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UniProtKB/Swiss-Prot entry Q92AH2


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

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Entry information
Entry name CARA_LISIN
Primary accession number Q92AH2
Secondary accession numbers None
Integrated into Swiss-Prot on July 11, 2002
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
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
Synonyms: pyrAA
OrderedLocusNames: lin1950
From
Listeria innocua [TaxID: 1642] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIP 11262 / Serovar 6a;
DOI=10.1126/science.1063447; PubMed=11679669 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
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
AL596170; CAC97180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR AD1676; AD1676.
RefSeq NP_471284.1; -.
3D structure databases
HSSP P00907; 1A9X. [HSSP ENTRY / PDB]
ModBase Q92AH2.
Enzyme and pathway databases
BioCyc LINN272626:LIN1950-MON; -.
Organism-specific databases
ListiList LIN01950; -.
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:0006541; Biological process: glutamine 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_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).
ProtoNet Q92AH2.
Genome annotation databases
GeneID 1130646; -.
GenomeReviews AL592022_GR; lin1950.
KEGG lin:lin1950; -.
NMPDR fig|272626.1.peg.1937; -.
Phylogenomic databases
HOGENOM Q92AH2; -.
Genome annotation databases
CMR Q92AH2; lin1950.
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   363  363     Carbamoyl-phosphate synthase small chain. PRO_0000112290
DOMAIN   172   359  188     Glutamine amidotransferase type-1. 
REGION   1   168  168     CPSase. 
ACT_SITE   247   247        Nucleophile (By similarity). 
ACT_SITE   332   332        By similarity. 
ACT_SITE   334   334        By similarity. 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 40157 Da [This is the MW of the unprocessed precursor] CRC64: FA5D80B199FBBE8E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTKRILMLED GNYFIGDAIG SEKETIGEVV FNTGMTGYQE TITDPSYYGQ IITFTYPLVG 

        70         80         90        100        110        120 
NYGVNRDDFE SINPAVKGVV VREAAEYPSN WRNQITLNEF LKEKGIPGIA GIDTRKLTKL 

       130        140        150        160        170        180 
IRKEGTLKGI LSAATADKEE LLHHLRSVRL PVDQVHEVSS AKAFASPGDG KRVVLVDYGV 

       190        200        210        220        230        240 
KSSILRELNK RNCYVTVVPY NTTAEEILAM HPDGVMLSNG PGDPKDVPEA LEMIRGIQGK 

       250        260        270        280        290        300 
LPLFGICLGH QLFALANGAD TFKLKFGHRG ANHPVKELAT GRVDFTAQNH GYAVEKESLI 

       310        320        330        340        350        360 
GTDLKVTHIE LNDETVEGLA HKEYQAYTVQ YHPEANPGPS DVNYLFDEFM EMMNVKEEGE 


LHA 

Q92AH2 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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