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Conserved domains on  [gi|497899652|ref|WP_010213808|]
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MULTISPECIES: UDP-glucose/GDP-mannose dehydrogenase family protein [Pseudomonas]

Protein Classification

UDP-glucose dehydrogenase family protein( domain architecture ID 11436818)

UDP-glucose dehydrogenase family protein similar to UDP-glucose dehydrogenase which catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0016616
PubMed:  37769033

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-437 0e+00

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


:

Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 707.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIDEVHASRVAELV 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAASPRR-DDGFEVISNPEFFKEGCAV 159
Cdd:COG1004   81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGaGVDFDVVSNPEFLREGSAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 160 SDCLRPDRIIVGGASPRALEQMRELYQPFSRNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIEQVR 239
Cdd:COG1004  161 EDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVEEVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 240 LGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYHGELRGKVFAVW 319
Cdd:COG1004  241 RGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVEKIREHLGGDLKGKTIAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 320 GLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGerDDLQLVQCKQDALEGADALVVVTEWQDYRVLD 399
Cdd:COG1004  321 GLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLP--DDITYADDAYEALEGADALVILTEWPEFRALD 398
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 497899652 400 LDQLGEKLRDRAVFDGRNLFDPSQLRDAGFAYYGIGRG 437
Cdd:COG1004  399 FARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
 
Name Accession Description Interval E-value
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-437 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 707.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIDEVHASRVAELV 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAASPRR-DDGFEVISNPEFFKEGCAV 159
Cdd:COG1004   81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGaGVDFDVVSNPEFLREGSAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 160 SDCLRPDRIIVGGASPRALEQMRELYQPFSRNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIEQVR 239
Cdd:COG1004  161 EDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVEEVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 240 LGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYHGELRGKVFAVW 319
Cdd:COG1004  241 RGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVEKIREHLGGDLKGKTIAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 320 GLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGerDDLQLVQCKQDALEGADALVVVTEWQDYRVLD 399
Cdd:COG1004  321 GLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLP--DDITYADDAYEALEGADALVILTEWPEFRALD 398
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 497899652 400 LDQLGEKLRDRAVFDGRNLFDPSQLRDAGFAYYGIGRG 437
Cdd:COG1004  399 FARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-417 5.43e-162

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: 462.85  E-value: 5.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652    1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIDEVHASRVAELV 80
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAAS--PRRDDGFEVISNPEFFKEGCA 158
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERsgLKLGEDFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  159 VSDCLRPDRiIVGGASPRALEQMRELYQPFsrNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIEQV 238
Cdd:TIGR03026 161 VHDLLHPDR-IVGGETEEAGEAVAELYSPI--IDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  239 RLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYhGELRGKVFAV 318
Cdd:TIGR03026 238 IEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL-GPLKGKTVLI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  319 WGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGERDDLqlvqckQDALEGADALVVVTEWQDYRVL 398
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDL------EEALKGADALVILTDHSEFKDL 390
                         410
                  ....*....|....*....
gi 497899652  399 DLDQLGEKLRDRAVFDGRN 417
Cdd:TIGR03026 391 DLEKIKDLMKGKVVVDTRN 409
UDPGDh_AglM NF041297
UDP-glucose 6-dehydrogenase AglM;
1-434 1.06e-115

UDP-glucose 6-dehydrogenase AglM;


