ID A0A1D9NYZ4_9FIRM Unreviewed; 536 AA. AC A0A1D9NYZ4; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 07-OCT-2020, entry version 16. 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 ORFNames=bhn_I0109 {ECO:0000313|EMBL:AOZ95145.1}; OS Butyrivibrio hungatei. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ95145.1, ECO:0000313|Proteomes:UP000179284}; RN [1] {ECO:0000313|Proteomes:UP000179284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284}; RA Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J., RA Attwood G.T.; RT "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei RT MB2003."; RL Submitted (OCT-2016) 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: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 --------------------------------------------------------------------------- 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; CP017831; AOZ95145.1; -; Genomic_DNA. DR RefSeq; WP_071174961.1; NZ_CP017831.1. DR KEGG; bhu:bhn_I0109; -. DR KO; K01937; -. DR OrthoDB; 783657at2; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000179284; Chromosome i. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01227}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|PROSITE-ProRule:PRU00605}; 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:UP000179284}. FT DOMAIN 293..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 189..194 FT /note="Allosteric inhibitor CTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 189..194 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT REGION 1..268 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 225 FT /note="Allosteric inhibitor CTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 225 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 243 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 536 AA; 60017 MW; F908E8338E313BCE CRC64; MAVKYIFVTG GVVSGLGKGI TAASLGRLLK ARGYKVTMQK FDPYINIDPG TMNPVQHGEV FVTEDGTETD LDLGHYERFI DENLDKNSNV TTGKIYWSVL QKERRGDYGG RTVQVIPHIT NEIKSKFYRN FTDDETRIAI IEVGGTVGDI ESQPFLEAIR QFQHEVGREN AMLILVSLIP YLRCSEEIKT KPTQSAVKTM QGMGLQPDVI VCRTEIELDQ DTKDKIALFC NVPSSHVLNN LDLEYLYEAP LAMEKEHLAQ VACECLELDC PEPDLTDWKA MVDTLYSLKH EVKVALVGKY TQLHDAYISV VEALKHGGIS NQTAVDIKWV DSEEVNDENV ASYLSDVDGI IVPGGFGDRG IEGMISSIKY ARENNVPFLG LCLGMQLAII EFARDVIGYK DAHSIEFDPN TTHPMIALLP DQNGVEDIGG TLRLGSYPCV LDKESKAYEL FGSTDITERH RHRYEVNNDY RTVLVQNGMR LCGMSPDGRI VEMIELPSND FHMATQAHPE LKSRPNRPHP LFSGFIKASL EHENKR //