ID A0A081LE79_9BACI Unreviewed; 535 AA. AC A0A081LE79; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 04-FEB-2015, entry version 3. 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=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}; RN [1] {ECO:0000313|EMBL:KEP27555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DW5-4 {ECO:0000313|EMBL:KEP27555.1}; 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. 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}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains glutamine amidotransferase type-1 domain. CC {ECO:0000256|SAAS:SAAS00037304}. 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 UniPathway; UPA00159; UER00277. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic 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:SAAS00037320}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037346}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037369}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037390}. FT DOMAIN 292 534 Glutamine amidotransferase type-1. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT REGION 1 254 Aminator domain. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 381 381 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 507 507 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 509 509 {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 //