ID PYRG_SPHAL Reviewed; 543 AA. AC Q1GTY6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 10-OCT-2018, entry version 85. DE RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; GN OrderedLocusNames=Sala_1170; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256; RX PubMed=19805210; DOI=10.1073/pnas.0903507106; RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S., RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A., RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V., RA Robb F.T., Kjelleberg S., Cavicchioli R.; RT "The genomic basis of trophic strategy in marine bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009). 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:0000255|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- ACTIVITY REGULATION: Allosterically activated by GTP, when CC glutamine is the substrate; GTP has no effect on the reaction when CC ammonia 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:0000255|HAMAP-Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}. 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:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01227}. 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; CP000356; ABF52886.1; -; Genomic_DNA. DR RefSeq; WP_011541471.1; NC_008048.1. DR ProteinModelPortal; Q1GTY6; -. DR SMR; Q1GTY6; -. DR STRING; 317655.Sala_1170; -. DR MEROPS; C26.964; -. DR PRIDE; Q1GTY6; -. DR EnsemblBacteria; ABF52886; ABF52886; Sala_1170. DR KEGG; sal:Sala_1170; -. DR eggNOG; ENOG4105C8D; Bacteria. DR eggNOG; COG0504; LUCA. DR HOGENOM; HOG000077515; -. DR KO; K01937; -. DR OMA; EFNNAYR; -. DR OrthoDB; POG091H02IX; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000006578; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule. 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-KW. 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; Complete proteome; Glutamine amidotransferase; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis; KW Reference proteome. FT CHAIN 1 543 CTP synthase. FT /FTId=PRO_0000266223. FT DOMAIN 291 542 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 14 19 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 146 148 Allosteric inhibitor CTP. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 186 191 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 186 191 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT REGION 1 265 Amidoligase domain. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT REGION 382 385 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 381 381 Nucleophile; for glutamine hydrolysis. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 515 515 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 517 517 {ECO:0000255|HAMAP-Rule:MF_01227}. FT METAL 71 71 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT METAL 139 139 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 13 13 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 13 13 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 54 54 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 71 71 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 222 222 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 222 222 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 354 354 L-glutamine; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 405 405 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 470 470 L-glutamine; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 543 AA; 59457 MW; B33AAC32224CA804 CRC64; MARFIFITGG VVSSLGKGLM AASLAALLQA RGYRVRIRKF DPYLNVDPGT MSPYQHGEVY VTDDGAETDL DLGHYERFTG VAARQSDNVT SGRIYQGIIA KERRGDYLGA TVQVVPHVTD AIKDFARAET DDLDFVLCEI GGTVGDIESL PFIEAIRQLK NEVGRDNAIS VHVTLVPYIA AAGELKTKPT QHSVRELASL GVQPDILLCR CEKPLPDSER AKIALFCNVR KEAVIPALDA DSIYSVPVQY HGEGLDSEVL RAFGILDAPA PDLTAWYDIM DRKQHPEGEV TIGVVGKYVS LPDAYKSLNE ALVHGGMAHR VKVNIRWLDA EMFERDEDLV ANLEPLHGIL VPGGFGERGS EGKIASVRFA RERNVPFFGI CLGMQMACIE AARNTSGIAN ASSTEFGPTD EPVVGLITEW MSAEGLQKRG ANTDLGGTMR LGAYDAKLSP NSHVASVYGT NEISERHRHR YEVNGAYRER LEKGGLVFSG MSPDGMLPEI VERPDHPWFI GVQFHPELKS KPFDPHPLFA GFIEAAVKQS RLV //