ID   A0A424Z0B6_9PROT        Unreviewed;       372 AA.
AC   A0A424Z0B6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   14-DEC-2022, entry version 18.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|ARBA:ARBA00019036, 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|ARBA:ARBA00030197, 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}, GC018_05190
GN   {ECO:0000313|EMBL:MPV98565.1}, GC019_05360
GN   {ECO:0000313|EMBL:MPV95799.1}, GC023_04825
GN   {ECO:0000313|EMBL:MPV77436.1}, GC026_05020
GN   {ECO:0000313|EMBL:MPV94359.1}, GC027_04970
GN   {ECO:0000313|EMBL:MPV80348.1}, GC028_04890
GN   {ECO:0000313|EMBL:MPW01763.1}, I5Q61_03970
GN   {ECO:0000313|EMBL:QPM43334.1};
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 vitro
RT   derived bacteria.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000429436, ECO:0000313|Proteomes:UP000430858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QLD_3/QLD {ECO:0000313|EMBL:MPV77436.1,
RC   ECO:0000313|Proteomes:UP000451781}, QLD_6/QLD
RC   {ECO:0000313|EMBL:MPV94359.1, ECO:0000313|Proteomes:UP000488150},
RC   VIC_4/VIC {ECO:0000313|EMBL:MPV98565.1,
RC   ECO:0000313|Proteomes:UP000430858}, VIC_5/VIC
RC   {ECO:0000313|EMBL:MPV95799.1, ECO:0000313|Proteomes:UP000429436},
RC   WA_1/WA {ECO:0000313|EMBL:MPV80348.1,
RC   ECO:0000313|Proteomes:UP000462254}, and WA_2/WA
RC   {ECO:0000313|EMBL:MPW01763.1, ECO:0000313|Proteomes:UP000480103};
RA   Van T.H., Moore R.J., Phung C.;
RT   "Campylobacter hepaticus, the cause of Spotty Liver Disease in chickens:
RT   Transmission and routes of infection.";
RL   Front. Microbiol. 0:0-0(2019).
RN   [3] {ECO:0000313|EMBL:QPM43334.1, ECO:0000313|Proteomes:UP000594429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UF2019SK1 {ECO:0000313|EMBL:QPM43334.1,
RC   ECO:0000313|Proteomes:UP000594429};
RA   Kariyawasam S., Arukha A., Denagamage T., Butcher G.;
RT   "Characterization and complete genome sequencing of a Campylobacter
RT   hepaticus strain isolated from a commercial layer flock in the United
RT   States.";
RL   Submitted (NOV-2020) 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; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; WHMK01000010; MPV77436.1; -; Genomic_DNA.
DR   EMBL; WHMO01000009; MPV80348.1; -; Genomic_DNA.
DR   EMBL; WHMN01000010; MPV94359.1; -; Genomic_DNA.
DR   EMBL; WHMG01000010; MPV95799.1; -; Genomic_DNA.
DR   EMBL; WHMF01000009; MPV98565.1; -; Genomic_DNA.
DR   EMBL; WHMP01000008; MPW01763.1; -; Genomic_DNA.
DR   EMBL; CP065357; QPM43334.1; -; Genomic_DNA.
DR   EMBL; QURW01000009; RQD87479.1; -; Genomic_DNA.
DR   RefSeq; WP_066779443.1; NZ_WHMR01000009.1.
DR   AlphaFoldDB; A0A424Z0B6; -.
DR   STRING; 1813019.A2J15_05285; -.
DR   GeneID; 44004662; -.
DR   KEGG; chw:A2J15_003930; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000286095; Unassembled WGS sequence.
DR   Proteomes; UP000429436; Unassembled WGS sequence.
DR   Proteomes; UP000430858; Unassembled WGS sequence.
DR   Proteomes; UP000451781; Unassembled WGS sequence.
DR   Proteomes; UP000462254; Unassembled WGS sequence.
DR   Proteomes; UP000480103; Unassembled WGS sequence.
DR   Proteomes; UP000488150; Unassembled WGS sequence.
DR   Proteomes; UP000594429; 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; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_01209};
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          1..131
FT                   /note="CPSase_sm_chain"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..187
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
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
//