CARA_ASHGO
ID CARA_ASHGO Reviewed; 399 AA.
AC Q752N9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
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; OrderedLocusNames=AFR534W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53905.1; -; Genomic_DNA.
DR RefSeq; NP_986081.1; NM_212217.1.
DR AlphaFoldDB; Q752N9; -.
DR SMR; Q752N9; -.
DR STRING; 33169.AAS53905; -.
DR EnsemblFungi; AAS53905; AAS53905; AGOS_AFR534W.
DR GeneID; 4622360; -.
DR KEGG; ago:AGOS_AFR534W; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_035901_1_1_1; -.
DR InParanoid; Q752N9; -.
DR OMA; CFNTGMT; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:EnsemblFungi.
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..399
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000290585"
FT DOMAIN 187..379
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 352
FT /evidence="ECO:0000250"
FT ACT_SITE 354
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 43842 MW; FEBA86DFDA1B2411 CRC64;
MTSDEAKKAR FCLHGGPSYE GYSFGAPVSV GGEVVFTTSL VGYPDSMTDP SYKGQILVFT
QPLIGNYGVP DGSVRDQYGL LKYMESSKVH VSAIVVAEYA WEYSHWTAVQ SLGDWCRKEG
VAAIGGIDTR AVVQYLRESG STMGRVDVEG AAASARVVDP SKVNLVAQVS TKSPFYIPGK
PSRVNYDVAL VDCGVKENIL RCLVVRGVNV TVFPYDYDVC SIAHHFDGVF ISNGPGDPIH
YRNSTVANLR RLLQDPDLQQ VPIFGICMGH QLLALAAGAS TVKMKYGNRA HNIPALDLST
GQCHITSQNH GYAVDAATLP RDEFVPLFVN LNDKSNEGII HVSRPIYSTQ FHPEGKGGPM
DCSFLFDEYV ERMRCYRKLF RQEPFIRFPV IGLPKARVL
