ID A0A3Q9FKI8_9BACT Unreviewed; 363 AA. AC A0A3Q9FKI8; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 08-MAY-2019, entry version 2. 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 sp. L12M1. OC Bacteria; Bacteroidetes; 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 -!- 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 --------------------------------------------------------------------------- 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 UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000267268; Chromosome 1. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC. 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 Complete proteome {ECO:0000313|Proteomes:UP000267268}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209, ECO:0000313|EMBL:AZQ60684.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}. FT DOMAIN 178 363 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT REGION 1 173 CPSase. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 254 254 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01209, ECO:0000256|PROSITE-ProRule: FT PRU00605}. FT ACT_SITE 340 340 {ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 342 342 {ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605}. 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 //