ID A0A1D9NYZ4_9FIRM Unreviewed; 536 AA. AC A0A1D9NYZ4; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 16-JAN-2019, entry version 11. 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|EMBL:AOZ95145.1, ECO:0000313|Proteomes:UP000179284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MB2003 {ECO:0000313|EMBL:AOZ95145.1, RC 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 RT hungatei 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|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; 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|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710699}; KW Complete proteome {ECO:0000313|Proteomes:UP000179284}; 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}; 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:UP000179284}. FT DOMAIN 293 535 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 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 1 268 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 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 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 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 //