Reviewed, UniProtKB/Swiss-Prot Q752N9 (CARA_ASHGO)

Names and origin

Protein names

Recommended name:
    Carbamoyl-phosphate synthase arginine-specific small chain
      Short name=CPS-A
    EC=6.3.5.5
Alternative name(s):
    Arginine-specific carbamoyl-phosphate synthetase, glutamine chain

Gene names

Name:	CPA1
Ordered Locus Names:	AFR534W

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Protein attributes

Sequence length	399 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.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from HCO(3)(-): step 1/1.
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.
Subcellular location	Cytoplasm 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
Cellular component	Cytoplasm
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 399	399	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290585
Regions
	Domain	187 – 379	193	Glutamine amidotransferase type-1
Sites
	Active site	267	1	Nucleophile By similarity
	Active site	352	1	By similarity
	Active site	354	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q752N9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FEBA86DFDA1B2411	FASTA	399	43,842
	10 20 30 40 50 60 MTSDEAKKAR FCLHGGPSYE GYSFGAPVSV GGEVVFTTSL VGYPDSMTDP SYKGQILVFT 70 80 90 100 110 120 QPLIGNYGVP DGSVRDQYGL LKYMESSKVH VSAIVVAEYA WEYSHWTAVQ SLGDWCRKEG 130 140 150 160 170 180 VAAIGGIDTR AVVQYLRESG STMGRVDVEG AAASARVVDP SKVNLVAQVS TKSPFYIPGK 190 200 210 220 230 240 PSRVNYDVAL VDCGVKENIL RCLVVRGVNV TVFPYDYDVC SIAHHFDGVF ISNGPGDPIH 250 260 270 280 290 300 YRNSTVANLR RLLQDPDLQQ VPIFGICMGH QLLALAAGAS TVKMKYGNRA HNIPALDLST 310 320 330 340 350 360 GQCHITSQNH GYAVDAATLP RDEFVPLFVN LNDKSNEGII HVSRPIYSTQ FHPEGKGGPM 370 380 390 DCSFLFDEYV ERMRCYRKLF RQEPFIRFPV IGLPKARVL

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016819 Genomic DNA. Translation: AAS53905.1.
RefSeq	NP_986081.1.
3D structure databases
HSSP	HSSP built from PDB template 1A9X based on UniProtKB P00907.
ModBase	Search...
Genome annotation databases
GeneID	4622360.
KEGG	ago:AGOS_AFR534W.
NMPDR	fig|33169.1.peg.3726.
Organism-specific databases
AGD	AFR534W.
Phylogenomic databases
HOGENOM	Q752N9.
OMA	Q752N9. EADIPFF.
Enzyme and pathway databases
BRENDA	6.3.5.5. 279361.
Family and domain databases
InterPro	IPR001317. CarbamoylP_synth_GATase. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view]
Pfam	PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
PRINTS	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_ASHGO

Accession

Primary (citable) accession number: Q752N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)