A1CA18 (CARA_ASPCL) 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:	ACLA_010090

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	455 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 – 455	455	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290586
Regions
	Domain	219 – 406	188	Glutamine amidotransferase type-1
	Compositional bias	444 – 455	12	Poly-Ala
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)
	A1CA18 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 58E167B7FA07E1B4	FASTA	455	49,703
	10 20 30 40 50 60 MFARFCKAIP AKGRAFPSVN ASIQSRLMAT VRNQRVPHER ATFTIRDGPI FHGKSFGART 70 80 90 100 110 120 NISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSAERDQHG LLKYFESPHL 130 140 150 160 170 180 QAAGVVVADV AEQYSHWTAV ESLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG 190 200 210 220 230 240 EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVIDCGVKEN ILRSLVSRGA 250 260 270 280 290 300 SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQDTTYHL RRLMETSQVP IFGICLGHQL 310 320 330 340 350 360 LALAAGARTI KLKYGNRAHN IPALDMSTGR CHITSQNHGY AVDVDTLPSD WKPYFVNLND 370 380 390 400 410 420 SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV RKYKANQAAF HPQRDSIPSP 430 440 450 LLVDLLAKER VGVQPTIGMQ NVQAAAAAAA VAAAA

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027049 Genomic DNA. Translation: EAW12586.1.
RefSeq	XP_001274012.1. XM_001274011.1.
3D structure databases
ProteinModelPortal	A1CA18.
ModBase	Search...
Protein-protein interaction databases
STRING	A1CA18.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00000920; CADACLAP00000901; CADACLAG00000920.
GeneID	4706589.
KEGG	act:ACLA_010090.
Phylogenomic databases
GeneTree	EFGT00050000001199.
OrthoDB	EOG4N8VDH.
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_ASPCL

Accession

Primary (citable) accession number: A1CA18

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program