ID A0A2T9WUR9_9CREN Unreviewed; 546 AA. AC A0A2T9WUR9; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 07-APR-2021, entry version 12. 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; Thermoproteaceae; OC Vulcanisaeta; unclassified Vulcanisaeta. OX NCBI_TaxID=1987493 {ECO:0000313|EMBL:PVU71556.1, ECO:0000313|Proteomes:UP000245871}; RN [1] {ECO:0000313|EMBL:PVU71556.1, ECO:0000313|Proteomes:UP000245871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AB-777_J10 {ECO:0000313|EMBL:PVU71556.1}; RX PubMed=26341207; DOI=10.1128/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). 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|ARBA:ARBA00000314, ECO:0000256|HAMAP- CC Rule:MF_01227}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is CC the substrate; GTP has no effect on the reaction when ammonia is the CC substrate. The allosteric effector GTP functions by stabilizing the CC protein conformation that binds the tetrahedral intermediate(s) formed CC during glutamine hydrolysis. Inhibited by the product CTP, via CC allosteric rather than competitive inhibition. {ECO:0000256|HAMAP- CC Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171, CC ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing CC between UTP and CTP. The overlapping regions of the product feedback CC inhibitory and substrate sites recognize a common feature in both CC compounds, the triphosphate moiety. To differentiate isosteric CC substrate and product pyrimidine rings, an additional pocket far from CC the expected kinase/ligase catalytic site, specifically recognizes the CC cytosine and ribose portions of the product inhibitor. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 Proteomes; UP000245871; Unassembled WGS sequence. 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; cd03113; CTPS_N; 1. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01227}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_01227}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01227}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01227}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01227}; Reference proteome {ECO:0000313|Proteomes:UP000245871}. FT DOMAIN 299..535 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000259|PROSITE:PS51273" FT NP_BIND 15..20 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 149..151 FT /note="Allosteric inhibitor CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 188..193 FT /note="Allosteric inhibitor CTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 188..193 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT REGION 1..267 FT /note="Amidoligase domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT REGION 383..386 FT /note="L-glutamine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT ACT_SITE 382 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 382 FT /note="Nucleophile; for glutamine hydrolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT ACT_SITE 508 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 510 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT METAL 72 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT METAL 142 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 14 FT /note="Allosteric inhibitor CTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 14 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 72 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 224 FT /note="Allosteric inhibitor CTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 224 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 242 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 355 FT /note="L-glutamine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 406 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 463 FT /note="L-glutamine; via amide nitrogen" FT /evidence="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 //