ID   CARA_WIGBR              Reviewed;         376 AA.
AC   Q8D3H7;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=WIGBR0240;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24170.1; -; Genomic_DNA.
DR   RefSeq; WP_011069828.1; NC_004344.2.
DR   AlphaFoldDB; Q8D3H7; -.
DR   SMR; Q8D3H7; -.
DR   STRING; 36870.25165979; -.
DR   EnsemblBacteria; BAC24170; BAC24170; BAC24170.
DR   KEGG; wbr:carA; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_2_1_6; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 662268at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000562; 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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000112347"
FT   DOMAIN          187..374
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..183
FT                   /note="CPSase"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ   SEQUENCE   376 AA;  42470 MW;  38048E26FB609538 CRC64;
     MENILLNKAL LILEDGTKFY GNSIGAKGTS IGEVIFNTSI TGYQEIITDP SYFNQIVAFT
     YPHIGNIGIE INNNESSKIQ VKAVILYQTH NIISDFRNKL SFSRFLLLNN IIGISGIDTR
     KLTRLIRKSG TQYGYVSSEG TNINFKEIKS KIKIFLEKKN LDLVKLVTTK RKIIYKKKYI
     EKNFFYNIVA YDFGIKFSII KNLINLGCRI TLVPATTKSK YVISLNPDGI LLSNGPGNPE
     IYKYAIRNIQ CLLETKIPIF GICLGHQLLA IANGAKILKM KFGHHGSNHP VKDLETNKII
     ITSQNHDFAI DKSTLSKNII ITHISMFDQT LQGIKLINKP VFSFQGHPES SPGPKDALFL
     FKNFINLVKD YRLNKK