ID   CARA_HELAH              Reviewed;         379 AA.
AC   Q17VI1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=Hac_1638;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAK00345.1; -; Genomic_DNA.
DR   RefSeq; WP_011578428.1; NC_008229.1.
DR   AlphaFoldDB; Q17VI1; -.
DR   SMR; Q17VI1; -.
DR   STRING; 382638.Hac_1638; -.
DR   MEROPS; C26.954; -.
DR   EnsemblBacteria; CAK00345; CAK00345; Hac_1638.
DR   KEGG; hac:Hac_1638; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_2_1_7; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 662268at2; -.
DR   BioCyc; HACI382638:HAC_RS06950-MON; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000775; Chromosome.
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.
FT   CHAIN           1..379
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_1000138861"
FT   DOMAIN          188..378
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..184
FT                   /note="CPSase"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ   SEQUENCE   379 AA;  42246 MW;  C1A7B0D99B1428F5 CRC64;
     MVSLYLENGL FLQVQSFGAS GTQVGELVFN TSMSGYQEVI SDPSYKGQFV IFSMPEIGVV
     GANSKDDESF FSSAGILVRH YNEFFSNSRA DFSLSAYLKE RGVLGICGVD TRSLIKTLRH
     HGCLMMVAST IEHDKNKLEE ILKNAPRISH TPLVASVSTP KIITHQRATF DFKTLDYKPF
     DEKNSHKTIA VLDFGAKGNI LNELQNVGLK ALIYPHHTKA NELIKAYEKK EIHGIFLSNG
     PGDPLSLQQE IGEIKQLIGA KIPMFGICLG HQLLSIAQGY PTYKLKFGHH GSNHPVKNLE
     TNAVEITAQN HNYCVPEAIE KIATITHRNL FDNTIEGVHY KNAPIISVQH HPESSPGPKE
     SHYIFKEFVK LLENFPTRE