Reviewed, UniProtKB/Swiss-Prot Q6BJG4 (CARA_DEBHA)

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:	DEHA2G02618g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	429 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.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: 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 – 429	429	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290594
Regions
	Domain	218 – 406	189	Glutamine amidotransferase type-1
Sites
	Active site	295	1	Nucleophile By similarity
	Active site	379	1	By similarity
	Active site	381	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BJG4-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 5B8B9DDEE57A3C18	FASTA	429	47,132
	10 20 30 40 50 60 MIRVIQPPLI ASKQLFRRYL ATGGTFTNKT SQLDRATLTI KDGPVFSGYS FGANKNISGE 70 80 90 100 110 120 AVFTTSLVGY PESMTDPSYK GQILCFTQPL IGNYGVPSST LKDEFNLLKH MESPSVQCIG 130 140 150 160 170 180 IVVADVALEY SHWTAVESLQ QWCQRSGVAA ISGVDTRQLV SYLREKGSSL AKITIGEEYD 190 200 210 220 230 240 ADEDAAFEDP GSVNLVHKVS TKAPFHISCP EKYAKGLHIA VLDCGAKENI LRCLVERGAS 250 260 270 280 290 300 LTVFPYNYPI DKIANKFDGI FISNGPGDPT HCSSTTENLA KTMEKYHDLP IFGICLGHQL 310 320 330 340 350 360 LALASGARTI KMKYGNRAHN IPALDLTTGK CHITSQNHGY SVDAETLDSD WEPYFTNLND 370 380 390 400 410 420 LSNEGMKHKS RPIFSTQFHP EAKGGPLDTA FLFDKFFENI EQYRATNGLN LGNVDDSLLV DILPKGRVL

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 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382139 Genomic DNA. Translation: CAG90105.1.
RefSeq	XP_461657.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6V based on UniProtKB P0A6F1.
SMR	Q6BJG4. Positions 34-406.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BJG4.
Genome annotation databases
GeneID	2904523.
GenomeReviews	Gene locus DEHA2G02618g in contig CR382139_GR.
KEGG	dha:DEHA0G03102g.
Phylogenomic databases
eggNOG	fuNOG04647.
HOGENOM	HBG286341.
OMA	FTYPELG.
OrthoDB	EOG9X9907.
PhylomeDB	Q6BJG4.
Enzyme and pathway databases
BRENDA	6.3.5.5. 74267.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase_dom. 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_DEBHA

Accession

Primary (citable) accession number: Q6BJG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	August 16, 2004
Last modified:	February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)