ID A0A1P8WAS0_9PLAN Unreviewed; 540 AA. AC A0A1P8WAS0; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 29-SEP-2021, entry version 18. 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:APZ91158.1}; GN ORFNames=Fuma_00744 {ECO:0000313|EMBL:APZ91158.1}; OS Fuerstia marisgermanicae. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Fuerstia. OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ91158.1, ECO:0000313|Proteomes:UP000187735}; RN [1] {ECO:0000313|EMBL:APZ91158.1, ECO:0000313|Proteomes:UP000187735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH11 {ECO:0000313|EMBL:APZ91158.1, RC ECO:0000313|Proteomes:UP000187735}; RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079; RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P., RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J., RA Kaster A.K., Rohde M., Wiegand S., Jogler C.; RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the RT Phylum Planctomycetes from the German Wadden Sea."; RL Front. Microbiol. 7:2079-2079(2016). 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; CP017641; APZ91158.1; -; Genomic_DNA. DR RefSeq; WP_077022962.1; NZ_CP017641.1. DR EnsemblBacteria; APZ91158; APZ91158; Fuma_00744. DR KEGG; fmr:Fuma_00744; -. DR OrthoDB; 783657at2; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000187735; Chromosome. 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; 3.40.50.300; -; 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; 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. 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:UP000187735}. FT DOMAIN 3..267 FT /note="CTP_synth_N" FT /evidence="ECO:0000259|Pfam:PF06418" FT DOMAIN 303..526 FT /note="GATase" FT /evidence="ECO:0000259|Pfam:PF00117" FT NP_BIND 14..19 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 147..149 FT /note="CTP; allosteric inhibitor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 187..192 FT /note="CTP; allosteric inhibitor; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT NP_BIND 187..192 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 382..385 FT /note="L-glutamine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT ACT_SITE 381 FT /note="Nucleophile; for glutamine hydrolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT ACT_SITE 507 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT ACT_SITE 509 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT METAL 71 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT METAL 140 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 13 FT /note="CTP; allosteric inhibitor; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 13 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 54 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 71 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 223 FT /note="CTP; allosteric inhibitor; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 223 FT /note="UTP; alternate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 354 FT /note="L-glutamine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 405 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" FT BINDING 462 FT /note="L-glutamine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227" SQ SEQUENCE 540 AA; 60577 MW; E652BF30541D6C0F CRC64; MTRHIFVTGG VVSSLGKGLT SASIGMLLER RGLTVRMQKL DPYINVDPGT MSPYQHGEVY VLDDGSETDL DLGHYERFTS SPLNRDSNYT TGQIYQTVIE KERRGEYLGR TVQVVPHITD EIKASIRRLA APDVDVVITE LGGTIGDIEG LPFLEAIRQI PLDIGKEKCL FIHLTLVPYL KAAREAKTKP TQHSVQQLRT IGIQPDILVC RTERPIGREH TDKIALFCNV EKRAVIEEVD KEYSIYEVPM GLVEHKLDEL IIEKLGMEAG QLQLDDYREL IHRIRNPRHE VTIAVVGKYI EHRDAYKSIY ESLDHAGFQH STRIIAKRIE AEDLERQGAE ALLKGVDGVL IPGGFGMRGV EGKIQAARYA RENNVPYFGI CLGMQVAVIE FARNVMGLQD ANSSEFDGDT QHPVICLLEE QVGMVEKGGT MRLGSQPCVL AEGSNSLQAY GTVEINERHR HRYEFNPQYR EQYIHAGMAP VGTSPDGGLV EIVEVTDHPW YVAVQYHPEF KSQPNKPHPL FTGFIGAALH QRQTRPKQLV //