Reviewed, UniProtKB/Swiss-Prot Q4WU09 (CARA_ASPFU)

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:	AFUA_5G06780

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	453 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 – 453	453	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290587
Regions
	Domain	219 – 406	188	Glutamine amidotransferase type-1
	Compositional bias	443 – 453	11	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)
	Q4WU09-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 714FE9F43B65E5F7	FASTA	453	49,337
	10 20 30 40 50 60 MFARVFKAMP ARASALTSVN ASIPARFMAT VRQQRPAHER ATFTIRDGPI FHGKSFGART 70 80 90 100 110 120 NISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSAERDEHG LLKYFESPNL 130 140 150 160 170 180 QAAGVVVADV AEQYSHWTAV ESLGEWCARE GVPAISGVDT RAIVTYLRER GSSLARITVG 190 200 210 220 230 240 EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVIDCGVKEN ILRSLVSRGA 250 260 270 280 290 300 GITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQETTYHL RRLMETSQVP IFGICLGHQL 310 320 330 340 350 360 LALAAGARTI KLKYGNRAHN IPALDLSTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND 370 380 390 400 410 420 SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV KKYKASQAAF YPQRDSLPSP 430 440 450 LLVDLLAKER VGVQPTIGMQ NIAAAATAAA AAA

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000003 Genomic DNA. Translation: EAL91917.1.
RefSeq	XP_753955.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3510728.
KEGG	afm:AFUA_5G06780.
Phylogenomic databases
HOGENOM	Q4WU09.
OMA	Q4WU09. EGVPAIS.
Enzyme and pathway databases
BRENDA	6.3.5.5. 18841.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. 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_ASPFU

Accession

Primary (citable) accession number: Q4WU09

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)