Reviewed, UniProtKB/Swiss-Prot Q8Y664 (CARA_LISMO)

Names and origin

Protein names

Recommended name:
    Carbamoyl-phosphate synthase small chain
    EC=6.3.5.5
Alternative name(s):
    Carbamoyl-phosphate synthetase glutamine chain

Gene names

Name:	carA
Synonyms:	pyrAA
Ordered Locus Names:	lmo1836

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP MF_01209
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP MF_01209
Subunit structure	Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity. HAMAP MF_01209
Sequence similarities	Belongs to the carA family. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Pyrimidine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112292
Regions
	Domain	172 – 359	188	Glutamine amidotransferase type-1
	Region	1 – 168	168	CPSase HAMAP MF_01209
Sites
	Active site	247	1	Nucleophile By similarity
	Active site	332	1	By similarity
	Active site	334	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y664-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 0CA6BB590FBFE3FF	FASTA	363	40,055
	10 20 30 40 50 60 MTKRILMLED GNYFIGDAIG SEKETIGEVV FNTGMTGYQE TITDPSYYGQ IITFTYPLVG 70 80 90 100 110 120 NYGVNRDDFE SINPAVKGVV VREAAEFASN WRNQITLNEF LKEKGIPGIA GIDTRKLTKL 130 140 150 160 170 180 IRKEGTLKGI LAAETADKEE LLHHLRSVRL PVDQVHEVSS AKAFASPGDG KRVVLVDYGV 190 200 210 220 230 240 KSSILRELNK RNCYVTVVPY NTSAEEILAM HPDGVMLSNG PGDPKDVPEA LEMIRGIQGK 250 260 270 280 290 300 LPLFGICLGH QLFALANGAD TFKLKFGHRG ANHPVKELAT GRVDFTAQNH GYAVEKDSLI 310 320 330 340 350 360 GTDLKVTHIE LNDETVEGLA HKEYPAYTVQ YHPEANPGPS DVNYLFDEFM EMMNGKEEGE LHA

References

[1]

"Comparative genomics of Listeria species." 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. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591981 Genomic DNA. Translation: CAC99914.1.
PIR	AD1304.
RefSeq	NP_465361.1.
3D structure databases
SMR	Q8Y664. Positions 1-357.
ModBase	Search...
Genome annotation databases
GeneID	985872.
KEGG	lmo:lmo1836.
Organism-specific databases
ListiList	LMO01836.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286341.
OMA	FTYPELG.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1836-MONOMER.
BRENDA	6.3.5.5. 96770.
Family and domain databases
HAMAP	MF_01209_B. CPSase_S_chain_B. [Tree]
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase_dom. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view]
PANTHER	PTHR11405:SF4. CarA_synth_small. 1 hit.
Pfam	PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE.
TIGRFAMs	TIGR01368. CPSaseIIsmall. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARA_LISMO

Accession

Primary (citable) accession number: Q8Y664

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)