Reviewed, UniProtKB/Swiss-Prot Q9HP42 (CARA_HALSA)

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
Ordered Locus Names:	VNG_1815G

Organism

Halobacterium salinarium (Halobacterium halobium) [Complete proteome] [HAMAP]

Taxonomic identifier

2242 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 – 353	353	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112356
Regions
	Domain	166 – 349	184	Glutamine amidotransferase type-1
	Region	1 – 166	166	CPSase HAMAP MF_01209
Sites
	Active site	241	1	Nucleophile By similarity
	Active site	322	1	By similarity
	Active site	324	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HP42-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: FA6E9E9834D964AF	FASTA	353	37,197
	10 20 30 40 50 60 MSDAYLALET GDVVEATARA PGMARGELVF TTAYTGYEES LTDPSYEAQV LTFAYPLIGN 70 80 90 100 110 120 YGVRPERTES DRVHPSAVVA RELTDDVADW LRTEGVPAVD GIDTRDLVLD IRDGGAMQVG 130 140 150 160 170 180 IAAGPDASPA TARAQLADCP RLSARTEIGA HVSVDTAETH GNGDTTVALV DCGAKRSIID 190 200 210 220 230 240 AFVARGATVH RLPYDATPAD IAAVDPDLLF ISNGPGDPAN FDAAEHLVDE YIGTVPIAGI 250 260 270 280 290 300 CLGQQIVARA LGGDTEKMDF GHRGVNQPVL DHDSGRVVMT TQNHGYTVAD PGDLTVTQVN 310 320 330 340 350 VNDGTPEALD SAPLDVLTRQ YHPEANPGPH DTRGFFDDVL AMADASYTPA TAD

References

[1]

"Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S. Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed: 11016950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE004437 Genomic DNA. Translation: AAG20028.1.
PIR	H84332.
RefSeq	NP_280548.1.
3D structure databases
HSSP	HSSP built from PDB template 1JDB based on UniProtKB P00907.
ModBase	Search...
Genome annotation databases
GeneID	1448329.
GenomeReviews	Gene locus VNG_1815G in contig AE004437_GR.
KEGG	hal:VNG1815G.
NMPDR	fig|64091.1.peg.1570.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9HP42.
OMA	FFTGMTG.
Enzyme and pathway databases
BioCyc	HSP64091:VNG1815G-MON.
BRENDA	6.3.5.5. 141893.
Family and domain databases
HAMAP	MF_01209. [Tree]
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. 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_HALSA

Accession

Primary (citable) accession number: Q9HP42

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 63 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)