ID   CARA_VIBVY              Reviewed;         379 AA.
AC   Q7MNU1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=VV0624;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93388.1; -; Genomic_DNA.
DR   RefSeq; WP_011149509.1; NC_005139.1.
DR   AlphaFoldDB; Q7MNU1; -.
DR   SMR; Q7MNU1; -.
DR   STRING; 672.VV93_v1c05670; -.
DR   EnsemblBacteria; BAC93388; BAC93388; BAC93388.
DR   KEGG; vvy:VV0624; -.
DR   PATRIC; fig|196600.6.peg.644; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_1_1_6; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 662268at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002675; 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..379
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000112346"
FT   DOMAIN          193..379
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..189
FT                   /note="CPSase"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ   SEQUENCE   379 AA;  40830 MW;  E7142818A3660ADE CRC64;
     MSKSALLVLE DGTVFRGVSI GADGISVGEV VFNTSMTGYQ EILTDPSYSQ QIVTLTYPHI
     GNTGTTSEDE ESSSIHAQGL VIRDLPLIAS NFRSEQSLSD YLKSQNIVGI ADIDTRKLTR
     ILREKGAQNG CIVAGNNLDE ALALAKAKEF PGLKGMDLAK EVTTKEAYQW KQGSWTLEGG
     LPEAKDDSEL PYHVVAYDFG AKRNILRMLV DRGCRLTVVP AETSAEDVLA LNPDGVFLSN
     GPGDPAPCTY AIEATKVFLE KGLPVFGICL GHQILALASG AKTVKMKFGH HGANHPVKDL
     DRNVVMITSQ NHGFAADEAT LPDNLRATHV SLFDGSLQGI HRTDKPAFSF QGHPEASPGP
     HDAAPLFDHF IELIKQHSA