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Conserved domains on  [gi|492271468|ref|WP_005795347|]
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MULTISPECIES: nucleotide sugar dehydrogenase [Bacteroides]

Protein Classification

nucleotide sugar dehydrogenase( domain architecture ID 11430796)

nucleotide sugar dehydrogenase such as UDP-N-acetylglucosamine 6-dehydrogenase, which catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA)

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0051287|GO:0016628

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-410 0e+00

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


:

Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 631.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   2 KIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEVTDVLLQAALDSG-FKCTSNLEDIRDCNFYVIA 79
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAgFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGrLRATTDPEALAEADVVIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  80 VPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKFNLDFFAGYSPERINPGDKEH 159
Cdd:COG0677   81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEDFFLAYSPERINPGNKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 160 TVEKIKKVTSGSTPEIADIVDKVYNSVLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAA 239
Cdd:COG0677  161 ELRNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 240 SSKWNFIKLRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMNKKGVLVKDSNILLLGI 318
Cdd:COG0677  241 NTKPGFLIFYPGPgVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 319 TFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGIRMIDNVNEKKYDAIILAVGHNEFKTIDIKALG-N 397
Cdd:COG0677  321 AYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRlK 400

                        410
                 ....*....|...
gi 492271468 398 DISVVFDVKCFLD 410
Cdd:COG0677  401 GAKVVVDTRGVLD 413
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-410 0e+00

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 631.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   2 KIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEVTDVLLQAALDSG-FKCTSNLEDIRDCNFYVIA 79
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAgFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGrLRATTDPEALAEADVVIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  80 VPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKFNLDFFAGYSPERINPGDKEH 159
Cdd:COG0677   81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEDFFLAYSPERINPGNKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 160 TVEKIKKVTSGSTPEIADIVDKVYNSVLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAA 239
Cdd:COG0677  161 ELRNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 240 SSKWNFIKLRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMNKKGVLVKDSNILLLGI 318
Cdd:COG0677  241 NTKPGFLIFYPGPgVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 319 TFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGIRMIDNVNEKKYDAIILAVGHNEFKTIDIKALG-N 397
Cdd:COG0677  321 AYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRlK 400

                        410
                 ....*....|...
gi 492271468 398 DISVVFDVKCFLD 410
Cdd:COG0677  401 GAKVVVDTRGVLD 413
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
1-418 1.09e-180

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 510.00  E-value: 1.09e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   1 MKIAVIGLGYVGLPLARLFSTKYQTIGFDMNQKRVESLMGGHDTTLEVTDVLLQAAldSGFKCTSNLEDIRDCNFYVIAV 80
Cdd:PRK15182   7 VKIAIIGLGYVGLPLAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREA--RYLKFTSEIEKIKECNFYIITV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  81 PTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKFNLDFFAGYSPERINPGDKEHT 160
Cdd:PRK15182  85 PTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTFNQDFYVGYSPERINPGDKKHR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 161 VEKIKKVTSGSTPEIADIVDKVYNSVLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAAS 240
Cdd:PRK15182 165 LTNIKKITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRAAG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 241 SKWNFIKLRPGLVGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMNKKGVLVKDSNILLLGITF 320
Cdd:PRK15182 245 SKWNFLPFRPGLVGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVLILGFTF 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 321 KENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGIRMIDNVNEKKYDAIILAVGHNEFKTI---DIKALGN 397
Cdd:PRK15182 325 KENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRREYGIIPVSEVKSSHYDAIIVAVGHQQFKQMgseDIRGFGK 404

                        410       420
                 ....*....|....*....|.
gi 492271468 398 DISVVFDVKCFLDRAIVDGRL 418
Cdd:PRK15182 405 DKHVLYDLKYVLPAEQSDVRL 425
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-406 3.87e-132

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: 385.81  E-value: 3.87e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468    1 MKIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEVT-DVLLQAALDSG-FKCTSNLEDI-RDCNFY 76
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLgHDVTGVDIDQEKVDKLNKGKSPIYEPGlDELLAKALKAGrLRATTDYEEAiRDADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   77 VIAVPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERvSGLKFNLDFFAGYSPERINPGD 156
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILER-SGLKLGEDFYLAYNPEFLREGN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  157 KEHTVEKIKKVTSGSTPEIADIVDKVYNSvLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVI 236
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGEAVAELYSP-IIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  237 EAASSKWNFIK--LRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMnkkgVLVKDSNI 313
Cdd:TIGR03026 239 EAAGTDPRIGFnfLNPGPgVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  314 LLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGirmIDNVNE--KKYDAIILAVGHNEFKTID 391
Cdd:TIGR03026 315 LILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPS---IDDLEEalKGADALVILTDHSEFKDLD 391

