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 A1WBQ7

[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_ACISJ
Primary accession number A1WBQ7
Secondary accession numbers None
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 17)
Name and origin of the protein
Protein name Aspartate carbamoyltransferase
Synonyms EC 2.1.3.2
Aspartate transcarbamylase
ATCase
Gene name
Name: pyrB
OrderedLocusNames: Ajs_3570
From
Acidovorax sp. (strain JS42) [TaxID: 232721] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000539; ABM43682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_987758.1; -.
3D structure databases
ModBase A1WBQ7.
Ontologies
GO
GO:0016597; Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0004070; Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006207; Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006520; Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
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.
ProtoNet A1WBQ7.
Genome annotation databases
GeneID 4672401; -.
GenomeReviews CP000539_GR; Ajs_3570.
KEGG ajs:Ajs_3570; -.
CMR A1WBQ7; Ajs_3570.
Other
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   320  320     Aspartate carbamoyltransferase. PRO_0000321063
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 35007 Da [This is the MW of the unprocessed precursor] CRC64: 9CEDFC008952A94C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLYKRNPQLN KNGELIHLLS IEGLPKDIVT HILDTATNFV SVQEREVKKV PLLRGKSVFN 

        70         80         90        100        110        120 
LFFENSTRTR TTFEIAAKRL SADVFNLDIA RSSTAKGETL LDTIDNLSAM AADIFVVRHS 

       130        140        150        160        170        180 
ESGAPYLIAQ HVAPHVHVVN AGDGRHSHPT QGLLDMYTIR HYKKDFSNLT VAIVGDVLHS 

       190        200        210        220        230        240 
RVARSDIHAL TTLGAAEVRV VGPRTLVPSD MAQMGVRVFH NLEEGIKGCD VVITLRLQNE 

       250        260        270        280        290        300 
RMSGALLPSS QEYFKSFGLT PEKLRLAKPD AIVMHPGPIN RGVEIDSAVV DGPQAVILPQ 

       310        320 
VTFGIAVRMA VMSIVAGNEA
A1WBQ7 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!