ID A0A3G7FI62_9MUSC Unreviewed; 196 AA. AC A0A3G7FI62; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 29-MAY-2024, entry version 9. DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738}; DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738}; DE Flags: Fragment; GN Name=CAD {ECO:0000313|EMBL:AZC86000.1}; OS Liriomyza cicerina. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Opomyzoidea; OC Agromyzidae; Phytomyzinae; Liriomyza. OX NCBI_TaxID=1659330 {ECO:0000313|EMBL:AZC86000.1}; RN [1] {ECO:0000313|EMBL:AZC86000.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30445780; RA Carapelli A., Soltani A., Leo C., Vitale M., Amri M., RA Mediouni-Ben Jemaa J.; RT "Cryptic Diversity Hidden within the Leafminer Genus Liriomyza (Diptera: RT Agromyzidae)."; RL Genes (Basel) 9:E554-E554(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; CC Evidence={ECO:0000256|ARBA:ARBA00043737}; CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine) CC chain promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000256|ARBA:ARBA00044031}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; MH878827; AZC86000.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3G7FI62; -. DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:TreeGrafter. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:TreeGrafter. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR036480; CarbP_synth_ssu_N_sf. DR InterPro; IPR029062; Class_I_gatase-like. 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; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}. FT DOMAIN 1..74 FT /note="Carbamoyl-phosphate synthase small subunit N- FT terminal" FT /evidence="ECO:0000259|SMART:SM01097" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AZC86000.1" FT NON_TER 196 FT /evidence="ECO:0000313|EMBL:AZC86000.1" SQ SEQUENCE 196 AA; 21838 MW; 1C25B8E421D7F212 CRC64; KDEYGMPKHF EWFEGISIAA LVVGEICETP SHWRAKENLS QWMAKNKVPG ISGIDTRALT KKIREHGAIL GRIVYEKPVD GIAYKFSDPN ARNLVAECSI TKPLVFNEKG SPRICAIDCG LKLNQIKCFV SRGARVELVP WNHQLDERKF DGLFISNGPG NPQVCQEVVT QIQRVLKSGK NPIFGICLGH QLLAKA //