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Conserved domains on  [gi|918766061|ref|WP_052613812|]
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UDP-glucose/GDP-mannose dehydrogenase family protein [Mycobacterium tuberculosis]

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];
1-439 0e+00

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


:

Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 632.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTDYDMAADFADVH 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  81 FLGVGTPQKigEYG-ADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHR-AGALAPRGVDVEIAWNPEFLREGF 158
Cdd:COG1004   81 FIAVGTPSD--EDGsADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIiAEELRGAGVDFDVVSNPEFLREGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 159 AVHDTLNPDRIVLEVqdDSTRAEVAVRELYAPLLAAGVPFLVTDLQTAELVKVSANAFLATKISFINAISEVCEAAGADV 238
Cdd:COG1004  159 AVEDFLRPDRIVIGV--DSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 239 SQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTACGGSLLG 318
Cdd:COG1004  237 EEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHLGGDLKG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 319 ANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFP-TLNYAVSVAEACERADAVLVLTEWREF 397
Cdd:COG1004  315 KTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPdDITYADDAYEALEGADALVILTEWPEF 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 918766061 398 IDLEPADLANRVRARVIVDGRNCLDVTRWRRAGWRVFRLGVP 439
Cdd:COG1004  395 RALDFARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
 
Name Accession Description Interval E-value
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-439 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 632.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTDYDMAADFADVH 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  81 FLGVGTPQKigEYG-ADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHR-AGALAPRGVDVEIAWNPEFLREGF 158
Cdd:COG1004   81 FIAVGTPSD--EDGsADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIiAEELRGAGVDFDVVSNPEFLREGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 159 AVHDTLNPDRIVLEVqdDSTRAEVAVRELYAPLLAAGVPFLVTDLQTAELVKVSANAFLATKISFINAISEVCEAAGADV 238
Cdd:COG1004  159 AVEDFLRPDRIVIGV--DSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 239 SQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTACGGSLLG 318
Cdd:COG1004  237 EEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHLGGDLKG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 319 ANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFP-TLNYAVSVAEACERADAVLVLTEWREF 397
Cdd:COG1004  315 KTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPdDITYADDAYEALEGADALVILTEWPEF 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 918766061 398 IDLEPADLANRVRARVIVDGRNCLDVTRWRRAGWRVFRLGVP 439
Cdd:COG1004  395 RALDFARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-419 1.59e-164

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: 469.01  E-value: 1.59e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061    1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTDYDMAADFADVH 80
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   81 FLGVGTPQKIgEYGADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHRAGALAP--RGVDVEIAWNPEFLREGF 158
Cdd:TIGR03026  81 IICVPTPLKE-DGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGlkLGEDFYLAYNPEFLREGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  159 AVHDTLNPDRIVLEVQDDSTRaevAVRELYAPLLAAgvPFLVTDLQTAELVKVSANAFLATKISFINAISEVCEAAGADV 238
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGE---AVAELYSPIIDG--PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  239 SQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTACgGSLLG 318
Cdd:TIGR03026 235 YEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL-GPLKG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  319 ANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFPTLNYAvsvAEACERADAVLVLTEWREFI 398
Cdd:TIGR03026 312 KTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDL---EEALKGADALVILTDHSEFK 388
                         410       420
                  ....*....|....*....|.
gi 918766061  399 DLEPADLANRVRARVIVDGRN 419
Cdd:TIGR03026 389 DLDLEKIKDLMKGKVVVDTRN 409
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
7-439 2.42e-82

