ID   CARA_BRUA2              Reviewed;         407 AA.
AC   Q2YM22;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; OrderedLocusNames=BAB1_1502;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
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:0000255|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
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DR   EMBL; AM040264; CAJ11458.1; -; Genomic_DNA.
DR   RefSeq; WP_002964590.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YM22; -.
DR   SMR; Q2YM22; -.
DR   STRING; 359391.BAB1_1502; -.
DR   MEROPS; C26.954; -.
DR   EnsemblBacteria; CAJ11458; CAJ11458; BAB1_1502.
DR   GeneID; 45124818; -.
DR   KEGG; bmf:BAB1_1502; -.
DR   PATRIC; fig|359391.11.peg.951; -.
DR   HOGENOM; CLU_035901_2_2_5; -.
DR   OMA; CFNTGMT; -.
DR   PhylomeDB; Q2YM22; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002719; Chromosome I.
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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..407
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_1000138853"
FT   DOMAIN          209..397
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..205
FT                   /note="CPSase"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ   SEQUENCE   407 AA;  43536 MW;  D6C01AFF0592F7E2 CRC64;
     MTETTPKTAP WTVQKRTAVL VLADGTVIEG KGLGATGAVE AEVVFNTALT GYEEILTDPS
     YAGQIVTFTF PHIGNVGANA EDIEDLTPAN RHGAVGAIFK ADITAPSNFR AAKDLDSWLK
     HRGIIALAGI DTRALTALIR ERGAQNAVIA HDPNGNFDLD ALKARAANWC GLENLDLAKD
     VTIGQSLVWK ELPWTLQDGY GEQDAPQYHV VALDFGVKRN ILRLLTGLGA KVTVLPATAT
     AEDVLAHNPD GVFLSNGPGD PAATGEYAVP TIGKLVETGI PLFGICLGHQ MLALALGGRT
     EKMHQGHHGA NHPVKDYTTG KVEIVSMNHG FAVDSDSLPE NVEETHVSLF DGTNCGLRVV
     GKPVFSVQHH PEASPGPQDS HYLFRRFINL IRERKGQAPL PEREQAA