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UniProtKB/Swiss-Prot entry P05654


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

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Entry information
Entry name PYRB_BACSU
Primary accession number P05654
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on November 1, 1988 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name Aspartate carbamoyltransferase
Synonyms EC 2.1.3.2
Aspartate transcarbamylase
ATCase
Gene name
Name: pyrB
OrderedLocusNames: BSU15490
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].
PubMed=3015959 [NCBI, ExPASy, EBI, Israel, Japan]
Lerner C.G., Switzer R.L.;
"Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).";
J. Biol. Chem. 261:11156-11165(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1709162 [NCBI, ExPASy, EBI, Israel, Japan]
Quinn C.L., Stephenson B.T., Switzer R.L.;
"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon.";
J. Biol. Chem. 266:9113-9127(1991).
[3]
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600464-MCP200; PubMed=17218307 [NCBI, ExPASy, EBI, Israel, Japan]
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
[5]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=1906175 [NCBI, ExPASy, EBI, Israel, Japan]
Stevens R.C., Reinisch K.M., Lipscomb W.N.;
"Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 88:6087-6091(1991).
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
M13128; AAA22685.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M59757; AAA21267.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99112; CAB13423.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25015; OWBSAC.
RefSeq NP_389432.1; -.
3D structure databases
PDB
2AT2; X-ray; 3.00 A; A/B/C=1-300.[ExPASy / RCSB / EBI]
PDBsum 2AT2; -.
ModBase P05654.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1551-MON; -.
Organism-specific databases
SubtiList BG10713; pyrB. [Micado]
Ontologies
GO
GO:0004070; Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00001; -; 1.
PBIL [Tree]
InterPro IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
Graphical view of domain structure.
Pfam PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00100; AOTCASE.
PR00101; ATCASE.
TIGRFAMs TIGR00670; asp_carb_tr; 1.
PROSITE PS00097; CARBAMOYLTRANSFERASE; 1.
BLOCKS P05654.
Genome annotation databases
GeneID 937734; -.
GenomeReviews AL009126_GR; BSU15490.
KEGG bsu:BSU15490; -.
NMPDR fig|224308.1.peg.1551; -.
Phylogenomic databases
HOGENOM P05654; -.
Other
LinkHub P05654; -.
Genome annotation databases
CMR P05654; BSU15490.
Other
ProtoNet P05654.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Phosphoprotein; Pyrimidine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   304  304     Aspartate carbamoyltransferase. PRO_0000113099
MOD_RES   303   303        Phosphoserine. 
Sequence information
Length: 304 AA [This is the length of the unprocessed precursor] Molecular weight: 34171 Da [This is the MW of the unprocessed precursor] CRC64: 375EA677346E15FE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKHLTTMSEL STEEIKDLLQ TAQELKSGKT DNQLTGKFAA NLFFEPSTRT RFSFEVAEKK 

        70         80         90        100        110        120 
LGMNVLNLDG TSTSVQKGET LYDTIRTLES IGVDVCVIRH SEDEYYEELV SQVNIPILNA 

       130        140        150        160        170        180 
GDGCGQHPTQ SLLDLMTIYE EFNTFKGLTV SIHGDIKHSR VARSNAEVLT RLGARVLFSG 

       190        200        210        220        230        240 
PSEWQDEENT FGTYVSMDEA VESSDVVMLL RIQNERHQSA VSQEGYLNKY GLTVERAERM 

       250        260        270        280        290        300 
KRHAIIMHPA PVNRGVEIDD SLVESEKSRI FKQMKNGVFI RMAVIQCALQ TNVKRGEAAY 


VISH 

P05654 in FASTA format

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