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 261.15  E-value: 2.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   7 GTGYLGA-THAVGMAQLGH-EVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDnlAAGR-LRFTTDYDMAADFADVHFLG 83
Cdd:PLN02353   8 GAGYVGGpTMAVIALKCPDiEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQ--CRGKnLFFSTDVEKHVAEADIVFVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  84 VGTPQKIGEYG----ADLRHVHAVidalvPRLVRAS-----ILVGKSTVPVGTAaELGHRAGALAPRGVDVEIAWNPEFL 154
Cdd:PLN02353  86 VNTPTKTRGLGagkaADLTYWESA-----ARMIADVsksdkIVVEKSTVPVKTA-EAIEKILTHNSKGINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 155 REGFAVHDTLNPDRIVLEVQD--DSTRAEVAVRELYAPLlaagVP---FLVTDLQTAELVKVSANAFLATKISFINAISE 229
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGREtpEGQKAVQALKDVYAHW----VPeerIITTNLWSAELSKLAANAFLAQRISSVNAMSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 230 VCEAAGADVSQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADQALTFLREVDSINMRRRTKMVELAT 309
Cdd:PLN02353 236 LCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 310 TACGGSLLGANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPK------ALDNAHRLF------------PT 371
Cdd:PLN02353 316 SSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQvteeqiQRDLSMNKFdwdhprhlqpmsPT 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918766061 372 LNYAVSVA----EACERADAVLVLTEWREFIDLEPADL-ANRVRARVIVDGRNCLDVTRWRRAGWRVFRLGVP 439
Cdd:PLN02353 396 AVKQVSVVwdayEATKGAHGICILTEWDEFKTLDYQKIyDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKP 468
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-187 4.49e-82

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: 250.63  E-value: 4.49e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061    1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAaGRLRFTTDYDMAADFADVH 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVS-GRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   81 FLGVGTPQKIGEYGADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHRAGALAPR--GVDVEIAWNPEFLREGF 158
Cdd:pfam03721  80 FIAVGTPSKKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKkvGVDFDVASNPEFLREGS 159
                         170       180
                  ....*....|....*....|....*....
gi 918766061  159 AVHDTLNPDRIVLEVQDDSTRAevAVREL 187
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEA--ALEEL 186
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
322-422 4.03e-35

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: 125.70  E-value: 4.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   322 AVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFptLNYAVSVAEACERADAVLVLTEWREFIDLE 401
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG--LTYVSDLEEALKGADAVVIATEHDEFRSLD 78
                           90       100
                   ....*....|....*....|.
gi 918766061   402 PADLANRVRARVIVDGRNCLD 422
Cdd:smart00984  79 PEELKDLMKKPVVVDGRNILD 99
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
1-115 1.11e-03

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133428 [Multi-domain]  Cd Length: 308  Bit Score: 40.94  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQ--LGHEVVGVDIDP----GKVAKLAGGdIPFYEPglrklltDNLAAGrlrfttDYDMAA 74
Cdd:cd05292    1 MKVAIVGAGFVGSTTAYALLLrgLASEIVLVDINKakaeGEAMDLAHG-TPFVKP-------VRIYAG------DYADCK 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 918766061  75 DfADVHFLGVGTPQKIGEYGADLRHVHA-VIDALVPRLVRAS 115
Cdd:cd05292   67 G-ADVVVITAGANQKPGETRLDLLKRNVaIFKEIIPQILKYA 107
 
Name Accession Description Interval E-value
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-439 0e+00

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 632.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTDYDMAADFADVH 80
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  81 FLGVGTPQKigEYG-ADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHR-AGALAPRGVDVEIAWNPEFLREGF 158
Cdd:COG1004   81 FIAVGTPSD--EDGsADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIiAEELRGAGVDFDVVSNPEFLREGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 159 AVHDTLNPDRIVLEVqdDSTRAEVAVRELYAPLLAAGVPFLVTDLQTAELVKVSANAFLATKISFINAISEVCEAAGADV 238
Cdd:COG1004  159 AVEDFLRPDRIVIGV--DSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 239 SQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTACGGSLLG 318
Cdd:COG1004  237 EEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHLGGDLKG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 319 ANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFP-TLNYAVSVAEACERADAVLVLTEWREF 397
Cdd:COG1004  315 KTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPdDITYADDAYEALEGADALVILTEWPEF 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 918766061 398 IDLEPADLANRVRARVIVDGRNCLDVTRWRRAGWRVFRLGVP 439
Cdd:COG1004  395 RALDFARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-419 1.59e-164

