ID A0A081LE79_9BACI Unreviewed; 535 AA. AC A0A081LE79; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-SEP-2016, entry version 13. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037303}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037401}; 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 AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227}; GN ORFNames=BA70_10510 {ECO:0000313|EMBL:KEP27555.1}; OS Bacillus sp. DW5-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1178540 {ECO:0000313|EMBL:KEP27555.1, ECO:0000313|Proteomes:UP000028091}; RN [1] {ECO:0000313|EMBL:KEP27555.1, ECO:0000313|Proteomes:UP000028091} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW5-4 {ECO:0000313|EMBL:KEP27555.1, RC ECO:0000313|Proteomes:UP000028091}; RA Lai Q., Liu Y., Shao Z.; RT "Genome Sequence of Bacillus sp. DW5-4."; RL Submitted (SEP-2012) 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: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00037321}. 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: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:SAAS00037318}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00356542}. 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:SAAS00548960}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEP27555.1}. 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; JOTP01000003; KEP27555.1; -; Genomic_DNA. DR RefSeq; WP_034318251.1; NZ_JOTP01000003.1. DR EnsemblBacteria; KEP27555; KEP27555; BA70_10510. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000028091; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. 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 {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434461}; KW Complete proteome {ECO:0000313|Proteomes:UP000028091}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434680}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434363}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00615993}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00615990}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434657}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00434336}. FT DOMAIN 292 534 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 14 19 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 148 150 Allosteric inhibitor CTP. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 188 193 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 188 193 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT REGION 1 267 Amidoligase domain. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT REGION 382 385 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 381 381 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 507 507 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227}. FT METAL 71 71 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 141 141 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 13 13 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 13 13 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 54 54 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 71 71 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 224 224 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 224 224 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 242 242 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 354 354 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 405 405 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 462 462 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 535 AA; 59715 MW; 5C1F20E946D25BA1 CRC64; MTKYIFVTGG VVSSLGKGIT AASLGRLLKN RGMDVTIQKF DPYINVDPGT MSPYQHGEVF VTDDGAETDL DLGHYERFID INLNKYSNVT TGKIYSTVLK KERRGDYLGG TVQVIPHITN EIKDRVYRAG KETGADVVIT EIGGTVGDIE SLPFLEAIRQ MKSDIGRENV MYIHCTLVPY IRAAGELKTK PTQHSVKELR SLGIQPNVIV VRTEMPMTQD MKDKIALFCD IDTKAVIECQ DADTLYSIPL DLQKQGLDKL VCEHMKLECQ DADMTEWTAL VDKVQNLSKQ VTIGLVGKYV ELQDAYISVV ESLRHAGYAF DADVQIKWIN AEEVTAENIA DFAQDVDGMI VPGGFGDRGV EGKIIATQYA RENKVPFFGI CLGMQVASIE YARNVLGLEG AHSAEIDPET AFPIIDLLPE QKDVDDLGGT LRLGLYPCKL NEDSKAFAAY NDEVVYERHR HRYEFNNEYR QQMEAAGFVF SGTSPDGRLV EIIELKDHPW FLASQFHPEF ISRPTRPQPL FRDFVGASLQ ASESK //