQE 410
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAME-----------------------EAREYGLTYVSDLEE 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1712725799  411 ASSDSHAIAVLTEWDEFADANFDAIYASMKKPaFVFDGRNRLK 453
Cdd:smart00984  58 ALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 10-468 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 772.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCPHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDQAIRAADMV 89
Cdd:PLN02353    3 KICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTFGVGAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILSNTANNASFDVLSNPEFLAEG 169
Cdd:PLN02353   83 FVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLAEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 170 TAIEDLLEPDRVLIGG-ERPE---SIEALVEIYANWVPRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:PLN02353  163 TAIEDLFKPDRVLIGGrETPEgqkAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPEVADYWEQVVRMNDYQKERFVTRMVRTMFNTV 325
Cdd:PLN02353  243 DVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNTV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 326 SDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILNDLEYVFTEGD--NKISEAKRELIEQhVT 403
Cdd:PLN02353  323 SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDhpRHLQPMSPTAVKQ-VS 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712725799 404 FASSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPAFVFDGRNRLKDLDLKAKGFEYHGIG 468
Cdd:PLN02353  402 VVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIG 466
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
10-468 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 573.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCPhiDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSR-GKNLTFTTEIDQAIRAADM 88
Cdd:COG1004     2 KIAVIGTGYVGLVTAACLAELGH--EVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  89 VFISVNTPTKTFGvgagrAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILSNTANNAS--FDVLSNPEFL 166
Cdd:COG1004    80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGAGvdFDVVSNPEFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 167 AEGTAIEDLLEPDRVLIGGERPESIEALVEIYANWVPR-ARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:COG1004   155 REGSAVEDFLRPDRIVIGVDSERAAEVLRELYAPFVRNgTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPevADYWEQVVRMNDYQKERFVTRMVRTMFNTV 325
Cdd:COG1004   235 DVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHLGGDL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 326 SDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEhqilndleyvftegdnkisEAKRELiEQHVTFA 405
Cdd:COG1004   313 KGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAME-------------------NARRLL-PDDITYA 372

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712725799 406 SSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPAfVFDGRNRLKDLDLKAKGFEYHGIG 468
Cdd:COG1004   373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIG 434
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 9-450 5.58e-112

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: 336.51  E-value: 5.58e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799   9 SKICCIGAGYVGGPTMAMIAHKcpHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQS-SRGKNLTFTTEIDQAIRAAD 87
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKaLKAGRLRATTDYEEAIRDAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  88 MVFISVNTPTKTfgvgaGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAV-KRIL--SNTANNASFDVLSNPE 164
Cdd:TIGR03026  79 VIIICVPTPLKE-----DGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVvKPILerSGLKLGEDFYLAYNPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 165 FLAEGTAIEDLLEPDRVlIGGERPESIEALVEIYANWVpRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATG 244
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRI-VGGETEEAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 245 ADVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLPevADYWEQVVRMNDYQKERfVTRMVRTMFNT 324
Cdd:TIGR03026 232 IDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDY-VVEKIKDLLGP 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 325 VSDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILNDLEYvftegdnkiseakrelieqhvtf 404
Cdd:TIGR03026 309 LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSI----------------------- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1712725799 405 aSSAQEASSDSHAIAVLTEWDEFADANFDAIYASMKKPaFVFDGRN 450
Cdd:TIGR03026 366 -DDLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 10-197 4.00e-74

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: 230.98  E-value: 4.00e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCphIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDQAIRAADMV 89
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTfgvgAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAE-AVKRILSNT--ANNASFDVLSNPEFL 166
Cdd:pfam03721  80 FIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGgkKVGVDFDVASNPEFL 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1712725799 167 AEGTAIEDLLEPDRVLIGGERPESIEALVEI 197
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEEL 186
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
10-453 1.10e-45

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 164.08  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKCphIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSSRGKNLTFTTEIDqAIRAADMV 89
Cdd:COG0677     1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPE-ALAEADVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPtktfgVGAGRAANLEFVEKCARRIAEV-SEGHKIVVEkSTLPVRTAEAV-KRILSNTAN---NASFDVLSNPE 164
Cdd:COG0677    78 IIAVPTP-----LDEDKEPDLSYLESASETIAPHlKPGDLVVLE-STVYPGTTEEVcVPILEKRSGlkaGEDFFLAYSPE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 165 FLAEGTAIEDLLEPDRVlIGGERPESIEALVEIYANWVPRARLLTTNLWSSELSKLTANAF------LAqrvssiNAISA 238
Cdd:COG0677   152 RINPGNKLHELRNIPKV-VGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYrdvniaLA------NELAL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 239 LCEATGADVDEVAAAIGTDsrigPKFLKSS--VGFGGSCFQKDILNLVYlcqyfGLPEVaDYWEQVV----RMNDYqKER 312
Cdd:COG0677   225 ICDRLGIDVWEVIEAANTK----PGFLIFYpgPGVGGHCIPVDPYYLTW-----KAREL-GYHPRLIlaarEINDS-MPE 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 313 FVTRMVRTMFN----TVSDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHqilndleyvftegdn 388
Cdd:COG0677   294 YVVERVVKALNeagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEE--------------- 358

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712725799 389 kisEAKRELIEqhvtfASSAQEASSDSHAIAVLTEWDEFADANFDAIyaSMKKPAFVFDGRNRLK 453
Cdd:COG0677   359 ---EVEGEYGE-----LVDLEEALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 214-307 1.68e-40

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: 140.21  E-value: 1.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 214 SSELSKLTANAFLAQRVSSINAISALCEATGADVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLVYLCQYFGLP 293
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80

