ID A0A424Z0B6_9PROT Unreviewed; 372 AA. AC A0A424Z0B6; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 02-DEC-2020, entry version 11. 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:ARBA00019661, 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}, GC023_04825 GN {ECO:0000313|EMBL:MPV77436.1}; 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|EMBL:MPV77436.1, ECO:0000313|Proteomes:UP000430858, ECO:0000313|Proteomes:UP000451781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QLD_3/QLD {ECO:0000313|EMBL:MPV77436.1, RC ECO:0000313|Proteomes:UP000451781}, and VIC_4/VIC RC {ECO:0000313|EMBL:MPV98565.1, ECO:0000313|Proteomes:UP000430858}; 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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RQD87479.1}. 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; WHMF01000009; MPV98565.1; -; Genomic_DNA. DR EMBL; QURW01000009; RQD87479.1; -; Genomic_DNA. DR RefSeq; WP_066779443.1; NZ_WHMR01000009.1. DR GeneID; 44004662; -. DR KEGG; chw:A2J15_003930; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000286095; Unassembled WGS sequence. DR Proteomes; UP000430858; Unassembled WGS sequence. DR Proteomes; UP000451781; 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_01209, 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 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000259|PROSITE:PS51273" 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 //