ID   CARX_GEOSE              Reviewed;         354 AA.
AC   P54324;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=carA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC   / NCTC 10339 / R-35646 / VKM B-510;
RX   PubMed=9370352; DOI=10.1111/j.1432-1033.1997.00443.x;
RA   Yang H., Park S.M., Nolan W.G., Lu C.-D., Abdelal A.T.;
RT   "Cloning and characterization of the arginine-specific carbamoyl-phosphate
RT   synthetase from Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 249:443-449(1997).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable up to 63 degrees Celsius.;
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   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR   EMBL; U43091; AAC78717.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54324; -.
DR   SMR; P54324; -.
DR   MEROPS; C26.963; -.
DR   SABIO-RK; P54324; -.
DR   UniPathway; UPA00068; UER00171.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding.
FT   CHAIN           1..354
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000112254"
FT   DOMAIN          165..352
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          1..161
FT                   /note="CPSase"
FT   ACT_SITE        240
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39171 MW;  C00240AAB0D29E8F CRC64;
     MKAYLHVASG KTFSGELAAP LEEKVSGEIV FFTGMTGYQE VLTDPSYKNQ IIVFTYPLIG
     NYGINENDFE SKRPHVEAVV VYEASREGFH YGAKYSLAEY LQHWNIPLLT HVDTRALVKE
     IRTAGTMMAE LSLSPISAVG GVEAVFPVRA VSTRTIETYG EGGPHLVLVD FGYKKSILQS
     LLARGCRVTV VPHDTAPEAI DALKPDGLVL SNGPGDPKQL RHQLPAIRQL IDRYPTLAIC
     LGHQLVALAT GRIRKKLRFG HRGANQPVWD AVKQNVMMTS QNHSYVVKEG SLVGKPFDIR
     FINVNDGSVE GIVHRHKPIL SVQYHPEAHP GPHDTGYIFD EFLQTVFKGE NVYA