ID A0A210QFF8_MIZYE Unreviewed; 613 AA. AC A0A210QFF8; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 31-JUL-2019, entry version 10. DE RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713}; DE EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713}; DE AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713}; GN ORFNames=KP79_PYT07716 {ECO:0000313|EMBL:OWF47484.1}; OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia; OC Pectinoida; Pectinoidea; Pectinidae; Mizuhopecten. OX NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF47484.1, ECO:0000313|Proteomes:UP000242188}; RN [1] {ECO:0000313|Proteomes:UP000242188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188}; RX PubMed=28812685; DOI=10.1038/s41559-017-0120; RA Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P., RA Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D., RA Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., RA Liang J., Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., RA Zhao L., Xing Q., Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., RA Jiang W., Fu Q., Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., RA Kong Y., Jiang Z., Chourrout D., Li R., Bao Z.; RT "Scallop genome provides insights into evolution of bilaterian RT karyotype and development."; RL Nat. Ecol. Evol. 1:120-120(2017). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000256|RuleBase:RU810713}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L- CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; CC Evidence={ECO:0000256|RuleBase:RU810713}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000256|RuleBase:RU810713}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|RuleBase:RU810713}. 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:OWF47484.1}. 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; NEDP02003883; OWF47484.1; -; Genomic_DNA. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000242188; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01746; GATase1_CTP_Synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR033828; GATase1_CTP_Synthase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU810713}; KW Complete proteome {ECO:0000313|Proteomes:UP000242188}; KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605, KW ECO:0000256|RuleBase:RU810713}; KW Ligase {ECO:0000256|RuleBase:RU810713}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU810713}; KW Pyrimidine biosynthesis {ECO:0000256|RuleBase:RU810713}; KW Reference proteome {ECO:0000313|Proteomes:UP000242188}. FT DOMAIN 303 557 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT REGION 592 613 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 592 607 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT ACT_SITE 402 402 Nucleophile. {ECO:0000256|PROSITE- FT ProRule:PRU00605}. FT ACT_SITE 529 529 {ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 531 531 {ECO:0000256|PROSITE-ProRule:PRU00605}. SQ SEQUENCE 613 AA; 68621 MW; 2F49A79ECF63F722 CRC64; MKYILVTGGV ISGIGKGVIA SSLGVILKSC GIRVTSIKID PYINIDAGTF SPYEHGEVFV LDDGGEVDLD LGNYERFMDI KLHRDNNITT GKIYQHVINR ERRGDYLGKT VQVVPHITDA IQEWVERVAK IPVDGDNTQP EVCIVELGGT IGDIEGMPFI EAFRQFFQFR VKREDYCLVH VSLVPQPQAT GEQKSKPTQS SVRELRGLGL SPDLIVCRCQ NPVDDSVKAK ISLFCHVEPG QVLSIHDVSS IYRVPLLLQE QGVSLYLIDR LKMAKLSSPH AGNIMFKWRD LADRYDRMLK EVTIALVGKY TRLEDAYASV IKALKHSSLS VSHRLNLRYI EATHLEADML KESPSKYHEA WHQLVSSDGI LVPGGFGVRG TEGKILATNW ARTKNVPFLG VCLGLQCAAI EFARSELGWT DAHSTELDPQ TKHPVVIDMP EHNTGQMGAT MRLGKRKTLF KTENSIIKRL YGNVQFVEER HRHRYEVNPK YIKDFEDRGM KFVGRSEDGQ RMEILELENH RYFVAVQYHP EYISRPMKPS PPYLGLLLAS CGKLSSYAAR GYRLSPHLSY SEGNNSEDEE IASIVQNLQV SSSSSSSKSS LESSPKAQAE GAN //