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: 469.01  E-value: 1.59e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061    1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTDYDMAADFADVH 80
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   81 FLGVGTPQKIgEYGADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHRAGALAP--RGVDVEIAWNPEFLREGF 158
Cdd:TIGR03026  81 IICVPTPLKE-DGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGlkLGEDFYLAYNPEFLREGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  159 AVHDTLNPDRIVLEVQDDSTRaevAVRELYAPLLAAgvPFLVTDLQTAELVKVSANAFLATKISFINAISEVCEAAGADV 238
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGE---AVAELYSPIIDG--PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  239 SQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTACgGSLLG 318
Cdd:TIGR03026 235 YEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL-GPLKG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  319 ANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFPTLNYAvsvAEACERADAVLVLTEWREFI 398
Cdd:TIGR03026 312 KTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDL---EEALKGADALVILTDHSEFK 388
                         410       420
                  ....*....|....*....|.
gi 918766061  399 DLEPADLANRVRARVIVDGRN 419
Cdd:TIGR03026 389 DLDLEKIKDLMKGKVVVDTRN 409
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
7-439 2.42e-82

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 261.15  E-value: 2.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   7 GTGYLGA-THAVGMAQLGH-EVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDnlAAGR-LRFTTDYDMAADFADVHFLG 83
Cdd:PLN02353   8 GAGYVGGpTMAVIALKCPDiEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQ--CRGKnLFFSTDVEKHVAEADIVFVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  84 VGTPQKIGEYG----ADLRHVHAVidalvPRLVRAS-----ILVGKSTVPVGTAaELGHRAGALAPRGVDVEIAWNPEFL 154
Cdd:PLN02353  86 VNTPTKTRGLGagkaADLTYWESA-----ARMIADVsksdkIVVEKSTVPVKTA-EAIEKILTHNSKGINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 155 REGFAVHDTLNPDRIVLEVQD--DSTRAEVAVRELYAPLlaagVP---FLVTDLQTAELVKVSANAFLATKISFINAISE 229
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGREtpEGQKAVQALKDVYAHW----VPeerIITTNLWSAELSKLAANAFLAQRISSVNAMSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 230 VCEAAGADVSQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGADQALTFLREVDSINMRRRTKMVELAT 309
Cdd:PLN02353 236 LCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 310 TACGGSLLGANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPK------ALDNAHRLF------------PT 371
Cdd:PLN02353 316 SSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQvteeqiQRDLSMNKFdwdhprhlqpmsPT 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918766061 372 LNYAVSVA----EACERADAVLVLTEWREFIDLEPADL-ANRVRARVIVDGRNCLDVTRWRRAGWRVFRLGVP 439
Cdd:PLN02353 396 AVKQVSVVwdayEATKGAHGICILTEWDEFKTLDYQKIyDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKP 468
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-187 4.49e-82

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: 250.63  E-value: 4.49e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061    1 MRCSVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAaGRLRFTTDYDMAADFADVH 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVS-GRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   81 FLGVGTPQKIGEYGADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELGHRAGALAPR--GVDVEIAWNPEFLREGF 158
Cdd:pfam03721  80 FIAVGTPSKKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKkvGVDFDVASNPEFLREGS 159
                         170       180
                  ....*....|....*....|....*....
gi 918766061  159 AVHDTLNPDRIVLEVQDDSTRAevAVREL 187
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEA--ALEEL 186
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
4-422 2.51e-72

