Q5BB37 (CARA_EMENI) 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:	cpa-1
ORF Names:	AN2243

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.
Sequence caution	The sequence EAA63928.1 differs from that shown. Reason: Erroneous gene model prediction.

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 Reference 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 – 454	454	Carbamoyl-phosphate synthase arginine-specific small chain		PRO_0000290595
Regions
	Domain	219 – 406	188	Glutamine amidotransferase type-1
	Compositional bias	443 – 454	12	Poly-Ala
Sites
	Active site	295	1	Nucleophile By similarity
	Active site	379	1	By similarity
	Active site	381	1	By similarity
Experimental info
	Sequence conflict	14	1	A → P in CAA11831. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5BB37 [UniParc]. Last modified November 16, 2011. Version 2. Checksum: 050C58FFCF9F4AD9	FASTA	454	49,638
	10 20 30 40 50 60 MMFSRFFKAV PARAPAFSSP LPVYQARTMA TVRNQRPVER ATFTIRDGPI FHGKSFGART 70 80 90 100 110 120 TISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSTERDRHG LLKYFESPNL 130 140 150 160 170 180 QAAGVVVADV AEQYSHWTAV QSLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG 190 200 210 220 230 240 EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVLDCGVKEN ILRSLVSRGA 250 260 270 280 290 300 SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQDTTYHL RRLMETSQVP IFGICLGHQL 310 320 330 340 350 360 LALAAGARTV KLKYGNRAHN IPALDLTTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND 370 380 390 400 410 420 SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV KKYKNSQLAF HPSRETIPSP 430 440 450 LLVDLLPKER VDVAPTIGMQ NVAAAAAAAA AATA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"A CPA-like gene from Aspergillus nidulans." Doonan J. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-304.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000036 Genomic DNA. Translation: EAA63928.1. Sequence problems. BN001307 Genomic DNA. Translation: CBF86449.1. AJ224085 mRNA. Translation: CAA11831.1.
RefSeq	XP_659847.1. XM_654755.1.
3D structure databases
HSSP	HSSP built from PDB template 1CE8 based on UniProtKB P0A6F1.
ProteinModelPortal	Q5BB37.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5BB37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2875485.
KEGG	ani:AN2243.2.
Phylogenomic databases
OrthoDB	EOG4N8VDH.
PhylomeDB	Q5BB37.
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_EMENI

Accession

Primary (citable) accession number: Q5BB37
Secondary accession number(s): C8VMT6, O42806

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	November 16, 2011
Last modified:	January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program