ID PYRG_XANOM Reviewed; 554 AA. AC Q2P1K5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 05-DEC-2018, entry version 86. 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=XOO2817; OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=342109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF 311018; RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests RT contribution of large numbers of effector genes and insertion RT sequences to its race diversity."; RL Jpn. Agric. Res. Q. 39:275-287(2005). 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: 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: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; AP008229; BAE69572.1; -; Genomic_DNA. DR RefSeq; WP_011259532.1; NC_007705.1. DR ProteinModelPortal; Q2P1K5; -. DR SMR; Q2P1K5; -. DR PRIDE; Q2P1K5; -. DR EnsemblBacteria; BAE69572; BAE69572; BAE69572. DR GeneID; 34179129; -. DR KEGG; xom:XOO2817; -. DR HOGENOM; HOG000156188; -. DR KO; K01937; -. DR OMA; EFNNAYR; -. DR OrthoDB; POG091H02IX; -. DR UniPathway; UPA00159; UER00277. 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; Glutamine amidotransferase; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis. FT CHAIN 1 554 CTP synthase. FT /FTId=PRO_0000266266. FT DOMAIN 292 545 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 381 384 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 380 380 Nucleophile; for glutamine hydrolysis. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 518 518 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 520 520 {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 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 353 353 L-glutamine; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 404 404 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 471 471 L-glutamine; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 554 AA; 61559 MW; 23615CCFCE279B1B CRC64; MTPLIFVTGG VVSSLGKGIA AASLASILEA RGLKVTMMKL DPYINVDPGT MSPFQHGEVY VTDDGAETDL DLGHYERYVR TRLSRKNSVT TGRIYENVIR KERRGDYLGA TVQVIPHITD EIRRCIDEAT AGFDVALIEI GGTVGDIESL PFLEAIRQVR TERGAEKAMF MHLTLVPYIA AAGELKTKPT QHSVKELRSI GIQPDVLLCR SEQAVPDSER RKIALFTNVS ERAVISCPDI DVLYGMPLEL LRQGLDELVI VQFKLRDKVA AADLSEWAAV VDAVKHPLDE VTIAVVGKYV DHQDAYKSVA EALRHGGLRQ RTKVNLKWLE AQDLERSDMA ALQDIDGILV PGGFGDRGFE GKVQTSKFAR EHKVPYFGIC YGMQAAVVDY ARHVADLDAA NSTENDRQSP HPVIGLITEW RTATGEVEKR DEKSDLGGTM RLGLQEQRLK PGTLARELYG KDVVAERHRH RYEFNNRYRT QLEDAGLVIS GKSMDDTLVE VVELPRDTHP WFLACQAHPE FLSTPRDGHP LFIGFVRAAR EKKAGGKLLK EARA //