Reviewed, UniProtKB/Swiss-Prot Q6FZ66 (CARA_BARQU)

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:	BQ09220

Organism

Bartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

803 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	398 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 – 398	398	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_1000138850
Regions
	Domain	209 – 397	189	Glutamine amidotransferase type-1
	Region	1 – 205	205	CPSase HAMAP MF_01209
Sites
	Active site	286	1	Nucleophile By similarity
	Active site	370	1	By similarity
	Active site	372	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FZ66-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: E6B4F5E0218D0C0C	FASTA	398	43,727
	10 20 30 40 50 60 MTQTIPSPNP WSISRPTALL ILADGTVIEG KGAGATGVAE GEICFNTAMT GYEEILTDPS 70 80 90 100 110 120 YKKQIINFTF PHIGNVGTNS EDIEDLTPLN CHGAVGAIFK ADITYPSNYR ANENLNQWLK 130 140 150 160 170 180 TRKIIALCGV DTRALTVLIR EKGSLNGIII HDPNGNFDIH ALKKHAQKWT GLINLDLAKE 190 200 210 220 230 240 VTSKQFVEWN EKPWVWNKGY STNDACNFHI VAIDYGIKRN ILRLMAAHGA RITIVPANTN 250 260 270 280 290 300 VEKILAMNPD GVFLSNGPGD PTATANYAVP TIQALIDSNI PLFGICLGHQ LLALAVGAKT 310 320 330 340 350 360 IKMHQGHHGA NHPVKDFITR KVEIASMNHG FAVETTSLPE HVEETHISLF DNSNCGLRII 370 380 390 GKPVFSVQHH PEASPGPQDS HYLFQRFFNL IMDYKRTA

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX897700 Genomic DNA. Translation: CAF26399.1.
RefSeq	YP_032523.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2867568.
GenomeReviews	Gene locus BQ09220 in contig BX897700_GR.
KEGG	bqu:BQ09220.
NMPDR	fig|283165.1.peg.793.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FZ66.
OMA	LFDGSNC.
Enzyme and pathway databases
BioCyc	BQUI283165:BQ09220-MON.
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_BARQU

Accession

Primary (citable) accession number: Q6FZ66

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 49 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)