ID   A0A424Z0B6_9PROT        Unreviewed;       372 AA.
AC   A0A424Z0B6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   18-SEP-2019, entry version 4.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000256|HAMAP-Rule:MF_01209,
GN   ECO:0000313|EMBL:RQD87479.1};
GN   ORFNames=DZD40_04310 {ECO:0000313|EMBL:RQD87479.1};
OS   Campylobacter hepaticus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1813019 {ECO:0000313|EMBL:RQD87479.1, ECO:0000313|Proteomes:UP000286095};
RN   [1] {ECO:0000313|EMBL:RQD87479.1, ECO:0000313|Proteomes:UP000286095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54L {ECO:0000313|EMBL:RQD87479.1,
RC   ECO:0000313|Proteomes:UP000286095};
RA   Van T.T.H., Moore R.J.;
RT   "Survival mechanisms of Campylobacter hepaticus identified by genomic
RT   analysis and comparative transcriptomic analysis of in vivo and in
RT   vitro derived bacteria.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-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
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01209}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RQD87479.1}.
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DR   EMBL; QURW01000009; RQD87479.1; -; Genomic_DNA.
DR   RefSeq; WP_066779443.1; NZ_QXDV01000008.1.
DR   KEGG; chw:A2J15_003930; -.
DR   KO; K01956; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000286095; Unassembled WGS sequence.
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-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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000286095};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01209, ECO:0000313|EMBL:RQD87479.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}.
FT   DOMAIN      188    372       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   REGION        1    187       CPSase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   ACT_SITE    268    268       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209, ECO:0000256|PROSITE-ProRule:
FT                                PRU00605}.
FT   ACT_SITE    351    351       {ECO:0000256|HAMAP-Rule:MF_01209,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    353    353       {ECO:0000256|HAMAP-Rule:MF_01209,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
SQ   SEQUENCE   372 AA;  42149 MW;  3E8C60BBE206BB0E CRC64;
     MKAYIYLEND IYLSAKAFGK GGTYFGELVF NTSLTGYQEI ISDPSYAGQF IVFSMPELGI
     VGTNENDNES RAIFASGILM RELSSTFSNF RAQESLQEYL EKYGKIGIYE LDTRYLVKMI
     RNNGNLRAVI STEISNKEDL KLALEKSMKI DEINFIKEVS TKKNYSHKQG VWNANLQKFN
     DAKRSAKKVA VIDYGVKINI LNELVEVGFE VEVYPYNTKA DELIALYKKG EIQGVFLSNG
     PGEPKILKQE IAEIKKLAEA KIPMLGICLG HQLLSNAFGY ETYKMKFGQH GANHPVINLD
     TKTVEITTQN HNYNVPEELS QIAIITHRNL FGDNVEGVRY KNYPIISVQH HPESSSGPHE
     SKYIFKEFMN LM
//