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UniProtKB/Swiss-Prot entry O32271


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

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Entry information
Entry name TUAD_BACSU
Primary accession number O32271
Secondary accession numbers None
Integrated into Swiss-Prot on April 26, 2004
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 52)
Name and origin of the protein
Protein name UDP-glucose 6-dehydrogenase
Synonyms UDP-Glc dehydrogenase
UDP-GlcDH
UDPGDH
EC 1.1.1.22
Teichuronic acid biosynthesis protein tuaD
Gene name
Name: tuaD
Synonyms: yvhD
OrderedLocusNames: BSU35580
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=10048024 [NCBI, ExPASy, EBI, Israel, Japan]
Soldo B., Lazarevic V., Pagni M., Karamata D.;
"Teichuronic acid operon of Bacillus subtilis 168.";
Mol. Microbiol. 31:795-805(1999).
[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]
CHARACTERIZATION.
STRAIN=168;
PubMed=10376820 [NCBI, ExPASy, EBI, Israel, Japan]
Pagni M., Lazarevic V., Soldo B., Karamata D.;
"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.";
Microbiology 145:1049-1053(1999).
[4]
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).
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
AF015609; AAB94865.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99122; CAB15575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F69727; F69727.
RefSeq NP_391438.1; -.
3D structure databases
HSSP P11759; 1MFZ. [HSSP ENTRY / PDB]
ModBase O32271.
PTM databases
PhosSite O32271; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3555-MON; -.
Organism-specific databases
SubtiList BG12691; tuaD. [Micado]
Ontologies
GO
GO:0003979; Molecular function: UDP-glucose 6-dehydrogenase activity (inferred from electronic annotation from EC).
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.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 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 O32271.
Genome annotation databases
GeneID 936766; -.
GenomeReviews AL009126_GR; BSU35580.
KEGG bsu:BSU35580; -.
NMPDR fig|224308.1.peg.3564; -.
Phylogenomic databases
HOGENOM O32271; -.
Genome annotation databases
CMR O32271; BSU35580.
Other
ProtoNet O32271.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   461  461     UDP-glucose 6-dehydrogenase. PRO_0000074075
NP_BIND   3    20  18     NAD (Potential). 
ACT_SITE   261   261        By similarity. 
Sequence information
Length: 461 AA [This is the length of the unprocessed precursor] Molecular weight: 49816 Da [This is the MW of the unprocessed precursor] CRC64: F3B4D189FEC90095 [This is a checksum on the sequence]
        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 

O32271 in FASTA format

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