ID A0A127W348_SPOPS Unreviewed; 531 AA. AC A0A127W348; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 08-JUN-2016, entry version 2. 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=CTP 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=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}; 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. CC {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037305}. 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. Inhibited by CTP. {ECO:0000256|HAMAP- CC 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 -!- 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 --------------------------------------------------------------------------- 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 Proteomes; UP000071057; Chromosome. 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:UP000071057}; 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 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 REGION 1 254 Aminator domain. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 505 505 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 507 507 {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 //