                         410
                  ....*....|....*..
gi 492271468  392 IKALGN--DISVVFDVK 406
Cdd:TIGR03026 392 LEKIKDlmKGKVVVDTR 408
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 199-287 4.97e-33

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: 119.41  E-value: 4.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  199 VAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAASSKWN--FIKLRPGL-VGGHCISVDPYYLIQKAQVYGVL 275
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPgVGGSCLPKDPRALIYLARELGVP 80

                          90
                  ....*....|..
gi 492271468  276 PRIMSSARRLND 287
Cdd:pfam00984  81 ARLLEAAREVNE 92
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 314-410 6.50e-24

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: 94.88  E-value: 6.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   314 LLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKvyEEYGIRMIDNVNE--KKYDAIILAVGHNEFKTID 391
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEA--REYGLTYVSDLEEalKGADAVVIATEHDEFRSLD 78

                           90       100
                   ....*....|....*....|.
gi 492271468   392 IKALGNDIS--VVFDVKCFLD 410
Cdd:smart00984  79 PEELKDLMKkpVVVDGRNILD 99
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-410 0e+00

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 631.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   2 KIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEVTDVLLQAALDSG-FKCTSNLEDIRDCNFYVIA 79
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAgFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGrLRATTDPEALAEADVVIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  80 VPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKFNLDFFAGYSPERINPGDKEH 159
Cdd:COG0677   81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEDFFLAYSPERINPGNKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 160 TVEKIKKVTSGSTPEIADIVDKVYNSVLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAA 239
Cdd:COG0677  161 ELRNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 240 SSKWNFIKLRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMNKKGVLVKDSNILLLGI 318
Cdd:COG0677  241 NTKPGFLIFYPGPgVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 319 TFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGIRMIDNVNEKKYDAIILAVGHNEFKTIDIKALG-N 397
Cdd:COG0677  321 AYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRlK 400

                        410
                 ....*....|...
gi 492271468 398 DISVVFDVKCFLD 410
Cdd:COG0677  401 GAKVVVDTRGVLD 413
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
1-418 1.09e-180

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 510.00  E-value: 1.09e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   1 MKIAVIGLGYVGLPLARLFSTKYQTIGFDMNQKRVESLMGGHDTTLEVTDVLLQAAldSGFKCTSNLEDIRDCNFYVIAV 80
Cdd:PRK15182   7 VKIAIIGLGYVGLPLAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREA--RYLKFTSEIEKIKECNFYIITV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  81 PTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKFNLDFFAGYSPERINPGDKEHT 160
Cdd:PRK15182  85 PTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTFNQDFYVGYSPERINPGDKKHR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 161 VEKIKKVTSGSTPEIADIVDKVYNSVLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAAS 240
Cdd:PRK15182 165 LTNIKKITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRAAG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 241 SKWNFIKLRPGLVGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMNKKGVLVKDSNILLLGITF 320
Cdd:PRK15182 245 SKWNFLPFRPGLVGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVLILGFTF 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 321 KENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGIRMIDNVNEKKYDAIILAVGHNEFKTI---DIKALGN 397
Cdd:PRK15182 325 KENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRREYGIIPVSEVKSSHYDAIIVAVGHQQFKQMgseDIRGFGK 404

                        410       420
                 ....*....|....*....|.
gi 492271468 398 DISVVFDVKCFLDRAIVDGRL 418
Cdd:PRK15182 405 DKHVLYDLKYVLPAEQSDVRL 425
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-406 3.87e-132

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: 385.81  E-value: 3.87e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468    1 MKIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEVT-DVLLQAALDSG-FKCTSNLEDI-RDCNFY 76
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLgHDVTGVDIDQEKVDKLNKGKSPIYEPGlDELLAKALKAGrLRATTDYEEAiRDADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   77 VIAVPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERvSGLKFNLDFFAGYSPERINPGD 156
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILER-SGLKLGEDFYLAYNPEFLREGN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  157 KEHTVEKIKKVTSGSTPEIADIVDKVYNSvLINGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVI 236
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGEAVAELYSP-IIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  237 EAASSKWNFIK--LRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSSARRLNDGMGDYVANQVIKLMnkkgVLVKDSNI 313
Cdd:TIGR03026 239 EAAGTDPRIGFnfLNPGPgVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  314 LLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKVYEEYGirmIDNVNE--KKYDAIILAVGHNEFKTID 391
Cdd:TIGR03026 315 LILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPS---IDDLEEalKGADALVILTDHSEFKDLD 391

                         410
                  ....*....|....*..
gi 492271468  392 IKALGN--DISVVFDVK 406
Cdd:TIGR03026 392 LEKIKDlmKGKVVVDTR 408
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 2-401 8.64e-56

