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O32271 (TUAD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucose 6-dehydrogenase TuaD

Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22
Alternative name(s):
Teichuronic acid biosynthesis protein TuaD
Gene names
Name:tuaD
Synonyms:yvhD
Ordered Locus Names:BSU35580
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.

Catalytic activity

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

Enzyme regulation

Activated by phosphorylation; inhibited by dephosphorylation. Ref.4

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.

Subcellular location

Cytoplasm.

Induction

By phosphate starvation, via the PhoP/PhoR two-component regulatory system. Ref.4

Post-translational modification

Phosphorylated by YwqD and dephosphorylated by YwqE in vitro. Ref.4

Miscellaneous

The nature of the anionic polymer present in the cell wall of B.subtilis depends on phosphate availability. Under phosphate-replete growth conditions teichoic acids are present, whereas under phosphate-depleted conditions, at least part of the wall teichoic acid is replaced with teichuronic acid, a non-phosphate containing anionic polymer. The synthesis of teichuronic acid is accompanied by degradation of teichoic acid and reutilization of liberated phosphate for other cellular processes such as nucleic acid synthesis.

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Stress response
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-glucuronate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

polysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

UDP-glucose 6-dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461UDP-glucose 6-dehydrogenase TuaD
PRO_0000074075

Regions

Nucleotide binding3 – 2018NAD Potential

Sites

Active site2611 By similarity

Sequences

Sequence LengthMass (Da)Tools
O32271 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F3B4D189FEC90095

FASTA46149,816
        10         20         30         40         50         60 
MKKIAVIGTG YVGLVSGTCF AEIGNKVVCC DIDESKIRSL KNGVIPIYEP GLADLVEKNV 

        70         80         90        100        110        120 
LDQRLTFTND IPSAIRASDI IYIAVGTPMS KTGEADLTYV KAAAKTIGEH LNGYKVIVNK 

       130        140        150        160        170        180 
STVPVGTGKL VQSIVQKASK GRYSFDVVSN PEFLREGSAI HDTMNMERAV IGSTSHKAAA 

       190        200        210        220        230        240 
IIEELHQPFH APVIKTNLES AEMIKYAANA FLATKISFIN DIANICERVG ADVSKVADGV 

       250        260        270        280        290        300 
GLDSRIGRKF LKAGIGFGGS CFPKDTTALL QIAKSAGYPF KLIEAVIETN EKQRVHIVDK 

       310        320        330        340        350        360 
LLTVMGSVKG RTISVLGLAF KPNTNDVRSA PALDIIPMLQ QLGAHVKAYD PIAIPEASAI 

       370        380        390        400        410        420 
LGEQVEYYTD VYAAMEDTDA CLILTDWPEV KEMELVKVKT LLKQPVIIDG RNLFSLEEMQ 

       430        440        450        460 
AAGYIYHSIG RPAVRGTEPS DKYFPGLPLE ELAKDLGSVN L 

« Hide

References

« Hide 'large scale' references
[1]"Teichuronic acid operon of Bacillus subtilis 168."
Soldo B., Lazarevic V., Pagni M., Karamata D.
Mol. Microbiol. 31:795-805(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis."
Pagni M., Lazarevic V., Soldo B., Karamata D.
Microbiology 145:1049-1053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 168.
[4]"Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases."
Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E., Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.
EMBO J. 22:4709-4718(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF015609 Genomic DNA. Translation: AAB94865.1.
AL009126 Genomic DNA. Translation: CAB15575.1.
PIRF69727.
RefSeqNP_391438.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32271.
SMRO32271. Positions 3-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU35580.

PTM databases

PhosSiteP0604163.

Proteomic databases

PaxDbO32271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15575; CAB15575; BSU35580.
GeneID936766.
KEGGbsu:BSU35580.
PATRIC18979124. VBIBacSub10457_3724.

Organism-specific databases

GenoListBSU35580. [Micado]

Phylogenomic databases

eggNOGCOG1004.
HOGENOMHOG000153773.
KOK00012.
OMAVEWARIA.
OrthoDBEOG6ZSP7N.
PhylomeDBO32271.

Enzyme and pathway databases

BioCycBSUB:BSU35580-MONOMER.
RETL1328306-WGS:GSTH-3291-MONOMER.
UniPathwayUPA00038; UER00491.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
IPR028357. UDPglc_DH_bac.
[Graphical view]
PANTHERPTHR11374. PTHR11374. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTUAD_BACSU
AccessionPrimary (citable) accession number: O32271
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList