Reviewed, UniProtKB/Swiss-Prot O25835 (CARA_HELPY)

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:	HP_1237

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	375 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 HCO(3)(-): step 1/1. HAMAP MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. 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 – 375	375	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112282
Regions
	Domain	188 – 375	188	Glutamine amidotransferase type-1
	Region	1 – 184	184	CPSase HAMAP MF_01209
Sites
	Active site	268	1	Nucleophile By similarity
	Active site	351	1	By similarity
	Active site	353	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O25835-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D7146CA079AB7C1F	FASTA	375	41,636
	10 20 30 40 50 60 MVSLYLENGL FLQAQSFGAS GTQAGELVFN TSMSGYQEVI SDPSYKGQFV VFSMPEIGVV 70 80 90 100 110 120 GANSKDDESF FSCAGVLARH YNEFFSNSRA DFSLSAYLKE RGVLGVCGVD TRSLIKTLRH 130 140 150 160 170 180 HGCLMMVAST IEHDKNKLEE ILKNAPKISH SPLVSSVSTP KITTHQRATF DFKTLDYKPF 190 200 210 220 230 240 DEKTSHKIIA VLDFGAKGNI LNELQNVGLK ALIYPHHTKA SELIKAYEKK EISGIFLSNG 250 260 270 280 290 300 PGDPLSLQQE IGEIKQLINA KIPMLGICLG HQLLSIAQGY PTYKLKFGHH GSNHPVKNLK 310 320 330 340 350 360 TNAVEITAQN HNYCVPEDIE EIAIITHRNL FDNTIEGVRY KNAPIISVQH HPESSPGPKE 370 SHYIFKEFVE LLKDF

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000511 Genomic DNA. Translation: AAD08282.1.
PIR	E64674.
RefSeq	NP_208029.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6V based on UniProtKB P00907.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3716N.
Genome annotation databases
GeneID	899987.
GenomeReviews	Gene locus HP_1237 in contig AE000511_GR.
KEGG	hpy:HP1237.
NMPDR	fig|85962.1.peg.1225.
TIGR	HP_1237.
Phylogenomic databases
HOGENOM	O25835.
OMA	O25835. FFTGMTG.
Enzyme and pathway databases
BRENDA	6.3.5.5. 1131.
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_HELPY

Accession

Primary (citable) accession number: O25835

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 65 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)