ID A0A424Z0B6_9BACT Unreviewed; 372 AA. AC A0A424Z0B6; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-MAY-2024, entry version 25. 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=A2J15_003930 {ECO:0000313|EMBL:AXP08856.1}, DZD40_04310 GN {ECO:0000313|EMBL:RQD87479.1}, GC018_05190 GN {ECO:0000313|EMBL:MPV98565.1}, GC019_05360 GN {ECO:0000313|EMBL:MPV95799.1}; OS Campylobacter hepaticus. OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1813019 {ECO:0000313|EMBL:RQD87479.1, ECO:0000313|Proteomes:UP000286095}; RN [1] {ECO:0000313|Proteomes:UP000093205, ECO:0000313|Proteomes:UP000286095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=54L {ECO:0000313|EMBL:RQD87479.1, RC ECO:0000313|Proteomes:UP000286095}, and HV10 RC {ECO:0000313|EMBL:AXP08856.1, ECO:0000313|Proteomes:UP000093205}; 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=VIC_4/VIC {ECO:0000313|EMBL:MPV98565.1, RC ECO:0000313|Proteomes:UP000430858}, and VIC_5/VIC RC {ECO:0000313|EMBL:MPV95799.1, ECO:0000313|Proteomes:UP000429436}; 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). CC -!- FUNCTION: Small subunit of the glutamine-dependent carbamoyl phosphate CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl CC phosphate from the ammonia moiety of glutamine, carbonate, and CC phosphate donated by ATP, constituting the first step of 2 biosynthetic CC pathways, one leading to arginine and/or urea and the other to CC pyrimidine nucleotides. The small subunit (glutamine amidotransferase) CC binds and cleaves glutamine to supply the large subunit with the CC substrate ammonia. {ECO:0000256|HAMAP-Rule:MF_01209}. 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 -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; 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. Tetramer of CC heterodimers (alpha,beta)4. {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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; CP031611; AXP08856.1; -; Genomic_DNA. DR EMBL; WHMG01000010; MPV95799.1; -; Genomic_DNA. DR EMBL; WHMF01000009; MPV98565.1; -; Genomic_DNA. DR EMBL; QURW01000009; RQD87479.1; -; Genomic_DNA. DR RefSeq; WP_066779443.1; NZ_WHMR01000009.1. DR STRING; 1813019.A2J15_05285; -. DR GeneID; 44004662; -. DR KEGG; chw:A2J15_003930; -. DR OrthoDB; 9804328at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000093205; Chromosome. DR Proteomes; UP000286095; Unassembled WGS sequence. DR Proteomes; UP000429436; Unassembled WGS sequence. DR Proteomes; UP000430858; Unassembled WGS sequence. DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:TreeGrafter. 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; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 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 NCBIfam; TIGR01368; CPSaseIIsmall; 1. DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. 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 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01209}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}. FT DOMAIN 1..131 FT /note="Carbamoyl-phosphate synthase small subunit N- FT terminal" 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 ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 351 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 353 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT BINDING 45 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 240 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 242 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 269 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 272 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 310 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 313 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" 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 //