ID PYRG_METBU Reviewed; 534 AA. AC Q12WH5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 05-OCT-2016, entry version 71. DE RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; GN OrderedLocusNames=Mbur_1282; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., RA Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., RA Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M., RA Thomas T., Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(2009). 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:0000255|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate; GTP has no effect on the reaction when ammonia CC 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:0000255|HAMAP-Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|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; CP000300; ABE52201.1; -; Genomic_DNA. DR RefSeq; WP_011499346.1; NC_007955.1. DR ProteinModelPortal; Q12WH5; -. DR STRING; 259564.Mbur_1282; -. DR MEROPS; C26.964; -. DR EnsemblBacteria; ABE52201; ABE52201; Mbur_1282. DR GeneID; 3998306; -. DR KEGG; mbu:Mbur_1282; -. DR eggNOG; arCOG00063; Archaea. DR eggNOG; COG0504; LUCA. DR HOGENOM; HOG000077514; -. DR KO; K01937; -. DR OMA; SCSERHR; -. DR BioCyc; MBUR259564:GHBZ-1305-MONOMER; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. 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-HAMAP. DR Gene3D; 3.40.50.300; -; 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; 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; Complete proteome; Glutamine amidotransferase; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis; KW Reference proteome. FT CHAIN 1 534 CTP synthase. FT /FTId=PRO_0000266273. FT DOMAIN 289 530 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 13 18 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 147 149 Allosteric inhibitor CTP. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 186 191 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT NP_BIND 186 191 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT REGION 1 265 Amidoligase domain. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT REGION 380 383 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 379 379 Nucleophile; for glutamine hydrolysis. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 503 503 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 505 505 {ECO:0000255|HAMAP-Rule:MF_01227}. FT METAL 70 70 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT METAL 140 140 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 12 12 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 12 12 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 53 53 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 70 70 ATP. {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 222 222 Allosteric inhibitor CTP; alternate. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 222 222 UTP; alternate. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 352 352 L-glutamine; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT BINDING 403 403 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT BINDING 460 460 L-glutamine; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 534 AA; 59573 MW; A08872A8BBD4BDE9 CRC64; MKYIIVTGGV MSGLGKGITT ASVGRNLKNK GYKVTAIKID PYINIDAGTM SPYQHGEVYV LKDGGEVDLD LGNYERFLDT ELTRDHNLTT GKIYQTVIDK ERKGEYLGKT VQIIPHITNE IKDRIRRIAA KSGADVCLIE VGGTVGDIES MPFLEAVRQM YREESPENIA LLHVTLVPID SQGDQKTKPT QHSVKELREL GLTPHVIVSR CKKALMESTR SKIALFCDVP VEAVISAHDS ADIYEVPLQL ENEGLSNYLL KKLILKSTLE DTNWEEMVIR MNNCTGNVNV AIVGKYTHLE DSYISIVESL KHGAIEIGCK FEITWFDAES FDDDPSEVEK LNGFDGILVP GGFGERGTEG KMLAIKYARE NNIPYLGLCL GMQLAVIEFA RNVVGLDGAN SSEFDENTPY PVIDLLPEQE DVVDMGATMR LGDYEATLKA GSLAESIYGA SLITERHRHR YEVNPNYVDR IEEHGMIFSG KNKNRMEIAE VPSKDFYFAS QFHPEFKSRP GRPSPPFKAF MGAMLKKSKE KKDQ //