ID A0A1M5PXD4_9FIRM Unreviewed; 356 AA. AC A0A1M5PXD4; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 22-FEB-2023, entry version 21. 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 ORFNames=SAMN02745221_01602 {ECO:0000313|EMBL:SHH06535.1}; OS Thermosyntropha lipolytica DSM 11003. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae; OC Thermosyntropha. OX NCBI_TaxID=1123382 {ECO:0000313|EMBL:SHH06535.1, ECO:0000313|Proteomes:UP000242329}; RN [1] {ECO:0000313|Proteomes:UP000242329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11003 {ECO:0000313|Proteomes:UP000242329}; RA Varghese N., Submissions S.; RL Submitted (NOV-2016) 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|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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01209, CC ECO:0000256|PROSITE-ProRule:PRU00605}. 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; FQWY01000027; SHH06535.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1M5PXD4; -. DR STRING; 1123382.SAMN02745221_01602; -. DR EnsemblBacteria; SHH06535; SHH06535; SAMN02745221_01602. DR OrthoDB; 9804328at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000242329; 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-KW. 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 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; 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 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}; Ligase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW Reference proteome {ECO:0000313|Proteomes:UP000242329}. FT DOMAIN 3..133 FT /note="Carbamoyl-phosphate synthase small subunit N- FT terminal" FT /evidence="ECO:0000259|SMART:SM01097" FT REGION 1..174 FT /note="CPSase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 337 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" SQ SEQUENCE 356 AA; 39173 MW; CB9A6F9A2988A205 CRC64; MMKKGYLVLE NGRVFTGKLL NDCLLAGGEV VFTTAMISYQ DIITDPSYYG QIVVMTYPLV GNVGLNEKSY ASRGAMVKGL VLREATDFPS HYEMETDLIS FLNKSEVAVL TEVDTRALTR VLRNEGIMGG VITADISHKD WLVEKARKEA EELKGDLVKY VSRRNIMKFG AGKKRVVLLD LGTKRGVIDS FIRRGCEVVA VPADTGWDEI LNLNPDGVFI SDGPGDPSAV PYAINTCREV LGKKPVFGIG LGHQILALAL GAGINKLPFG HRGGNQPVKD MKNGRVYITT QNHGYCIDEK TIDGTGLQVT MRNLNDNTIE AVEHEKMPAF SVQFDPEGYP GYSETGFLFE KFISMF //