                          90
                  ....*....|....
gi 1712725799 294 evADYWEQVVRMND 307
Cdd:pfam00984  81 --ARLLEAAREVNE 92
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 10-377 1.29e-30

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 122.05  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHkcpHIDVKVVDINADRIAQWNSDRLPIYEpglDEIVQSSRGKNLTFTTEIDQ--AIRAAD 87
Cdd:PRK15057    2 KITISGTGYVGLSNGLLIAQ---NHEVVALDILPSRVAMLNDRISPIVD---KEIQQFLQSDKIHFNATLDKneAYRDAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  88 MVFISvnTPT----KTfgvgagRAANLEFVEKCARRIAEVSEGHKIVVeKSTLPVRTAEAVKRILsNTANnasfdVLSNP 163
Cdd:PRK15057   76 YVIIA--TPTdydpKT------NYFNTSSVESVIKDVVEINPYAVMVI-KSTVPVGFTAAMHKKY-RTEN-----IIFSP 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 164 EFLAEGTAIEDLLEPDRVLIG--GERPESIEALVEIYA--NWVPRarlLTTNLWSSELSKLTANAFLAQRVSSINAISAL 239
Cdd:PRK15057  141 EFLREGKALYDNLHPSRIVIGerSERAERFAALLQEGAikQNIPT---LFTDSTEAEAIKLFANTYLAMRVAYFNELDSY 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 240 CEATGADVDEVAAAIGTDSRIGPKFLKSSVGFGGSCFQKDILNLvyLCQYFGLPEvaDYWEQVVRMNDYQKErFVTRMVR 319
Cdd:PRK15057  218 AESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVPN--NLISAIVDANRTRKD-FIADAIL 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1712725799 320 TMfntvSDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQILN 377
Cdd:PRK15057  293 SR----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKEDSFFN 346
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 331-453 6.04e-29

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: 109.59  E-value: 6.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 331 GIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQIlndleyvftegdnkiseakrELIEQHVTFASSAQE 410
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAI--------------------EALGDGVTLVDDLEE 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1712725799 411 ASSDSHAIAVLTEWDEFADANFDAIyASMKKPAFVFDGRNRLK 453
Cdd:pfam03720  61 ALKGADAIVILTDHDEFKSLDWEKL-KKLMKPPVVFDGRNVLD 102
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 331-453 5.10e-26

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: 101.43  E-value: 5.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  331 GIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEhqilndleyvftegdnkiseakrELIEQHVTFASSAQE 410
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAME-----------------------EAREYGLTYVSDLEE 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1712725799  411 ASSDSHAIAVLTEWDEFADANFDAIYASMKKPaFVFDGRNRLK 453
Cdd:smart00984  58 ALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 10-356 5.45e-26

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 109.30  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKcpHIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSS-RGKNLTFTTEIDqairAADM 88
Cdd:PRK11064    5 TISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATTTPE----PADA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  89 VFISVNTPTKtfgvgAGRAANLEFVEKCARRIAEVSEGHKIVVEKSTLPVRTAEAVKRILS----------NTANNASFD 158
Cdd:PRK11064   79 FLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAearpdltfpqQAGEQADIN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 159 VLSNPEFLAEGTAIEDLLEPDRVlIGGERPESIEALVEIYANWVpRARLLTTNLWSSELSKLTANAFLAQRVSSINAISA 238
Cdd:PRK11064  154 IAYCPERVLPGQVMVELIKNDRV-IGGMTPVCSARASELYKIFL-EGECVVTNSRTAEMCKLTENSFRDVNIAFANELSL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 239 LCEATGADVDEVAAAIGTDSRIgpKFLKSSVGFGGSCFQKDILNLVYLCqyfglPEVAdyweQVVRM----NDyQKERFV 314
Cdd:PRK11064  232 ICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIVAQN-----PQQA----RLIRTarevND-GKPHWV 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1712725799 315 TRMVRTMF--------NTVSDKKIGIWGFAFKKDTNDTRESASIYVCRDL 356
Cdd:PRK11064  300 IDQVKAAVadclaatdKRASEVKIACFGLAFKPNIDDLRESPAMEIAELI 349
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
10-375 6.63e-14

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 73.18  E-value: 6.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  10 KICCIGAGYVGGPTMAMIAHKcphIDVKVVDINADRIAQWNSDRLPIYEPGLDEIVQSsrgKNLTFTTEIDQaIRAADMV 89
Cdd:PRK15182    8 KIAIIGLGYVGLPLAVEFGKS---RQVVGFDVNKKRILELKNGVDVNLETTEEELREA---RYLKFTSEIEK-IKECNFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799  90 FISVNTPTKTFgvgagRAANLEFVEKCARRIAEV-SEGHKIVVEKSTLPVRTAEAVKRILSNTAN---NASFDVLSNPEF 165
Cdd:PRK15182   81 IITVPTPINTY-----KQPDLTPLIKASETVGTVlNRGDIVVYESTVYPGCTEEECVPILARMSGmtfNQDFYVGYSPER 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 166 LAEGTAIEDLLEPDRVlIGGERPESIEALVEIYANWVPRARLLTTNLWSSELSKLTANAFLAQRVSSINAISALCEATGA 245
Cdd:PRK15182  156 INPGDKKHRLTNIKKI-TSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712725799 246 DVDEVAAAIGTDSrigpKFLKSSVGF-GGSCFQKDILNLVYLCQYFGlpevadYWEQVV----RMND----YQKERFVTR 316
Cdd:PRK15182  235 DTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIG------YYPEIIlagrRLNDnmgnYVSEQLIKA 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1712725799 317 MVRTMFNtVSDKKIGIWGFAFKKDTNDTRESASIYVCRDLLLEKARLCIYDPQVSEHQI 375
Cdd:PRK15182  305 MIKKGIN-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.
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