Q5AML6 (CARA_CANAL) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	CaO19.4630, CaO19.12100

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	430 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
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 – 430	430	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290590
Regions
	Domain	219 – 407	189	Glutamine amidotransferase type-1
	Compositional bias	10 – 17	8	Poly-Ala
	Compositional bias	18 – 23	6	Poly-Thr
Sites
	Active site	296	1	Nucleophile By similarity
	Active site	380	1	By similarity
	Active site	382	1	By similarity
Natural variations
	Natural variant	14	1	A → T in allele CaO19.12100.
	Natural variant	18	1	T → TATAT in allele CaO19.12100.

Sequences

	Sequence		Length	Mass (Da)
	Q5AML6 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: A4B30B27F157AB5E	FASTA	430	46,898
	10 20 30 40 50 60 MLSATKRYLA TAAAAAATNT TTTSKAFTNT TSQLGRATLT IKDGPVFNGY SFGANRNVSG 70 80 90 100 110 120 EAVFTTSLVG YPESMTDPSY RGQILCFTQP LIGNYGVPSS TAKDQFNLLK YMESPKVQCI 130 140 150 160 170 180 GIVVADAALE YSHWTAVESL QQWCKRSGVA AITGVDTRQL VSYLRDKGSS LGRITIGEEY 190 200 210 220 230 240 DADEDAAFED PGAINLVHKV TTKAPFHIAC PPQYSKGIHI AVLDCGAKEN ILRCLVERGA 250 260 270 280 290 300 SLTVFPYDYP IDKIANKFDG IFISNGPGDP THCSTTVNNL KKIITNHQDL PIFGICLGHQ 310 320 330 340 350 360 LLALASGAKT IKLKYGNRAH NIPAIDLITG NCHITSQNHG YAVDANTLSE NWQPYFTNLN 370 380 390 400 410 420 DLSNEGMIHK YQPIFSTQFH PEAKGGPLDT SFLFDKFFDN INVYKKSNGL NLPPVENSLL 430 VDILPKERVE

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000006 Genomic DNA. Translation: EAL03965.1. AACQ01000005 Genomic DNA. Translation: EAL04120.1.
RefSeq	XP_722702.1. XM_717609.1. XP_722848.1. XM_717755.1.
3D structure databases
HSSP	HSSP built from PDB template 1A9X based on UniProtKB P0A6F1.
ProteinModelPortal	Q5AML6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5AML6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3635569. 3635715.
KEGG	cal:CaO19.12100. cal:CaO19.4630.
Organism-specific databases
CGD	CAL0003663. CPA1.
Phylogenomic databases
PhylomeDB	Q5AML6.
Family and domain databases
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_CANAL

Accession

Primary (citable) accession number: Q5AML6
Secondary accession number(s): Q5AN21

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program