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 189.42  E-value: 8.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   2 KIAVIGLGYVGLPLARLF-STKYQTIGFDMNQKRVESLMGGHDTTLEVT-DVLLQAALDSGF-KCTSNLEDirdCNFYVI 78
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFaSRQKQVIGVDINQHAVDTINRGEIHIVEPDlDMVVKTAVEGGYlRATTTPEP---ADAFLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  79 AVPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKF------NLDFFAGYSPERI 152
Cdd:PRK11064  82 AVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFpqqageQADINIAYCPERV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 153 NPGdkEHTVEKIK--KVTSGSTPEIADIVDKVYNSVLiNGTHKAPSIRVAEASKIIENSQRDVNIAFMNELAKIFNAMDI 230
Cdd:PRK11064 162 LPG--QVMVELIKndRVIGGMTPVCSARASELYKIFL-EGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 231 DTNDVIEAASS--KWNFIKLRPGlVGGHCISVDPYYLIQKAQvygVLPRIMSSARRLNDGMGDYVANQV----IKLMNKK 304
Cdd:PRK11064 239 NVWELIRLANRhpRVNILQPGPG-VGGHCIAVDPWFIVAQNP---QQARLIRTAREVNDGKPHWVIDQVkaavADCLAAT 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 305 GVLVKDSNILLLGITFKENCPDIRNTKVVDIYSTLLEY-TKNISVYDPwaNAEKVYEEY-GIRMIDNVNE--KKYDAIIL 380
Cdd:PRK11064 315 DKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWhSGETLVVEP--NIHQLPKKLdGLVTLVSLDEalATADVLVM 392

                        410       420
                 ....*....|....*....|.
gi 492271468 381 AVGHNEFKTIDIKALGNDISV 401
Cdd:PRK11064 393 LVDHSQFKAINGDNVHQQWVV 413
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-417 1.42e-38

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 144.01  E-value: 1.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   1 MKIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGG----HDTTLEVtdvLLQAALDSG---FkcTSNLED-IR 71
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELgHEVTCVDIDEEKIEALNAGeipiYEPGLEE---LVARNVAAGrlrF--TTDLAEaVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  72 DCNFYVIAVPTPVDRNNRPDLTPLISASETVGKVISKGDIVVYESTVYPGVTE--EECLPVVERVSGLKFNL-------- 141
Cdd:COG1004   76 EADVVFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADrvRAIIAEELRGAGVDFDVvsnpeflr 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 142 ------DFFagySPERInpgdkehtvekikkVTSGSTPEIADIVDKVYNSVLINGThkaP----SIRVAEASKIIENS-- 209
Cdd:COG1004  156 egsaveDFL---RPDRI--------------VIGVDSERAAEVLRELYAPFVRNGT---PiivtDLRSAELIKYAANAfl 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 210 -QRdvnIAFMNELAKIFNAMDIDTNDVIEAA------SSKwnFikLRPGL-VGGHCISVDPYYLIQKAQVYGVLPRIMSS 281
Cdd:COG1004  216 aTK---ISFINEIANLCEKVGADVEEVARGIgldsriGPK--F--LYAGIgYGGSCFPKDVRALIATARELGYDLRLLEA 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 282 ARRLNDGMGDYVANQVIKLMNKKgvlVKDSNILLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWA--NAEKVY 359
Cdd:COG1004  289 VEEVNERQKRRLVEKIREHLGGD---LKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAmeNARRLL 365

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 360 EEyGIRMIDNVNE--KKYDAIILAVGHNEFKTIDIKALGNDISvvfdvkcflDRAIVDGR 417
Cdd:COG1004  366 PD-DITYADDAYEalEGADALVILTEWPEFRALDFARLKALMK---------GPVIFDGR 415
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 199-287 4.97e-33

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: 119.41  E-value: 4.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  199 VAEASKIIENSQRDVNIAFMNELAKIFNAMDIDTNDVIEAASSKWN--FIKLRPGL-VGGHCISVDPYYLIQKAQVYGVL 275
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPgVGGSCLPKDPRALIYLARELGVP 80

                          90
                  ....*....|..
gi 492271468  276 PRIMSSARRLND 287
Cdd:pfam00984  81 ARLLEAAREVNE 92
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 1-174 1.62e-30

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: 115.81  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468    1 MKIAVIGLGYVGLPLARLFSTK-YQTIGFDMNQKRVESLMGGHDTTLEV-TDVLLQAALDSGFKCTSNLE-DIRDCNFYV 77
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIgHDVIGVDIDEEKVDKLNSGQIPIYEPgLDELVKANVSGRLSFTTDYStAIEEADVIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   78 IAVPTPVDRNNR-PDLTPLISASETVGKVISKGDIVVYESTVYPGVTEEECLPVVERVSGLKfNLDFFAGYSPERINPGD 156
Cdd:pfam03721  81 IAVGTPSKKGGGaADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKV-GVDFDVASNPEFLREGS 159

