ID A0A090QM87_9FLAO Unreviewed; 539 AA. AC A0A090QM87; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 01-APR-2015, entry version 5. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=CTP 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}; RN [1] {ECO:0000313|EMBL:GAK96651.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 19294 {ECO:0000313|EMBL:GAK96651.1}; 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. CC {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037305}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00037321}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP. {ECO:0000256|HAMAP- CC 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:SAAS00037318}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01227}. 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 UniPathway; UPA00159; UER00277. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. 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 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; 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:SAAS00037320}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037346}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037369}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037390}. FT DOMAIN 295 536 Glutamine amidotransferase type-1. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT REGION 1 256 Aminator domain. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 384 384 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 511 511 {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 //