Q2U913 (CARA_ASPOR) 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:	AO090701000214

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	450 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 – 450	450	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290589
Regions
	Domain	220 – 407	188	Glutamine amidotransferase type-1
	Compositional bias	444 – 450	7	Poly-Ala
Sites
	Active site	296	1	Nucleophile By similarity
	Active site	380	1	By similarity
	Active site	382	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2U913 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 4F52C179BA753038	FASTA	450	49,118
	10 20 30 40 50 60 MFAARLFKAM PARASAFPSV NASIQSRFMA TVRNGRVAHE RATFTIRDGP IFHGKSFGAR 70 80 90 100 110 120 SNISGEAVFT TSLVGYPESL TDPSYRGQIL VFTQPLIGNY GVPSAEKDQH GLLKYFESPH 130 140 150 160 170 180 LQAAGVVVAD VAEQYSHWTA VQSLGEWCAR EGVPAISGVD TRAIVTYLRE QGSSLARITV 190 200 210 220 230 240 GEEYDADQDE AFVDPEQIHL VRQVSTKAPF HVSAADPQCH VAVIDCGVKE NILRSLVSRG 250 260 270 280 290 300 ASITVFPYDY PIHKVAHHFD GVFISNGPGD PTHCQETAYH LRRLMETSQV PIFGICLGHQ 310 320 330 340 350 360 LLALAIGART IKLKYGNRAH NIPALDMSTG RCHITSQNHG YAVDASTLPS DWKPYFVNLN 370 380 390 400 410 420 DSSNEGMIHK TRPIFSTQFH PEAKGGPLDS SYLFDIYLDS VRKYKASQSA FHPTRDSLPS 430 440 450 PLLVDLLAKE RVGVQPTIGM QNVAAAAAAA

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007164 Genomic DNA. Translation: BAE61952.1.
RefSeq	XP_001823085.1. XM_001823033.2.
3D structure databases
ProteinModelPortal	Q2U913.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2U913.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00010567; CADAORAP00010355; CADAORAG00010567.
GeneID	5995142.
GenomeReviews	Gene locus cpa1 in contig AP007164_GR.
KEGG	aor:AOR_1_398114.
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_ASPOR

Accession

Primary (citable) accession number: Q2U913

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program