Q6D0C8 (CARA_ERWCT) 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:	ECA3871

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	382 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.
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: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112277
Regions
	Domain	193 – 380	188	Glutamine amidotransferase type-1
	Region	1 – 189	189	CPSase HAMAP MF_01209
Sites
	Active site	269	1	Nucleophile By similarity
	Active site	353	1	By similarity
	Active site	355	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6D0C8 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 027C127F53A2CED4	FASTA	382	41,488
	10 20 30 40 50 60 MIKSALLVLE DGTQFHGRAI GAEGLAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI 70 80 90 100 110 120 GNVGANANDE ESPSVQAQGL VIRDLPLIAS NYRSEESLSE YLKRNNIVAI ADIDTRKLTR 130 140 150 160 170 180 LLREKGAQNG CIIAGDAPDA VVALEKAKAF PGLKGMDLAK EVTTAESYSW LQGSWTLEGE 190 200 210 220 230 240 LPAAKNESEL PYHVVAYDYG VKRNILRMLV DRGCRLTVVP AQTPAEDVLK LNPDGIFLSN 250 260 270 280 290 300 GPGDPEPCDY AIRAIKTFLE TGIPVFGICL GHQLLALASG AKTTKMKLGH HGGNHPVKDL 310 320 330 340 350 360 DNNCVMITAQ NHGFAVDEDN LPDTLRVTHK SLFDHTVQGI HRTDKPAFSF QGHPEASPGP 370 380 HDAAPLFDHF IDLIQTYRSS AK

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG76769.1.
RefSeq	YP_051959.1. NC_004547.2.
3D structure databases
ProteinModelPortal	Q6D0C8.
SMR	Q6D0C8. Positions 2-381.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2882112.
GenomeReviews	Gene locus ECA3871 in contig BX950851_GR.
KEGG	eca:ECA3871.
NMPDR	fig|218491.3.peg.2515.
PATRIC	20483147. VBIPecAtr54885_3927.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286341.
OMA	FTYPELG.
ProtClustDB	PRK12564.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA3871-MONOMER.
Family and domain databases
HAMAP	MF_01209. CPSase_S_chain. [Tree]
InterPro	IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. [Graphical view]
Gene3D	G3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit.
KO	K01956.
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_ERWCT

Accession

Primary (citable) accession number: Q6D0C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program