ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q65JV0


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PYRB_BACLD
Primary accession number Q65JV0
Secondary accession number Q62VA5
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on October 25, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
Name and origin of the protein
Protein name Aspartate carbamoyltransferase
Synonyms EC 2.1.3.2
Aspartate transcarbamylase
ATCase
Gene name
Name: pyrB
OrderedLocusNames: BLi01769, BL02273
From
Bacillus licheniformis (strain DSM 13 / ATCC 14580) [TaxID: 279010] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(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
AE017333; AAU40664.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU23304.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_078942.1; -.
YP_091357.1; -.
3D structure databases
ModBase Q65JV0.
Enzyme and pathway databases
BioCyc BLIC279010:BL02273-MON; -.
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 Q65JV0.
Genome annotation databases
GeneID 3030919; -.
3097708; -.
GenomeReviews CP000002_GR; BL02273.
AE017333_GR; BLi01769.
KEGG bld:BLi01769; -.
bli:BL02273; -.
NMPDR fig|279010.5.peg.1711; -.
Phylogenomic databases
HOGENOM Q65JV0; -.
Genome annotation databases
CMR Q65JV0; BLi01769.
Other
ProtoNet Q65JV0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Pyrimidine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   306  306     Aspartate carbamoyltransferase. PRO_0000113097
Sequence information
Length: 306 AA [This is the length of the unprocessed precursor] Molecular weight: 34264 Da [This is the MW of the unprocessed precursor] CRC64: BB2BC44134F86D26 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKHLTAMNEL SLEDIHELIE EARELKKGKS DSVLSGKFAA NLFFEPSTRT RFSFEVAEKK 

        70         80         90        100        110        120 
LGMNVLNLDG VSTSVQKGES LYDTVKTLES IGADVCVIRH SHDHYYDELI GHVGIPVINA 

       130        140        150        160        170        180 
GDGCGQHPTQ SLLDLMTIHE EWGRFAGLTV SIHGDIKHSR VARSNAEVLT RLGAKVLFSG 

       190        200        210        220        230        240 
PDEWRDEDNP YGTYVSPDEA VAHSDVVMLL RIQHERHEKK AAERDYLETF GLSLKRAELL 

       250        260        270        280        290        300 
KKDAVIMHPA PVNRGVEIDS ALVESGRSRI FKQMENGVYI RMAVLKRALL NGENKKRGDQ 


AYVLFN 

Q65JV0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!