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 233.41  E-value: 2.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   4 SVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGlRKLLTDNLAAGRLRFTTDYDMAADfADVHFLG 83
Cdd:COG0677    3 AVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEALAE-ADVVIIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  84 VGTPqkIGEYG-ADLRHVHAVIDALVPRLVRASILVGKSTVPVGT---------AAELGHRAGalaprgVDVEIAWNPEF 153
Cdd:COG0677   81 VPTP--LDEDKePDLSYLESASETIAPHLKPGDLVVLESTVYPGTteevcvpilEKRSGLKAG------EDFFLAYSPER 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 154 LREGFAVHDTLNPDRIVLEVQDDSTRAevaVRELYAPLLAAGVpFLVTDLQTAELVKVSANAFLATKISFINAISEVCEA 233
Cdd:COG0677  153 INPGNKLHELRNIPKVVGGITPESAER---AAALYGSVVTAGV-VPVSSIKVAEAAKLIENTYRDVNIALANELALICDR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 234 AGADVSQLADALGYDPRigRQCLNAGLGFGGGCLPKDIRAFMARAGELGADqaLTFLREVDSINMRRRTKMVELATTA-- 311
Cdd:COG0677  229 LGIDVWEVIEAANTKPG--FLIFYPGPGVGGHCIPVDPYYLTWKARELGYH--PRLILAAREINDSMPEYVVERVVKAln 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 312 -CGGSLLGANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKAldNAHRLFPTLNYAVSVAEACERADAVLV 390
Cdd:COG0677  305 eAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYV--DEEEVEGEYGELVDLEEALEGADAVVL 382
                        410       420       430
                 ....*....|....*....|....*....|..
gi 918766061 391 LTEWREFIDLEPADLANRvRARVIVDGRNCLD 422
Cdd:COG0677  383 AVDHDEFDELDPEELRLK-GAKVVVDTRGVLD 413
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
1-359 1.50e-41

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 151.71  E-value: 1.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQlGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLtdnlAAGRLRFTTDYDMAADFADVH 80
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLNDRISPIVDKEIQQFL----QSDKIHFNATLDKNEAYRDAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  81 FLGVGTPQkigEYGADLRH-----VHAVIDALVpRLVRASILVGKSTVPVGTAAelghragALAPRGVDVEIAWNPEFLR 155
Cdd:PRK15057  76 YVIIATPT---DYDPKTNYfntssVESVIKDVV-EINPYAVMVIKSTVPVGFTA-------AMHKKYRTENIIFSPEFLR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 156 EGFAVHDTLNPDRIVleVQDDSTRAEvavreLYAPLLAAG-----VPFLVTDLQTAELVKVSANAFLATKISFINAISEV 230
Cdd:PRK15057 145 EGKALYDNLHPSRIV--IGERSERAE-----RFAALLQEGaikqnIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSY 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 231 CEAAGADVSQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELgADQALTFLREVDsinmRRRTKMVELATT 310
Cdd:PRK15057 218 AESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQSV-PNNLISAIVDAN----RTRKDFIADAIL 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 918766061 311 ACGGSLLGANIAVLgaafKPESDDVRDSPALNVAGQLQLNGATVHVYDP 359
Cdd:PRK15057 293 SRKPQVVGIYRLIM----KSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
205-297 2.51e-38

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: 134.04  E-value: 2.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  205 TAELVKVSANAFLATKISFINAISEVCEAAGADVSQLADALGYDPRIGRQCLNAGLGFGGGCLPKDIRAFMARAGELGAD 284
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|...
gi 918766061  285 qaLTFLREVDSIN 297
Cdd:pfam00984  81 --ARLLEAAREVN 91
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
4-416 4.25e-37

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 140.12  E-value: 4.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   4 SVFGTGYLGATHAVGMAQLGHEVVGVDIDPGKVAKLAGGDIPFYEPGLRKLLTDNLAAGRLRFTTdydmAADFADVHFLG 83
Cdd:PRK11064   7 SVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATT----TPEPADAFLIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  84 VGTPQKiGEYGADLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAELG-------------HRAGALAprgvDVEIAWN 150
Cdd:PRK11064  83 VPTPFK-GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAewlaearpdltfpQQAGEQA----DINIAYC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 151 PEFLREGFAVHDTLNPDRIVLEVQDDSTRAEVavrELYAPLLAAGVpfLVTDLQTAELVKVSANAFLATKISFINAISEV 230
Cdd:PRK11064 158 PERVLPGQVMVELIKNDRVIGGMTPVCSARAS---ELYKIFLEGEC--VVTNSRTAEMCKLTENSFRDVNIAFANELSLI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 231 CEAAGADVSQLADALGYDPRIgrQCLNAGLGFGGGCLPKDIRAFMARAGELGadQALTFLREV-DS-----INMRRRTKM 304
Cdd:PRK11064 233 CADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIVAQNPQQA--RLIRTAREVnDGkphwvIDQVKAAVA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 305 VELATTACGGSLLgaNIAVLGAAFKPESDDVRDSPALNVAGQL-QLNGATVHVYDPkaldNAHRLFPTLNYA---VSVAE 380
Cdd:PRK11064 309 DCLAATDKRASEV--KIACFGLAFKPNIDDLRESPAMEIAELIaQWHSGETLVVEP----NIHQLPKKLDGLvtlVSLDE 382
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 918766061 381 ACERADAVLVLTEWREFIDLEPadlaNRVRARVIVD 416
Cdd:PRK11064 383 ALATADVLVMLVDHSQFKAING----DNVHQQWVVD 414
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
322-422 4.03e-35

