Reviewed, UniProtKB/Swiss-Prot Q8FLB1 (CARA_ECOL6)

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:	c0040

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	382 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 – 382	382	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112276
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)
	Q8FLB1-1 [UniParc]. Last modified June 6, 2003. Version 2. Checksum: 308D2BA2EE1478AD	FASTA	382	41,415
	10 20 30 40 50 60 MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI 70 80 90 100 110 120 GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS YLKRHNIVAI ADIDTRKLTR 130 140 150 160 170 180 LLREKGAQNG CIIAGDNPDA ALALEKARAF PGLNGMDLAK EVTTAEPYSW TQGSWTLTGG 190 200 210 220 230 240 LPEAKKEDEL PYHVVAYDFG AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN 250 260 270 280 290 300 GPGDPAPCDY AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV 310 320 330 340 350 360 EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF QGHPEASPGP 370 380 HDAAPLFDHF IALIEQYRKT AK

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN78538.1. Different initiation.
RefSeq	NP_751994.1.
3D structure databases
HSSP	HSSP built from PDB template 1JDB based on UniProtKB P00907.
ModBase	Search...
Genome annotation databases
GeneID	1038618.
GenomeReviews	Gene locus c0040 in contig AE014075_GR.
KEGG	ecc:c0040.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8FLB1.
OMA	LFDGSNC.
Enzyme and pathway databases
BRENDA	6.3.5.5. 292881.
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_ECOL6

Accession

Primary (citable) accession number: Q8FLB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2003
Last sequence update:	June 6, 2003
Last modified:	November 3, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)