Pssm-ID: 469194 [Multi-domain]  Cd Length: 429  Bit Score: 345.74  E-value: 1.06e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELL-RNGLDckRLSFTIDeVHASRVAEL 79
Cdd:NF041297   1 MNVSVIGSGYVGTTVAACFADLGHDVVNVDIDEDIVATINDGEAPIHEPGLDELVaEHAGD--RLRATTD-YDAVLETDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  80 VFIAVGTPAQADGKADLSQVFAVLRSV---LRHADGARIIVNKSTSPVGTVDRLLA---EIAASPRRDDGFEVISNPEFF 153
Cdd:NF041297  78 TFLALPTPSNDDGSIDLSIMEAGAESLgeaLAEKDDDHLVVVKSTVVPGTTEEVIApalEDASGKTAGEDFGVAMNPEFL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 154 KEGCAVSDCLRPDRIIVGGASPRALEQMRELYQP-FSRNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVG 232
Cdd:NF041297 158 REGSAVEDFLNPDKVVLGADDDRALDRLREVYEPlVEAADAPVVETGIREAEMIKYANNAFLASKVSLINDLGNICKEFG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 233 ADIEQVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYhgELR 312
Cdd:NF041297 238 VDAYEVADAIGLDDRIGEQFLRSGVGWGGSCFPKDVAAIIAAAREAGYEPALLEAAVEVNDRQPERLLDLLDEHV--DVA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 313 GKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYgerDDLQLVQCKQDALEGADALVVVTEW 392
Cdd:NF041297 316 GERVAVLGLAFKPGTDDVRNSRAIPVIEGLQERGADVVAYDPVATENMRERF---PDIEYADSAADALDGADGALVVTDW 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 497899652 393 QDYRvlDLDQLGEKLRDRAVFDGRNLFDPsqlRDaGFAYYGI 434
Cdd:NF041297 393 DEFA--ALDEEFDAMATPVVVDGRRIVER---RD-GITYEGL 428
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-436 4.44e-88

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 276.17  E-value: 4.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLA----EVghTVCCMDVDSKRIDALREGICPIFEPGLGELLRnglDC--KRLSFTIDEVHAS 74
Cdd:PLN02353   2 VKICCIGAGYVGGPTMAVIAlkcpDI--EVVVVDISVPRIDAWNSDQLPIYEPGLDEVVK---QCrgKNLFFSTDVEKHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  75 RVAELVFIAVGTPAQADG-----KADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLlAEIAASPRRDDGFEVISN 149
Cdd:PLN02353  77 AEADIVFVSVNTPTKTRGlgagkAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAI-EKILTHNSKGINFQILSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 150 PEFFKEGCAVSDCLRPDRIIVGG----ASPRALEQMRELYQ---PfsrnREKFVIMDARSAELAKYAANCLLATKISFIN 222
Cdd:PLN02353 156 PEFLAEGTAIEDLFKPDRVLIGGretpEGQKAVQALKDVYAhwvP----EERIITTNLWSAELSKLAANAFLAQRISSVN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 223 EMANLAEQVGADIEQVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGV-ETA-LLNAVEQVNRRQKHRLF 300
Cdd:PLN02353 232 AMSALCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLpEVAeYWKQVIKMNDYQKSRFV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 301 KNIHAHYHGELRGKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEA----------------IRHHY 364
Cdd:PLN02353 312 NRVVSSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEqiqrdlsmnkfdwdhpRHLQP 391
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497899652 365 GERDDLQLVQCKQDALE---GADALVVVTEWQDYRVLDLDQLGEKLRDRA-VFDGRNLFDPSQLRDAGFAYYGIGR 436
Cdd:PLN02353 392 MSPTAVKQVSVVWDAYEatkGAHGICILTEWDEFKTLDYQKIYDNMQKPAfVFDGRNVLDHEKLREIGFIVYSIGK 467
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-184 2.71e-65

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: 207.49  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652    1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDcKRLSFTIDEVHASRVAELV 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVS-GRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   81 FIAVGTPA-QADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAA--SPRRDDGFEVISNPEFFKEGC 157
Cdd:pfam03721  80 FIAVGTPSkKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEegGKKVGVDFDVASNPEFLREGS 159
                         170       180
                  ....*....|....*....|....*..
gi 497899652  158 AVSDCLRPDRIIVGGASPRALEQMREL 184
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALEEL 186
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
317-420 7.29e-38

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: 133.01  E-value: 7.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   317 AVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYgerddLQLVQCKQDALEGADALVVVTEWQDYR 396
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG-----LTYVSDLEEALKGADAVVIATEHDEFR 75
                           90       100
                   ....*....|....*....|....
gi 497899652   397 VLDLDQLGEKLRDRAVFDGRNLFD 420
Cdd:smart00984  76 SLDPEELKDLMKKPVVVDGRNILD 99
 
Name Accession Description Interval E-value
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-437 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 707.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIDEVHASRVAELV 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAASPRR-DDGFEVISNPEFFKEGCAV 159
Cdd:COG1004   81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGaGVDFDVVSNPEFLREGSAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 160 SDCLRPDRIIVGGASPRALEQMRELYQPFSRNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIEQVR 239
Cdd:COG1004  161 EDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVEEVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 240 LGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYHGELRGKVFAVW 319
Cdd:COG1004  241 RGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVEKIREHLGGDLKGKTIAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 320 GLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGerDDLQLVQCKQDALEGADALVVVTEWQDYRVLD 399
Cdd:COG1004  321 GLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLP--DDITYADDAYEALEGADALVILTEWPEFRALD 398
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 497899652 400 LDQLGEKLRDRAVFDGRNLFDPSQLRDAGFAYYGIGRG 437
Cdd:COG1004  399 FARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-417 5.43e-162

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: 462.85  E-value: 5.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652    1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIDEVHASRVAELV 80
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAAS--PRRDDGFEVISNPEFFKEGCA 158
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERsgLKLGEDFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  159 VSDCLRPDRiIVGGASPRALEQMRELYQPFsrNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIEQV 238
Cdd:TIGR03026 161 VHDLLHPDR-IVGGETEEAGEAVAELYSPI--IDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  239 RLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYhGELRGKVFAV 318
Cdd:TIGR03026 238 IEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL-GPLKGKTVLI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  319 WGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGERDDLqlvqckQDALEGADALVVVTEWQDYRVL 398
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDL------EEALKGADALVILTDHSEFKDL 390
                         410
                  ....*....|....*....
gi 497899652  399 DLDQLGEKLRDRAVFDGRN 417
Cdd:TIGR03026 391 DLEKIKDLMKGKVVVDTRN 409
UDPGDh_AglM NF041297
UDP-glucose 6-dehydrogenase AglM;
1-434 1.06e-115

UDP-glucose 6-dehydrogenase AglM;


Pssm-ID: 469194 [Multi-domain]  Cd Length: 429  Bit Score: 345.74  E-value: 1.06e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELL-RNGLDckRLSFTIDeVHASRVAEL 79
Cdd:NF041297   1 MNVSVIGSGYVGTTVAACFADLGHDVVNVDIDEDIVATINDGEAPIHEPGLDELVaEHAGD--RLRATTD-YDAVLETDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  80 VFIAVGTPAQADGKADLSQVFAVLRSV---LRHADGARIIVNKSTSPVGTVDRLLA---EIAASPRRDDGFEVISNPEFF 153
Cdd:NF041297  78 TFLALPTPSNDDGSIDLSIMEAGAESLgeaLAEKDDDHLVVVKSTVVPGTTEEVIApalEDASGKTAGEDFGVAMNPEFL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 154 KEGCAVSDCLRPDRIIVGGASPRALEQMRELYQP-FSRNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVG 232
Cdd:NF041297 158 REGSAVEDFLNPDKVVLGADDDRALDRLREVYEPlVEAADAPVVETGIREAEMIKYANNAFLASKVSLINDLGNICKEFG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 233 ADIEQVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKNIHAHYhgELR 312
Cdd:NF041297 238 VDAYEVADAIGLDDRIGEQFLRSGVGWGGSCFPKDVAAIIAAAREAGYEPALLEAAVEVNDRQPERLLDLLDEHV--DVA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 313 GKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYgerDDLQLVQCKQDALEGADALVVVTEW 392
Cdd:NF041297 316 GERVAVLGLAFKPGTDDVRNSRAIPVIEGLQERGADVVAYDPVATENMRERF---PDIEYADSAADALDGADGALVVTDW 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 497899652 393 QDYRvlDLDQLGEKLRDRAVFDGRNLFDPsqlRDaGFAYYGI 434
Cdd:NF041297 393 DEFA--ALDEEFDAMATPVVVDGRRIVER---RD-GITYEGL 428
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-436 4.44e-88