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: 125.70  E-value: 4.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   322 AVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFptLNYAVSVAEACERADAVLVLTEWREFIDLE 401
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG--LTYVSDLEEALKGADAVVIATEHDEFRSLD 78
                           90       100
                   ....*....|....*....|.
gi 918766061   402 PADLANRVRARVIVDGRNCLD 422
Cdd:smart00984  79 PEELKDLMKKPVVVDGRNILD 99
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
322-422 1.60e-33

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: 121.53  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  322 AVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDPKALDNAHRLFP-TLNYAVSVAEACERADAVLVLTEWREFIDL 400
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGdGVTLVDDLEEALKGADAIVILTDHDEFKSL 80
                          90       100
                  ....*....|....*....|..
gi 918766061  401 EPADLANRVRARVIVDGRNCLD 422
Cdd:pfam03720  81 DWEKLKKLMKPPVVFDGRNVLD 102
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
1-359 1.01e-09

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 60.09  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQlGHEVVGVDIDPGKVAKLAGG---DIPFYEPGLRKlltdnlaAGRLRFTTDYDmaaDFA 77
Cdd:PRK15182   7 VKIAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELKNGvdvNLETTEEELRE-------ARYLKFTSEIE---KIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061  78 DVHFLGVGTPQKIGEYGA-DLRHVHAVIDALVPRLVRASILVGKSTVPVGTAAE-----LGHRAGALAPRgvDVEIAWNP 151
Cdd:PRK15182  76 ECNFYIITVPTPINTYKQpDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEecvpiLARMSGMTFNQ--DFYVGYSP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 152 EFLREGFAVHDTLNPDRIVlevqdDSTRAEVA--VRELYAPLLAAGVpFLVTDLQTAELVKVSANAFLATKISFINAISE 229
Cdd:PRK15182 154 ERINPGDKKHRLTNIKKIT-----SGSTAQIAelIDEVYQQIISAGT-YKAESIKVAEAAKVIENTQRDLNIALVNELAI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061 230 VCEAAGADVSQLADALGydPRIGRQCLNAGLgFGGGCLPKDIRAFMARAGELG--ADQALTFLREVDSINMRRRTKMVEl 307
Cdd:PRK15182 228 IFNRLNIDTEAVLRAAG--SKWNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGyyPEIILAGRRLNDNMGNYVSEQLIK- 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 918766061 308 ATTACGGSLLGANIAVLGAAFKPESDDVRDSPALNVAGQLQLNGATVHVYDP 359
Cdd:PRK15182 304 AMIKKGINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDP 355
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
1-115 1.11e-03

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133428 [Multi-domain]  Cd Length: 308  Bit Score: 40.94  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918766061   1 MRCSVFGTGYLGATHAVGMAQ--LGHEVVGVDIDP----GKVAKLAGGdIPFYEPglrklltDNLAAGrlrfttDYDMAA 74
Cdd:cd05292    1 MKVAIVGAGFVGSTTAYALLLrgLASEIVLVDINKakaeGEAMDLAHG-TPFVKP-------VRIYAG------DYADCK 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 918766061  75 DfADVHFLGVGTPQKIGEYGADLRHVHA-VIDALVPRLVRAS 115
Cdd:cd05292   67 G-ADVVVITAGANQKPGETRLDLLKRNVaIFKEIIPQILKYA 107
 
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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