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Reviewed, UniProtKB/Swiss-Prot O32271 (TUAD_BACSU)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    UDP-glucose 6-dehydrogenase
      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 [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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-glucuronic acid biosynthesis; UDP-glucuronic acid from UDP-glucose: step 1/1.

Subcellular location

Cytoplasm.

Induction

By phosphate starvation, via the phoP/phoR two-component regulatory system.

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.

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Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Stress response
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

UDP-glucose 6-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461UDP-glucose 6-dehydrogenase
PRO_0000074075

Regions

Nucleotide binding3 – 2018NAD Potential

Sites

Active site2611 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O32271-1 [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

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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: 10048024] [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: 9384377] [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: 10376820] [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: 12970183] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION.

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Cross-references

Sequence databases

AF015609 Genomic DNA. Translation: AAB94865.1.
AL009126 Genomic DNA. Translation: CAB15575.1.
PIRF69727.
RefSeqNP_391438.1.

3D structure databases

HSSPHSSP built from PDB template 1MFZ based on UniProtKB P11759.
ModBaseSearch...

PTM databases

PhosSiteO32271.

Genome annotation databases

GeneID936766.
GenomeReviewsGene locus BSU35580 in contig AL009126_GR.
KEGGbsu:BSU35580.
NMPDRfig|224308.1.peg.3564.

Organism-specific databases

SubtiListBG12691. tuaD. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32271.
OMAO32271. CLADVGH.

Enzyme and pathway databases

BioCycBSUB224308:BSU3555-MON.
BRENDA1.1.1.22. 150.

Family and domain databases

InterProIPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR014028. UDP-Glc/GDP-Man_DH_dimer-bd.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.
PANTHERPTHR11374. UDPG_MGDP_DH_Creg. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

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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: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents