Reviewed, UniProtKB/Swiss-Prot Q6FQ30 (CARA_CANGA)

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:	CAGL0I09592g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	392 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 – 392	392	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290591
Regions
	Domain	179 – 370	192	Glutamine amidotransferase type-1
Sites
	Active site	258	1	Nucleophile By similarity
	Active site	343	1	By similarity
	Active site	345	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FQ30-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 5CABCF6E245CDF6D	FASTA	392	43,225
	10 20 30 40 50 60 MSQATFEIKN GPSFSGYSFG ADKSISGEAV FTTSLVGYPE SMTDPSYRGQ ILVFTQPLIG 70 80 90 100 110 120 NYGVPSMEAR DEYNLLKHFE SSHIQVAGIV VADYAAQYSH WTAVESLGDW CKREGVAAIT 130 140 150 160 170 180 GVDTREIVQY LREQGSSQSR ILVEGSDTPK FYDSMATHLV AEVSTKETLY VPAKNPVANI 190 200 210 220 230 240 AVIDCGVKVN IIRSLVARGA NVTIFPHNAR IQDVAGQFDG VFLSNGPGNP ETCHETIENL 250 260 270 280 290 300 KELLANEDLQ QLPIFGICLG HQLLALASGG KTHKLQYGNR AHNIPAMDLT TGQCHITSQN 310 320 330 340 350 360 HGYAVDPQTL PQEEWKPYFI NLNDQSNEGM IHTTRPIFST QFHPEAKGGP LDTMPLFDKF 370 380 390 FNNIECYKTH LSQSSYRMVS QIPAIDKKEI MA

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380955 Genomic DNA. Translation: CAG60601.1.
RefSeq	XP_447664.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2888937.
KEGG	cgr:CAGL0I09592g.
Phylogenomic databases
HOGENOM	Q6FQ30.
OMA	Q6FQ30. LFDGSNC.
Enzyme and pathway databases
BRENDA	6.3.5.5. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FQ30

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)