                         170
                  ....*....|....*...
gi 492271468  157 KEHTVEKIKKVTSGSTPE 174
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEK 177
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 314-411 2.86e-25

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: 98.80  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  314 LLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKV-YEEYGIRMIDNVNE--KKYDAIILAVGHNEFKTI 390
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIeALGDGVTLVDDLEEalKGADAIVILTDHDEFKSL 80

                          90       100
                  ....*....|....*....|...
gi 492271468  391 DIKALGNDIS--VVFDVKCFLDR 411
Cdd:pfam03720  81 DWEKLKKLMKppVVFDGRNVLDP 103
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 314-410 6.50e-24

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: 94.88  E-value: 6.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   314 LLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISVYDPWANAEKvyEEYGIRMIDNVNE--KKYDAIILAVGHNEFKTID 391
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEA--REYGLTYVSDLEEalKGADAVVIATEHDEFRSLD 78

                           90       100
                   ....*....|....*....|.
gi 492271468   392 IKALGNDIS--VVFDVKCFLD 410
Cdd:smart00984  79 PEELKDLMKkpVVVDGRNILD 99
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 1-298 4.84e-11

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 63.89  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   1 MKIAVIGLGYVGLPLARLFSTKYQTIGFDMNQKRVESLmggHDTTLEVTDVLLQAALDSG---FKCT-SNLEDIRDCNFY 76
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQNHEVVALDILPSRVAML---NDRISPIVDKEIQQFLQSDkihFNATlDKNEAYRDADYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  77 VIAvpTPVDRNNRPDLTPLISASETVGKVIS--KGDIVVYESTVYPGVTEeeclpvverVSGLKFNLDFFAgYSPERINP 154
Cdd:PRK15057  78 IIA--TPTDYDPKTNYFNTSSVESVIKDVVEinPYAVMVIKSTVPVGFTA---------AMHKKYRTENII-FSPEFLRE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 155 GDKEHTVEKIKKVTSGSTPEIAdivdKVYNSVLINGTHKA--PSIRV----AEASKIIENSQRDVNIAFMNELAKIFNAM 228
Cdd:PRK15057 146 GKALYDNLHPSRIVIGERSERA----ERFAALLQEGAIKQniPTLFTdsteAEAIKLFANTYLAMRVAYFNELDSYAESL 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492271468 229 DIDTNDVIEAA------SSKWNfiklRPGL-VGGHCISVDPYYLIQKAQvyGVLPRIMSSARRLNDGMGDYVANQVI 298
Cdd:PRK15057 222 GLNTRQIIEGVcldpriGNHYN----NPSFgYGGYCLPKDTKQLLANYQ--SVPNNLISAIVDANRTRKDFIADAIL 292
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 1-358 9.70e-08

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 53.91  E-value: 9.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468   1 MKIAVIGLGYVGLPLARLFSTKYQTIG---FDMNQKRVESLMGGHDTTLE--VTDVLLQAALDSGFKCTSNLEDIRDCNF 75
Cdd:PLN02353   2 VKICCIGAGYVGGPTMAVIALKCPDIEvvvVDISVPRIDAWNSDQLPIYEpgLDEVVKQCRGKNLFFSTDVEKHVAEADI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468  76 YVIAVPTP-----VDRNNRPDLTPLISASETVGKVISKGDIVVYESTVyPGVTEEeclpVVERV-----SGLKF----NL 141
Cdd:PLN02353  82 VFVSVNTPtktrgLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTV-PVKTAE----AIEKIlthnsKGINFqilsNP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 142 DFFAG-------YSPERINPGDKEhtvekikkvtsgsTPE----IADIVDkVYnsvlingTHKAPSIRV-------AEAS 203
Cdd:PLN02353 157 EFLAEgtaiedlFKPDRVLIGGRE-------------TPEgqkaVQALKD-VY-------AHWVPEERIittnlwsAELS 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 204 KIIENS---QRdvnIAFMNELAKIFNAMDIDTNDVIEAASSKW----NFIKLRPGLvGGHCISVDPYYLIQKAQVYGvLP 276
Cdd:PLN02353 216 KLAANAflaQR---ISSVNAMSALCEATGADVSQVSHAVGKDSrigpKFLNASVGF-GGSCFQKDILNLVYICECNG-LP 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492271468 277 RIMS---SARRLNDGMGDYVANQVIKLM-----NKKgvlvkdsnILLLGITFKENCPDIRNTKVVDIYSTLLEYTKNISV 348
Cdd:PLN02353 291 EVAEywkQVIKMNDYQKSRFVNRVVSSMfntvsGKK--------IAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSI 362

                        410
                 ....*....|
gi 492271468 349 YDPWANAEKV 358
Cdd:PLN02353 363 YDPQVTEEQI 372
 
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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