ID A0A0M2KDF9_9ENTR Unreviewed; 545 AA. AC A0A0M2KDF9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 17-FEB-2016, entry version 4. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037303}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037401}; 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 ECO:0000313|EMBL:KKF35372.1}; GN ORFNames=SY86_07995 {ECO:0000313|EMBL:KKF35372.1}; OS Erwinia tracheiphila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF35372.1, ECO:0000313|Proteomes:UP000033924}; RN [1] {ECO:0000313|EMBL:KKF35372.1, ECO:0000313|Proteomes:UP000033924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF35372.1, RC ECO:0000313|Proteomes:UP000033924}; RA Shapiro L.R.; RT "Erwinia tracheiphila."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. 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:KKF35372.1}. 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; JXNU01000003; KKF35372.1; -; Genomic_DNA. DR RefSeq; WP_016190169.1; NZ_JXNU01000003.1. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000033924; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic 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:SAAS00434461}; KW Complete proteome {ECO:0000313|Proteomes:UP000033924}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434680}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434363, ECO:0000313|EMBL:KKF35372.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434657}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434336}; KW Reference proteome {ECO:0000313|Proteomes:UP000033924}. FT DOMAIN 291 542 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT REGION 1 253 Aminator domain. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 379 379 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 515 515 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 517 517 {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 545 AA; 60314 MW; B5F8AD701C1D9CC5 CRC64; MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPTQHGEV FVTDDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSEVL RKERRGDYLG ATVQVIPHIT NAIKERIIEG GEGNDVVLVE IGGTVGDIES LPFLEAIRQM AVDVGREHTM YMHLTLVPYM AAAGEVKTKP TQHSVKELLS IGIQPDVLIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL LNSQGLDDYI CKRFNLNAPE ANLAEWEQVI YEEANPGGEV TIGMVGKYVE LPDAYKSVIE ALKHGGLKNR VTVNIKLIDS QDVESRGVEL LKDLDAILIP GGFGYRGVEG KLMTARYARE NKVPFLGICL GMQVALMEFA RNVASMENAN STEFVPYCKY PVVALITEWR DEEGNVEVRT EKSDLGGTMR LGSQQCQLTS DSLVRQLYGS DIIVERHRHR YEVNNLLLKQ IEAAGLRVAG RSGDDQLVEI IEIPEHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAANEHQ KRLAK //