ID A0A127W348_SPOPS Unreviewed; 531 AA. AC A0A127W348; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 15-FEB-2017, entry version 9. 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=AZE41_19590 {ECO:0000313|EMBL:AMQ07962.1}; OS Sporosarcina psychrophila (Bacillus psychrophilus). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ07962.1, ECO:0000313|Proteomes:UP000071057}; RN [1] {ECO:0000313|EMBL:AMQ07962.1, ECO:0000313|Proteomes:UP000071057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ07962.1, RC ECO:0000313|Proteomes:UP000071057}; RA Yan W.; RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a RT psychrophila Bacillus that can mediate the Ca2+ precipitation."; RL Submitted (MAR-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: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00675542}. 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:SAAS00675541}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00675548}. 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:SAAS00675551}. 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; CP014616; AMQ07962.1; -; Genomic_DNA. DR RefSeq; WP_067213177.1; NZ_CP014616.1. DR KEGG; spsy:AZE41_19590; -. DR KO; K01937; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000071057; 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:0006241; P:CTP biosynthetic process; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. 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. 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:SAAS00675539}; KW Complete proteome {ECO:0000313|Proteomes:UP000071057}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675556}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675552}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675554}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675547}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675530}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00675546}; KW Reference proteome {ECO:0000313|Proteomes:UP000071057}. FT DOMAIN 292 531 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 505 505 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 507 507 {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 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 460 460 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 531 AA; 59458 MW; B57D3488E366C064 CRC64; MTKYIFVTGG VVSSLGKGIN AASLGRLLKS RGLQVTIQKF DPYINLDPRM MSPLQHGEVF VTEDGAETDL DLGHYERFID IKLNKYSNVT MGKVYSSVLQ KERRGEYNGA TVQVIPHITN EIKSLIKRAG KETNADVVIT EIGGSVGDIE SLPYLEALRQ MKTDLGKSDV MYIHNTLIPY LHAAGEMKTK PTQHSVKELR SLGIQPNMIV VRSEYPVPQE MKDKIALFCN IKPEEVIEAL DAETLYEVPL RLHEQNMDQI VVDFLELETK QPDMTEIKEL VTLVKSLSKK VRIGLVGKYV EMQDAYISAV EALRHAGYGF DTEIEIKWIN SEDVTAQSAA ELLSDVDGIL VPAGFGKRGI DGKIEAITYA RINGIPFFGI GLGMQLAAVE YARNVMGIEN AHSVEFDKDT ENQIIESPPE SNGNPESYFR LGAYPCKLKE GTKARAAYGE ELIYERHRNR YEFNNEYREQ FEAAGMRISG ISPNEQLVEI IELEGHPFFV GVSFHPEFAS RPTRPQPLFR EFLGAIIAGK E //