ID A0A3Q9FKI8_9BACT Unreviewed; 363 AA. AC A0A3Q9FKI8; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 27-NOV-2024, entry version 20. 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=EI427_00215 {ECO:0000313|EMBL:AZQ60684.1}; OS Flammeovirga pectinis. OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae; OC Flammeovirga. OX NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ60684.1, ECO:0000313|Proteomes:UP000267268}; RN [1] {ECO:0000313|EMBL:AZQ60684.1, ECO:0000313|Proteomes:UP000267268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L12M1 {ECO:0000313|EMBL:AZQ60684.1, RC ECO:0000313|Proteomes:UP000267268}; RA Bae J.-W., Jeong Y.-S., Kang W.; RT "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean RT scallop, Patinopecten yessoensis."; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. 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=hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl CC phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+); 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=L-glutamine + H2O = 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 --------------------------------------------------------------------------- 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; CP034562; AZQ60684.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3Q9FKI8; -. DR KEGG; fll:EI427_00215; -. DR OrthoDB; 9804328at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000267268; Chromosome 1. 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:0004359; F:glutaminase activity; IEA:RHEA. 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 FunFam; 3.50.30.20:FF:000001; Carbamoyl-phosphate synthase small chain; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000267268}. FT DOMAIN 4..134 FT /note="Carbamoyl-phosphate synthase small subunit N- FT terminal" FT /evidence="ECO:0000259|SMART:SM01097" FT REGION 1..173 FT /note="CPSase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 254 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 340 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 342 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT BINDING 48 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 226 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 228 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 255 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 258 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 296 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 298 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT BINDING 299 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" SQ SEQUENCE 363 AA; 39990 MW; A53C412DAC04C6C4 CRC64; MEKKTAILML QDGTTYKGTA IGAIGTTTGE ICFNTSMTGY QEIYTDPSYY GQIIVNTVSH IGNYGTVHNE NESAKPQING LVVKSFSSVY SRNTAEGSLQ DYLENANLVG IADIDTRELV RHIRQKGAMN AIITSEISDL DEIKKKLKAT PDMEGLELSS VVCTKEPYSV GDPHAAVKVA VLDLGIKKSI LDNFTSRGML CKVFPSNTTF EQMKQWKPDG YFLSNGPGDP AVMDYAVETA KQILEADKPL FGICLGHQVI SRAVGLSTYK MHHGHRGANH PVKNLISGRS EITSQNHGFA VDMDSIKKND NIELTHINLN DDTVEGIKVL DKKAFSIQYH PEASPGPHDS RYLFTRFLEL IQD //