ID A0A424Z0B6_9BACT Unreviewed; 372 AA. AC A0A424Z0B6; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 24-JAN-2024, entry version 23. 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}, 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; Campylobacterota; 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; CC Evidence={ECO:0000256|ARBA:ARBA00001777, 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|HAMAP- CC 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 OrthoDB; 9804328at2; -. 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-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" 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 //