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 276.17  E-value: 4.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLA----EVghTVCCMDVDSKRIDALREGICPIFEPGLGELLRnglDC--KRLSFTIDEVHAS 74
Cdd:PLN02353   2 VKICCIGAGYVGGPTMAVIAlkcpDI--EVVVVDISVPRIDAWNSDQLPIYEPGLDEVVK---QCrgKNLFFSTDVEKHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  75 RVAELVFIAVGTPAQADG-----KADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLlAEIAASPRRDDGFEVISN 149
Cdd:PLN02353  77 AEADIVFVSVNTPTKTRGlgagkAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAI-EKILTHNSKGINFQILSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 150 PEFFKEGCAVSDCLRPDRIIVGG----ASPRALEQMRELYQ---PfsrnREKFVIMDARSAELAKYAANCLLATKISFIN 222
Cdd:PLN02353 156 PEFLAEGTAIEDLFKPDRVLIGGretpEGQKAVQALKDVYAhwvP----EERIITTNLWSAELSKLAANAFLAQRISSVN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 223 EMANLAEQVGADIEQVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGV-ETA-LLNAVEQVNRRQKHRLF 300
Cdd:PLN02353 232 AMSALCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLpEVAeYWKQVIKMNDYQKSRFV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 301 KNIHAHYHGELRGKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEA----------------IRHHY 364
Cdd:PLN02353 312 NRVVSSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEqiqrdlsmnkfdwdhpRHLQP 391
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497899652 365 GERDDLQLVQCKQDALE---GADALVVVTEWQDYRVLDLDQLGEKLRDRA-VFDGRNLFDPSQLRDAGFAYYGIGR 436
Cdd:PLN02353 392 MSPTAVKQVSVVWDAYEatkGAHGICILTEWDEFKTLDYQKIYDNMQKPAfVFDGRNVLDHEKLREIGFIVYSIGK 467
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-420 5.09e-76

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 243.04  E-value: 5.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   2 KVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGlGELLRNGLDCKRLSFTiDEVHASRVAELVF 81
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRAT-TDPEALAEADVVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  82 IAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAAsprRDDGFEVisNPEFFkegCAVSd 161
Cdd:COG0677   79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILE---KRSGLKA--GEDFF---LAYS- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 162 clrPDRI--------------IVGGASPRALEQMRELYQPFSRNREkFVIMDARSAELAKYAANCLLATKISFINEMANL 227
Cdd:COG0677  150 ---PERInpgnklhelrnipkVVGGITPESAERAAALYGSVVTAGV-VPVSSIKVAEAAKLIENTYRDVNIALANELALI 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 228 AEQVGADIEQVRLGIGSDPRigYDFIYPGCGFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQ-KH---RLFKNI 303
Cdd:COG0677  226 CDRLGIDVWEVIEAANTKPG--FLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMpEYvveRVVKAL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 304 HAHyHGELRGKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEA-IRHHYGERDDLqlvqckQDALEG 382
Cdd:COG0677  304 NEA-GKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEeVEGEYGELVDL------EEALEG 376
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 497899652 383 ADALVVVTEWQDYRVLDLDQLGEKlRDRAVFDGRNLFD 420
Cdd:COG0677  377 ADAVVLAVDHDEFDELDPEELRLK-GAKVVVDTRGVLD 413
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-184 2.71e-65

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: 207.49  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652    1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDcKRLSFTIDEVHASRVAELV 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVS-GRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   81 FIAVGTPA-QADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDRLLAEIAA--SPRRDDGFEVISNPEFFKEGC 157
Cdd:pfam03721  80 FIAVGTPSkKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEegGKKVGVDFDVASNPEFLREGS 159
                         170       180
                  ....*....|....*....|....*..
gi 497899652  158 AVSDCLRPDRIIVGGASPRALEQMREL 184
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALEEL 186
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
1-379 8.39e-49

