ID A0A090QM87_9FLAO Unreviewed; 539 AA. AC A0A090QM87; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-NOV-2016, entry version 17. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638782}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638793}; DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227}; GN ORFNames=JCM19294_960 {ECO:0000313|EMBL:GAK96651.1}; OS Nonlabens sediminis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Nonlabens. OX NCBI_TaxID=319236 {ECO:0000313|EMBL:GAK96651.1, ECO:0000313|Proteomes:UP000029221}; RN [1] {ECO:0000313|EMBL:GAK96651.1, ECO:0000313|Proteomes:UP000029221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19294 {ECO:0000313|Proteomes:UP000029221}; RA Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W., RA Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., RA Thompson F.L., Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains RT NR17, NR24, NR27, NR32, NR33, and Ara13."; RL Genome Announc. 2:e01165-14(2014). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. Regulates CC intracellular CTP levels through interactions with the four CC ribonucleotide triphosphates. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638784}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate; GTP has no effect on the reaction when ammonia CC is the substrate. The allosteric effector GTP functions by CC stabilizing the protein conformation that binds the tetrahedral CC intermediate(s) formed during glutamine hydrolysis. Inhibited by CC the product CTP, via allosteric rather than competitive CC inhibition. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638787}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638797}. CC -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for CC distinguishing between UTP and CTP. The overlapping regions of the CC product feedback inhibitory and substrate sites recognize a common CC feature in both compounds, the triphosphate moiety. To CC differentiate isosteric substrate and product pyrimidine rings, an CC additional pocket far from the expected kinase/ligase catalytic CC site, specifically recognizes the cytosine and ribose portions of CC the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638789}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-Rule:MF_01227}. 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:GAK96651.1}. 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; BBML01000003; GAK96651.1; -; Genomic_DNA. DR RefSeq; WP_042278077.1; NZ_BBML01000003.1. DR EnsemblBacteria; GAK96651; GAK96651; JCM19294_960. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000029221; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR CDD; cd01746; GATase1_CTP_Synthase; 1. DR Gene3D; 3.40.50.300; -; 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|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638801}; KW Complete proteome {ECO:0000313|Proteomes:UP000029221}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638788}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638786, ECO:0000313|EMBL:GAK96651.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638781}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638795}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638799}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638802}; KW Reference proteome {ECO:0000313|Proteomes:UP000029221}. FT DOMAIN 295 536 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 16 21 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 150 152 Allosteric inhibitor CTP. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 190 195 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 190 195 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT REGION 1 269 Amidoligase domain. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT REGION 385 388 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 384 384 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 511 511 {ECO:0000256|HAMAP-Rule:MF_01227}. FT METAL 73 73 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 143 143 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 15 15 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 15 15 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 56 56 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 73 73 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 226 226 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 226 226 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 244 244 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 357 357 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 408 408 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 464 464 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 539 AA; 60423 MW; AE1F87BC41595BA5 CRC64; MAHAKYIFVT GGVTSSLGKG IIAASLAKLL QARGLRVTIQ KLDPYINVDP GTLNPYEHGE CYVTEDGAET DLDLGHYERF LNVNTSQANN VTTGRIYQSV IQKERRGEFL GKTVQVIPHI TDEIKERIQI LGKSGDYDVI ITEIGGTVGD IESLPYIESV RQLQWELGDN NSLVIHLTLI PFLSAAGELK TKPTQHSVKT LMESGVQADI LVCRTEHELS DEIRTKLARF CNVKPEAVIQ SIDVETIYDV PNKMLLEGLD RVVIKQLHIE TESQPNLKSW NEFVIKHKNP KSQVTIGLIG KYVELQDSYK SILEAFIHAG AENEVKVKIE SIHSEYLEVE NVEKKLSHLD GILVAPGFGE RGIEGKIEAV RYARENGLPF FGICLGMQMA VIEYSRNVLG LKESNSIEMD DNTPHPVISL MEDQKNILDM GGTMRLGAWD CKLNGGKVSE IYGNELISER HRHRYEYNNE YRNQLEQAGL KTTGVNPKTD LVEIVEIENH PWFIGVQYHP EYKSTVANPH PLFKSFVAAA ATFKSNKNK //