ID PYRG_SPHAL Reviewed; 543 AA. AC Q1GTY6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 02-MAR-2010, entry version 34. DE RecName: Full=CTP synthase; DE EC=6.3.4.2; DE AltName: Full=UTP--ammonia ligase; DE AltName: Full=CTP synthetase; GN Name=pyrG; OrderedLocusNames=Sala_1170; OS Sphingopyxis alaskensis (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=117207; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., RA Chertkov O., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., RA Ting L.M., Richardson P.; RT "Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."; RL Submitted (APR-2006) 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 (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP (By similarity). CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the CTP synthase family. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. 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; CP000356; ABF52886.1; -; Genomic_DNA. DR RefSeq; YP_616219.1; -. DR SMR; Q1GTY6; 2-541. DR GeneID; 4080876; -. DR GenomeReviews; CP000356_GR; Sala_1170. DR KEGG; sal:Sala_1170; -. DR NMPDR; fig|317655.9.peg.1104; -. DR HOGENOM; HBG597806; -. DR OMA; CLGLQCM; -. DR ProtClustDB; PRK05380; -. DR BioCyc; SALA317655:SALA_1170-MONOMER; -. DR BRENDA; 6.3.4.2; 297633. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01227; PyrG; 1; -. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE_1. DR InterPro; IPR000991; GATase_class1_C. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis. FT CHAIN 1 543 CTP synthase. FT /FTId=PRO_0000266223. FT DOMAIN 291 542 Glutamine amidotransferase type-1. FT REGION 1 252 Aminator domain. FT ACT_SITE 381 381 Nucleophile (By similarity). FT ACT_SITE 515 515 By similarity. FT ACT_SITE 517 517 By similarity. SQ SEQUENCE 543 AA; 59457 MW; B33AAC32224CA804 CRC64; MARFIFITGG VVSSLGKGLM AASLAALLQA RGYRVRIRKF DPYLNVDPGT MSPYQHGEVY VTDDGAETDL DLGHYERFTG VAARQSDNVT SGRIYQGIIA KERRGDYLGA TVQVVPHVTD AIKDFARAET DDLDFVLCEI GGTVGDIESL PFIEAIRQLK NEVGRDNAIS VHVTLVPYIA AAGELKTKPT QHSVRELASL GVQPDILLCR CEKPLPDSER AKIALFCNVR KEAVIPALDA DSIYSVPVQY HGEGLDSEVL RAFGILDAPA PDLTAWYDIM DRKQHPEGEV TIGVVGKYVS LPDAYKSLNE ALVHGGMAHR VKVNIRWLDA EMFERDEDLV ANLEPLHGIL VPGGFGERGS EGKIASVRFA RERNVPFFGI CLGMQMACIE AARNTSGIAN ASSTEFGPTD EPVVGLITEW MSAEGLQKRG ANTDLGGTMR LGAYDAKLSP NSHVASVYGT NEISERHRHR YEVNGAYRER LEKGGLVFSG MSPDGMLPEI VERPDHPWFI GVQFHPELKS KPFDPHPLFA GFIEAAVKQS RLV //