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 170.97  E-value: 8.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEvGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNglDCKRLSFTIDEVHASRVAELV 80
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS--DKIHFNATLDKNEAYRDADYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  81 FIAvgTPAQADGKADL---SQVFAVLRSVLRhADGARIIVNKSTSPVGTVdrllaeiAASPRRDDGFEVISNPEFFKEGC 157
Cdd:PRK15057  78 IIA--TPTDYDPKTNYfntSSVESVIKDVVE-INPYAVMVIKSTVPVGFT-------AAMHKKYRTENIIFSPEFLREGK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 158 AVSDCLRPDRIIVGGASPRAlEQMRELYQPFSRNRE-KFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIE 236
Cdd:PRK15057 148 ALYDNLHPSRIVIGERSERA-ERFAALLQEGAIKQNiPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNTR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 237 QVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIgtASENGVETALLNAVEQVNRRQKHRLFKNIHAHyhgelRGKVF 316
Cdd:PRK15057 227 QIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLL--ANYQSVPNNLISAIVDANRTRKDFIADAILSR-----KPQVV 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497899652 317 AVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAirHHYGERDDLQLVQCKQDA 379
Cdd:PRK15057 300 GIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKED--SFFNSRLERDLATFKQQA 360
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
202-293 7.31e-48

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: 159.08  E-value: 7.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  202 SAELAKYAANCLLATKISFINEMANLAEQVGADIEQVRLGIGSDPRIGYDFIYPGCGFGGSCFPKDLQALIGTASENGVE 281
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|..
gi 497899652  282 TALLNAVEQVNR 293
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 ...
317-420 7.29e-38

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: 133.01  E-value: 7.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   317 AVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYgerddLQLVQCKQDALEGADALVVVTEWQDYR 396
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG-----LTYVSDLEEALKGADAVVIATEHDEFR 75
                           90       100
                   ....*....|....*....|....
gi 497899652   397 VLDLDQLGEKLRDRAVFDGRNLFD 420
Cdd:smart00984  76 SLDPEELKDLMKKPVVVDGRNILD 99
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
317-421 3.72e-35

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


Pssm-ID: 427462 [Multi-domain]  Cd Length: 103  Bit Score: 125.77  E-value: 3.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  317 AVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQAIEAIRHHYGerDDLQLVQCKQDALEGADALVVVTEWQDYR 396
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALG--DGVTLVDDLEEALKGADAIVILTDHDEFK 78
                          90       100
                  ....*....|....*....|....*
gi 497899652  397 VLDLDQLGEKLRDRAVFDGRNLFDP 421
Cdd:pfam03720  79 SLDWEKLKKLMKPPVVFDGRNVLDP 103
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
2-406 2.13e-32

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 127.02  E-value: 2.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   2 KVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREGICPIFEPGLGELLRNGLDCKRLSFTIdevhASRVAELVF 81
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATT----TPEPADAFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  82 IAVGTPAQADGKADLSQVFAVLRS---VLRHADgarIIVNKSTSPVGTVDRlLAEIAASPRRDDGF----------EVIS 148
Cdd:PRK11064  81 IAVPTPFKGDHEPDLTYVEAAAKSiapVLKKGD---LVILESTSPVGATEQ-MAEWLAEARPDLTFpqqageqadiNIAY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 149 NPEFFKEGCAVSDCLRPDRIIvGGASPRALEQMRELYQPFSRNRekFVIMDARSAELAKYAANCLLATKISFINEMANLA 228
Cdd:PRK11064 157 CPERVLPGQVMVELIKNDRVI-GGMTPVCSARASELYKIFLEGE--CVVTNSRTAEMCKLTENSFRDVNIAFANELSLIC 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 229 EQVGADI-EQVRLGiGSDPRIgyDFIYPGCGFGGSCFPKD---------LQA-LIGTASE----------NGVETALLNA 287
Cdd:PRK11064 234 ADQGINVwELIRLA-NRHPRV--NILQPGPGVGGHCIAVDpwfivaqnpQQArLIRTAREvndgkphwviDQVKAAVADC 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 288 VEQVNRRQKHrlfknihahyhgelrgKVFAVWGLAFKPNTDDIREASSHALLE--ALWAAGaRVQAHDPQaIEAIRHHYG 365
Cdd:PRK11064 311 LAATDKRASE----------------VKIACFGLAFKPNIDDLRESPAMEIAEliAQWHSG-ETLVVEPN-IHQLPKKLD 372
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 497899652 366 ERddLQLVQCkQDALEGADALVVVTEWQDYRVLDLDQLGEK 406
Cdd:PRK11064 373 GL--VTLVSL-DEALATADVLVMLVDHSQFKAINGDNVHQQ 410
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
1-426 1.79e-11

