P57245 (CARA_BUCAI) Reviewed, UniProtKB/Swiss-Prot

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:	BU145

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

Protein attributes

Sequence length	387 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-Rule MF_01209
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP-Rule MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule 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 Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP carbamoyl phosphate biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine catabolic process Inferred from electronic annotation. Source: InterPro
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 – 387	387	Carbamoyl-phosphate synthase small chain HAMAP-Rule MF_01209		PRO_0000112261
Regions
	Domain	197 – 384	188	Glutamine amidotransferase type-1
	Region	1 – 193	193	CPSase HAMAP-Rule MF_01209
Sites
	Active site	273	1	Nucleophile By similarity
	Active site	357	1	By similarity
	Active site	359	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57245 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 2D5F9E8C8EAE1941	FASTA	387	43,020
	10 20 30 40 50 60 MEGVLSQLAV LVLEDGTKFH GRAIGAKGIT VGEVVFNTSI TGYQEIITDP SYSHQIVTLT 70 80 90 100 110 120 HPHIGNVGTN SNDEESSKIY IKGLIIRDLS LTASNYRNKK SFSSYLKENN IIAISDIDTR 130 140 150 160 170 180 KLTRILRTKG SQNGCIIEDK KQNYSIAYNK AKNFISLQDL DLAKKVSTKS IYNWDQGSFT 190 200 210 220 230 240 FKKNNFFSIN KQKFLFHVVV YDFGVKRNIL RMLVDRGCYL TVVPAITDPK TVLNLSPDGI 250 260 270 280 290 300 FLSNGPGDPR PCDYAIHAIQ YFLKTNIPIF GICLGHQLLA LASGAKIVKM KFGHHGGNHP 310 320 330 340 350 360 VKDIKNNRVI ITSQNHSFTV DTENLPNNIE ITHSSLFDGT LQGLSLTNKS AFSFQGHPEA 370 380 SPGPHDASYL FDYFIKLIVS QKTTLSN

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12863.1.
RefSeq	NP_239977.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57245.
SMR	P57245. Positions 9-384.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB12863; BAB12863; BAB12863.
GeneID	1109589.
KEGG	buc:BU145.
PATRIC	21243804. VBIBucAph127364_0154.
Phylogenomic databases
eggNOG	COG0505.
HOGENOM	HOG000038087.
KO	K01956.
OMA	RDSHYLF.
ProtClustDB	PRK12564.
Enzyme and pathway databases
UniPathway	UPA00068; UER00171. UPA00070; UER00115.
Family and domain databases
Gene3D	3.50.30.20. 1 hit.
HAMAP	MF_01209. CPSase_S_chain.
InterPro	IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. [Graphical view]
Pfam	PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
SMART	SM01097. CPSase_sm_chain. 1 hit. [Graphical view]
SUPFAM	SSF52021. CP_synthsmall. 1 hit.
TIGRFAMs	TIGR01368. CPSaseIIsmall. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARA_BUCAI

Accession

Primary (citable) accession number: P57245

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program