ID A0A2T9WUR9_9CREN Unreviewed; 546 AA. AC A0A2T9WUR9; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 05-DEC-2018, 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=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:PVU71556.1}; GN ORFNames=DDW08_04220 {ECO:0000313|EMBL:PVU71556.1}; OS Vulcanisaeta sp. SCGC AB-777_J10. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=1987493 {ECO:0000313|EMBL:PVU71556.1}; RN [1] {ECO:0000313|EMBL:PVU71556.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCGC AB-777_J10 {ECO:0000313|EMBL:PVU71556.1}; RX PubMed=26341207; DOI=.1128/AEM.01539-15; RA Munson-McGee J.H., Field E.K., Bateson M., Rooney C., Stepanauskas R., RA Young M.J.; RT "Nanoarchaeota, Their Sulfolobales Host, and Nanoarchaeota Virus RT Distribution across Yellowstone National Park Hot Springs."; RL Appl. Environ. Microbiol. 81:7860-7868(2015). RN [2] {ECO:0000313|EMBL:PVU71556.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCGC AB-777_J10 {ECO:0000313|EMBL:PVU71556.1}; RA Song R., Chenine A.L., Ruprecht R.M.; RL Submitted (MAY-2017) 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. 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:456216, CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58359; EC=6.3.4.2; CC Evidence={ECO:0000256|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: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- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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:PVU71556.1}. 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; QEFL01000041; PVU71556.1; -; 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-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 Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000313|EMBL:PVU71556.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227}. FT DOMAIN 299 535 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 15 20 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 149 151 Allosteric inhibitor CTP. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 188 193 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 188 193 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT REGION 1 267 Amidoligase domain. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT REGION 383 386 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 382 382 Nucleophile. {ECO:0000256|PROSITE- FT ProRule:PRU00605}. FT ACT_SITE 382 382 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 508 508 {ECO:0000256|HAMAP-Rule:MF_01227, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 510 510 {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 142 142 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 224 224 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 224 224 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 242 242 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 355 355 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 406 406 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 463 463 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 546 AA; 61613 MW; 9242B87D1F075662 CRC64; MTTKYIFITG GVLSGLGKGI TTASIGKILQ ARGYHVTAIK IDPYLNMDAG TMNPFQHGEV FVTFDGGETD LDLGHYERFL DVEVPKYHNI TSGQVYYTVI RRERKGKYLG QTVQLIPHVT EEIKRRIMLV AKREKPDIIL IEVGGTVGDY EGLPFLEAAR QMKLEMPSDV LFVHVALVPV LSTTGELKTK PLQHSVAELR RVGIQPDIII ARAPKPLDES TRRKISLFTN VPINAVFTSH DVNTIYKVPL ILEEQGLGRY IVTKLGLEPR EPRLDDWIAF VRSLEDGKDE VNIYMCGKYV KLHDSYISIV EAIKHAAAKL RIKPNIIWCD TEEIEKEPSK VTELNNADAV IVLPGFGARG VEGKIEAIRY VRENNIPFLG ICYGMQLATV EFARNVANLK GAHTTEVDPN TPYPVIDITP EEKDIKELGG TMILGNRRIN IVKGTIAHAI YGTTEIVERH RHRYEVNPKF FKILTEKGLV FSAWRSDVPR VEMIELPNHY FFVATQFHPE FRSRPLRPHP IFVALLNAAY SKKHGLPSPW SHVLVK //