CARA_ASPNC
ID CARA_ASPNC Reviewed; 453 AA.
AC A2R9B9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE Short=CPS-A;
DE EC=6.3.5.5;
DE AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain;
GN Name=cpa1; ORFNames=An17g00820;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; AM270385; CAK43010.1; -; Genomic_DNA.
DR RefSeq; XP_001398311.1; XM_001398274.2.
DR AlphaFoldDB; A2R9B9; -.
DR SMR; A2R9B9; -.
DR PaxDb; A2R9B9; -.
DR PRIDE; A2R9B9; -.
DR EnsemblFungi; CAK43010; CAK43010; An17g00820.
DR GeneID; 4989405; -.
DR KEGG; ang:ANI_1_106154; -.
DR VEuPathDB; FungiDB:An17g00820; -.
DR HOGENOM; CLU_035901_1_0_1; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000006706; Chromosome 5L.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..453
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000290588"
FT DOMAIN 219..406
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 49398 MW; F9521D4F0740D548 CRC64;
MFARVFKAMP ARAPAFTSVN ASIQSRFMAT VRQGRPATER ATFTIRDGPI FHGKSFGARS
NISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSAERDQHG LLKYFESPNL
QAAGVVVADV AEQYSHWTAV ESLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG
EEYDADQDEA FVDPEQIHLV RQVSTKAPFH VSAADPQCHV AVIDCGVKEN ILRSLVSRGA
SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQDTVYHL RRLMETSQVP IFGICLGHQL
LALANGARTI KLKYGNRAHN IPALDTTTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND
SSNEGMIHKT RPIFSTQFHP EAKGGPLDSS YLFDIYLDSV VKYKNHQLAF HPNRNTVPSP
LLVDLLAKER VGVQPTIGMQ NVAAAAAAAV AAA