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 65.48  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEvGHTVCCMDVDSKRIDALREGICPIFEPGLGELLrnglDCKRLSFTiDEVHASRVAELV 80
Cdd:PRK15182   7 VKIAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELKNGVDVNLETTEEELR----EARYLKFT-SEIEKIKECNFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  81 FIAVGTPAQADGKADLSQVFAVLRSVLRHADGARIIVNKSTSPVGTVDR----LLAEIAASPRRDDgFEVISNPEFFKEG 156
Cdd:PRK15182  81 IITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEecvpILARMSGMTFNQD-FYVGYSPERINPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 157 cAVSDCLRPDRIIVGGASPRALEQMRELYQPFSrNREKFVIMDARSAELAKYAANCLLATKISFINEMANLAEQVGADIE 236
Cdd:PRK15182 160 -DKKHRLTNIKKITSGSTAQIAELIDEVYQQII-SAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 237 QVRLGIGSDprigYDFI--YPGCgFGGSCFPKDLQALIGTASENGVETALLNAVEQVNRRQKHRLFKN-IHAHYHG--EL 311
Cdd:PRK15182 238 AVLRAAGSK----WNFLpfRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQlIKAMIKKgiNV 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 312 RGKVFAVWGLAFKPNTDDIREASSHALLEALWAAGARVQAHDPQA-IEAIRHHYGerddlqLVQCKQDALEGADALVVVT 390
Cdd:PRK15182 313 EGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVdAEEVRREYG------IIPVSEVKSSHYDAIIVAV 386
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 497899652 391 EWQDYRVLDLDQLGEKLRDRAVFDGRNLFDPSQLRD 426
Cdd:PRK15182 387 GHQQFKQMGSEDIRGFGKDKHVLYDLKYVLPAEQSD 422
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
1-138 3.07e-05

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 45.61  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALREgicpifepglgellrNGLDCKRLSFTIDEVHASRVAEL- 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNE---------------NGLRLEDGEITVPVLAADDPAELg 65
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497899652  80 ----VFIAVgtpaqadgKADlsQVFAVLRSVLRHADGARIIV---NKstspVGTVDRLLAEIAASP 138
Cdd:PRK06522  66 pqdlVILAV--------KAY--QLPAALPSLAPLLGPDTPVLflqNG----VGHLEELAAYIGPER 117
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
1-212 4.42e-05

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 45.23  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMdVDSKRIDALREGicpifepGLgELLRNGLDCKRLSFTI-DEVHASRVAEL 79
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLV-ARGAHAEALREN-------GL-RLESPDGDRTTVPVPAvTDPEELGPADL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652  80 VFIAVgtpaqadgKA-DLSQVFAVLRSVLrhADGARIIV--NkstsPVGTVDRLLAEIAASPrrddgfeVIS---NPEFF 153
Cdd:COG1893   72 VLVAV--------KAyDLEAAAEALAPLL--GPDTVVLSlqN----GLGHEERLAEALGAER-------VLGgvvTIGAT 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652 154 KEGCAVSDCLRPDRIIVGGASPRALEQMRELYQPFSRNREKFVIM-DARSAELAKYAANC 212
Cdd:COG1893  131 REEPGVVRHTGGGRLVLGELDGGPSERLEALAELLEAAGIPVEVSdDIRGALWEKLLLNA 190
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
1-116 8.81e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 38.09  E-value: 8.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497899652   1 MKVTVFGTGYVGLTLAACLAEVGHTVCCMDVDSKRIDALRE-GICPIFEPGLgELLRNgldckrLSFTIDEVHASRVAEL 79
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINEtRENPRYLPGV-KLPEN------LRATSDLEEALAGADL 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 497899652  80 VFIAVgtPAQAdgkadLSQVFAVLRSVLRhaDGARII 116
Cdd:COG0240   74 VLLAV--PSQA-----LREVLEQLAPLLP--PGAPVV 101
 
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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