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UniProtKB/Swiss-Prot entry P96718


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name YWQF_BACSU
Primary accession number P96718
Secondary accession number Q795B4
Integrated into Swiss-Prot on October 17, 2006
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 59)
Name and origin of the protein
Protein name UDP-glucose 6-dehydrogenase
Synonyms UDP-Glc dehydrogenase
UDP-GlcDH
UDPGDH
EC 1.1.1.22
Gene name
Name: ywqF
OrderedLocusNames: BSU36230
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9353933 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).";
Microbiology 143:3313-3328(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PHOSPHORYLATION, AND ENZYME REGULATION.
DOI=10.1093/emboj/cdg458; PubMed=12970183 [NCBI, ExPASy, EBI, Israel, Japan]
Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E., Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.;
"Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.";
EMBO J. 22:4709-4718(2003).
[4]
FUNCTION, MUTAGENESIS OF TYR-10, AND PHOSPHORYLATION.
DOI=10.1159/000082077; PubMed=15741737 [NCBI, ExPASy, EBI, Israel, Japan]
Mijakovic I., Petranovic D., Deutscher J.;
"How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF.";
J. Mol. Microbiol. Biotechnol. 8:19-25(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z92952; CAB07444.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99122; CAB15640.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A70067; A70067.
RefSeq NP_391504.1; -.
3D structure databases
HSSP P11759; 1MFZ. [HSSP ENTRY / PDB]
ModBase P96718.
PTM databases
PhosSite P96718; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3621-MON; -.
Organism-specific databases
SubtiList BG12510; ywqF. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0003979; Molecular function: UDP-glucose 6-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0007047; Biological process: cell wall organization (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11374; UDPG_MGDP_DH_Creg; 1.
Pfam PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.
BLOCKS P96718.
ProtoNet P96718.
Genome annotation databases
GeneID 936890; -.
GenomeReviews AL009126_GR; BSU36230.
KEGG bsu:BSU36230; -.
NMPDR fig|224308.1.peg.3630; -.
Phylogenomic databases
HOGENOM P96718; -.
Genome annotation databases
CMR P96718; BSU36230.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   440  440     UDP-glucose 6-dehydrogenase. PRO_0000253341
NP_BIND   2    19  18     NAD (Potential). 
ACT_SITE   260   260        By similarity. 
MUTAGEN   10    10        Y->F: 30-fold decrease in activity but no decrease in the overall phosphorylation level. 
Sequence information
Length: 440 AA [This is the length of the unprocessed precursor] Molecular weight: 47784 Da [This is the MW of the unprocessed precursor] CRC64: 1ADA9454EBE1F645 [This is a checksum on the sequence]
        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 

P96718 in FASTA format

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