Reviewed, UniProtKB/Swiss-Prot Q6G5M0 (CARA_BARHE)

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:	BH11590

Organism

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

Taxonomic identifier

38323 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	399 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 – 399	399	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_1000138849
Regions
	Domain	210 – 398	189	Glutamine amidotransferase type-1
	Region	1 – 206	206	CPSase HAMAP MF_01209
Sites
	Active site	287	1	Nucleophile By similarity
	Active site	371	1	By similarity
	Active site	373	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G5M0-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 2BC4D9DA528B95DB	FASTA	399	43,758
	10 20 30 40 50 60 MTQTIPSPKP WSINKPTALL VLANGTVIEG KGAGATGFAE AEICFNTAMT GYEEILTDPS 70 80 90 100 110 120 YKKQIVNFTF PHIGNVGTNS EDIEDLIPLN CHGAVGAIFK ADITHPSNYR ANENLNQWLK 130 140 150 160 170 180 KRKIIALCGI DTRALTVLIR EKGALNGIIA HDPNGNFDIN TLKKRAQKWT GLVNLDLAQE 190 200 210 220 230 240 VTSKQSMKWN EKPWVWNKGY KTNNDASNFH IVAIDYGIKR NILRLIAAHS AHITIVPANT 250 260 270 280 290 300 NIEEILAMNP DGVFLSNGPG DPAATANYAV PTIQALIDSN IPLFGICLGH QLLALAVGAK 310 320 330 340 350 360 TIKMHQGHHG ANHPVKDFIT GKVEIVSMNH GFTVDTTSLP QHVEETHISL FDNSNCGLRI 370 380 390 IGKPVFSVQH HPEASPGPQD SHYLFQRFFN LIMDYKKTA

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: ATCC 49882 / Houston 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX897699 Genomic DNA. Translation: CAF27942.1.
RefSeq	YP_033925.1.
3D structure databases
HSSP	HSSP built from PDB template 1JDB based on UniProtKB P0A6F1.
ModBase	Search...
Genome annotation databases
GeneID	2865404.
GenomeReviews	Gene locus BH11590 in contig BX897699_GR.
KEGG	bhe:BH11590.
NMPDR	fig|283166.1.peg.1053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286341.
OMA	FTYPELG.
PhylomeDB	Q6G5M0.
Enzyme and pathway databases
BioCyc	BHEN283166:BH11590-MONOMER.
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_BARHE

Accession

Primary (citable) accession number: Q6G5M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 54 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)