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UniProtKB/Swiss-Prot entry Q732I2

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

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Entry information
Entry name CARA_BACC1
Primary accession number Q732I2
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 38)
Name and origin of the protein
Protein name Carbamoyl-phosphate synthase small chain
Synonyms EC 6.3.5.5
Carbamoyl-phosphate synthetase glutamine chain
Gene name
Name: carA
OrderedLocusNames: BCE_3932
From
Bacillus cereus (strain ATCC 10987) [TaxID: 222523] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh258; PubMed=14960714 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.";
Nucleic Acids Res. 32:977-988(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
AE017194; AAS42835.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_980227.1; -.
3D structure databases
HSSP P00907; 1A9X. [HSSP ENTRY / PDB]
ModBase Q732I2.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004088; Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from HAMAP).
GO:0006526; Biological process: arginine biosynthetic process (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_01209; -; 1.
PBIL [Tree]
InterPro IPR006220; Anth_synthII.
IPR001317; CarbamoylP_synth_GATase.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
Graphical view of domain structure.
PANTHER PTHR11405:SF4; CarA_synth_small; 1.
Pfam PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
Pfam graphical view of domain structure.
PRINTS PR00097; ANTSNTHASEII.
PR00099; CPSGATASE.
PR00096; GATASE.
TIGRFAMs TIGR01368; CPSaseIIsmall; 1.
PROSITE PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q732I2.
ProtoNet Q732I2.
Genome annotation databases
GeneID 2751846; -.
GenomeReviews AE017194_GR; BCE_3932.
KEGG bca:BCE_3932; -.
NMPDR fig|222523.1.peg.3899; -.
TIGR BCE_3932; -.
Phylogenomic databases
HOGENOM Q732I2; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   365  365     Carbamoyl-phosphate synthase small chain. PRO_0000112247
DOMAIN   170   357  188     Glutamine amidotransferase type-1. 
REGION   1   166  166     CPSase. 
ACT_SITE   245   245        Nucleophile (By similarity). 
ACT_SITE   330   330        By similarity. 
ACT_SITE   332   332        By similarity. 
Sequence information
Length: 365 AA [This is the length of the unprocessed precursor] Molecular weight: 40377 Da [This is the MW of the unprocessed precursor] CRC64: 0F31591333FA2CBA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN 

        70         80         90        100        110        120 
YGINRDDFES IHPSVNGLIV NEICDHPSNF RNEISLNDYL KERNIPGLAG IDTRKLTRKI 

       130        140        150        160        170        180 
RQYGTLRGRL CNMDADVEYI VSQLKATVFT DHVKRVSTKD PYPSPGRGHR VVLVDFGMKH 

       190        200        210        220        230        240 
GILRELNKRD CDVIVVPYNT TAEEILRLSP DGIMLSNGPG DPKDVPEAIE MLKDIIGKVP 

       250        260        270        280        290        300 
LFGICLGHQL FALASGANTS KLKFGHRGLN HPVKNLATGK VAITSQNHGY AVEEESVENT 

       310        320        330        340        350        360 
ELEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE 


LCQNA
Q732I2 in FASTA format

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