ID A0A1V4U0K2_9EURY Unreviewed; 354 AA. AC A0A1V4U0K2; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 16-JAN-2019, entry version 10. 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=trpG_2 {ECO:0000313|EMBL:OPX66089.1}; GN Synonyms=carA {ECO:0000256|HAMAP-Rule:MF_01209}; GN ORFNames=A4E37_02037 {ECO:0000313|EMBL:OPX66089.1}; OS Methanoregulaceae archaeon PtaB.Bin056. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanoregulaceae. OX NCBI_TaxID=1811721 {ECO:0000313|EMBL:OPX66089.1}; RN [1] {ECO:0000313|EMBL:OPX66089.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PtaB.Bin056 {ECO:0000313|EMBL:OPX66089.1}; RA Nobu M.K., Narihiro T., Liu M., Kuroda K., Mei R., Liu W.-T.; RT "Diverse syntrophic catabolism for escaping thermodynamic limitations RT and driving niche segregation."; RL Submitted (FEB-2017) 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:OPX66089.1}. 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; MVQD01000106; OPX66089.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. 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:0016829; F:lyase activity; IEA:UniProtKB-KW. 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|HAMAP-Rule:MF_01209, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Lyase {ECO:0000313|EMBL:OPX66089.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}. FT DOMAIN 173 354 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT REGION 1 172 CPSase. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 248 248 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01209, ECO:0000256|PROSITE-ProRule: FT PRU00605}. FT ACT_SITE 331 331 {ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 333 333 {ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605}. SQ SEQUENCE 354 AA; 38477 MW; B219EB4EAE6DDCF9 CRC64; MEIMKAVLGL EDGTCVTGEG FGAVGECSGE LVFSTQMGGY MEALTDPSYH GQILMFTFPT IGNYGVDRMN FQAPRVWALG CVAREICPVP EARPAFADFF EENGLLGIQG VDTRMLTVKT RVQGTLRAAL LVGDEDTDRA VDMARRAKPI SDADLIPAVS CTEPYHIAGK GKRIAVIDLG IKKNMIISLR HRDADIHVFP YNSTPDQVMA CRPDALFISN GPGDPVHATD AIRCVKDLAG TLPIYGICMG NQICGLGLGG KTYKMKFGHR GTNQPVRYKD GSIYITTQNH GFAVAADTLP EGANVLYSNV NDGTLEGFED PYLEITCVQF HPEAHGGPRD TEIPFFDTMF RRLG //