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Reviewed, UniProtKB/Swiss-Prot P96718 (YWQF_BACSU)

Last modified February 9, 2010. Version 73. 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 ywqF
      Short name=UDP-Glc dehydrogenase
      Short name=UDP-GlcDH
      Short name=UDPGDH
    EC=1.1.1.22
Gene names
Name: ywqF
Ordered Locus Names: BSU36230
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length440 AA.
Sequence statusComplete.
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. Ref.4

Catalytic activity

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

Enzyme regulation

Competitively inhibited by UDP-glucose. Activated by phosphorylation, which may increase affinity for NAD+; inhibited by dephosphorylation. Ref.3

Pathway

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

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Phosphorylated on tyrosine residue(s). Phosphorylated by ywqD and dephosphorylated by ywqE in vitro. Ref.4 Ref.3

Sequence similarities

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

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

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 – 440440UDP-glucose 6-dehydrogenase ywqF
PRO_0000253341

Regions

Nucleotide binding2 – 1918NAD Potential

Sites

Active site2601 By similarity

Experimental info

Mutagenesis101Y → F: 30-fold decrease in activity but no decrease in the overall phosphorylation level. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P96718-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1ADA9454EBE1F645

FASTA44047,784
        10         20         30         40         50         60 
MNITVIGTGY VGLVTGVSLS EIGHHVTCID IDAHKIDEMR KGISPIFEPG LEELMRKNTA 

        70         80         90        100        110        120 
DGRLNFETSY EKGLAQADII FIAVGTPQKS DGHANLEQIT DAAKRIAKHV KRDTVVVTKS 

       130        140        150        160        170        180 
TVPVGTNDLI NGLITEHLAE PVSISVASNP EFLREGSAIY DTFHGDRIVI GTADEKTANT 

       190        200        210        220        230        240 
LEELFRPFQI PIYQTDIRSA EMIKYASNAF LATKISFINE ISNICEKVGA DIEAVAYGMG 

       250        260        270        280        290        300 
QDKRIGSQFL KAGIGYGGSC FPKDTNALVQ IAGNVEHDFE LLKSVIKVNN NQQAMLVDKA 

       310        320        330        340        350        360 
LNRLGGVTGK TIALLGLSFK PNTDDMREAP SIVIADRLAA LDARIRAYDP IAVSHAKHVL 

       370        380        390        400        410        420 
PQAVEYKETI EEAVKGSDAV MILTDWADIK QFPLAAYQDL METPLIFDGR NCYTLDEALA 

       430        440 
AGVEYYSVGR KAVVPSGAIQ

« Hide

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References

« Hide 'large scale' references
[1]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed: 9353933] [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]"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.
[4]"How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF."
Mijakovic I., Petranovic D., Deutscher J.
J. Mol. Microbiol. Biotechnol. 8:19-25(2004) [PubMed: 15741737] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-10, PHOSPHORYLATION.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z92952 Genomic DNA. Translation: CAB07444.1.
AL009126 Genomic DNA. Translation: CAB15640.1.
PIRA70067.
RefSeqNP_391504.1.

3D structure databases

HSSPHSSP built from PDB template 1MV8 based on UniProtKB P11759.
SMRP96718. Positions 2-431.
ModBaseSearch...

PTM databases

PhosSiteP96718.

Genome annotation databases

GeneID936890.
GenomeReviewsGene locus BSU36230 in contig AL009126_GR.
KEGGbsu:BSU36230.
NMPDRfig|224308.1.peg.3630.

Organism-specific databases

SubtiListBG12510. ywqF. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG400967.
OMALEGANVC.
PhylomeDBP96718.

Enzyme and pathway databases

BioCycSUBTI:BSU36230-MONOMER.
BRENDA1.1.1.22. 150.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 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.
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 nameYWQF_BACSU
AccessionPrimary (citable) accession number: P96718
Secondary accession number(s): Q795B4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 1, 1997
Last modified: February 9, 2010
This is version 73 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