ID D6YWF4_WADCW Unreviewed; 538 AA. AC D6YWF4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-JAN-2019, entry version 63. 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=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227}; DE Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227}; DE Short=CTPS {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:ADI38465.1}; GN OrderedLocusNames=wcw_1108 {ECO:0000313|EMBL:ADI38465.1}; OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044). OC Bacteria; Chlamydiae; Parachlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38465.1, ECO:0000313|Proteomes:UP000001505}; RN [1] {ECO:0000313|EMBL:ADI38465.1, ECO:0000313|Proteomes:UP000001505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505}; RX PubMed=20531937; DOI=10.1371/journal.pone.0010890; RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.; RT "The Waddlia genome: a window into chlamydial biology."; RL PLoS ONE 5:E10890-E10890(2010). 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: 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:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS01116648}; 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: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:SAAS00710815}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00710816}. 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:SAAS00710794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|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; CP001928; ADI38465.1; -; Genomic_DNA. DR RefSeq; WP_013182178.1; NZ_LVEB01000045.1. DR ProteinModelPortal; D6YWF4; -. DR STRING; 716544.wcw_1108; -. DR EnsemblBacteria; ADI38465; ADI38465; wcw_1108. DR KEGG; wch:wcw_1108; -. DR eggNOG; ENOG4105C8D; Bacteria. DR eggNOG; COG0504; LUCA. DR HOGENOM; HOG000077515; -. DR KO; K01937; -. DR OMA; EFNNAYR; -. DR OrthoDB; 783657at2; -. DR BioCyc; WCHO716544:G1GLF-1079-MONOMER; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000001505; 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-UniRule. 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 {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710699}; KW Complete proteome {ECO:0000313|Proteomes:UP000001505}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00710676}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710762, ECO:0000313|EMBL:ADI38465.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710689}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710675}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710810}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710748}; KW Reference proteome {ECO:0000313|Proteomes:UP000001505}. FT DOMAIN 294 537 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 15 20 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 189 194 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 189 194 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. {ECO:0000256|PROSITE- FT ProRule:PRU00605}. FT ACT_SITE 384 384 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 510 510 {ECO:0000256|HAMAP-Rule:MF_01227, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 512 512 {ECO:0000256|HAMAP-Rule:MF_01227, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT METAL 72 72 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 143 143 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 14 14 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 14 14 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 72 72 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 225 225 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 225 225 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 243 243 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 465 465 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 538 AA; 60421 MW; E21E9942FFB01F74 CRC64; MSTKYIFFTG GVCSSLGKGL TAASTALLLE KKGLRVAMLK LDPYLNVDPG TMNPFQHGEV YVTDDGAETD LDLGHYYRYS NSPLSKASNA TSGQIYNTVI KRERHGDYLG NTVQVIPHIT DEIKRRILNC ARQEDGIDIL IIEIGGTVGD IESLPFLEAI RQFRNENERN CISIHLTYVP YIKAAGEVKT KPTQHSVQSL REIGLYPDII LCRSEMTLPD SVKDKISLFC NVNRKAVIEE VDVEHSIYEV PLELKNQGLD SMIMELLHLE DKEIDMSEWI KIVDTIKNPK GKITVGVVGK YVKHQDAYKS VFEALDHGAL AHGYELEIKR FEADKVLTAA DLEQAFGRCD GYLIPGGFGE RGWEGKIQAA KYCRENKIPY FGICLGMQVM SVEFARNAAK LEDANTTEVD PGTSTPIISL LSEQQQVSDM GGTMRLGAQD CLIEKGSKAF EIYDSEKISE RHRHRYEFNS KYKELMEKAG LRISGKHAET KLCEIVEVED HPWMIGVQFH PEFKSKPTAP HPLFRSFIEA AIKRKTSS //