ID PYRG_GEOLS Reviewed; 535 AA. AC B3EAK5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 26-NOV-2014, entry version 50. DE RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; GN OrderedLocusNames=Glov_1727; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=398767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., RA Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.; RT "Complete sequence of chromosome of Geobacter lovleyi SZ."; RL Submitted (MAY-2008) 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:0000255|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|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; CP001089; ACD95443.1; -; Genomic_DNA. DR RefSeq; YP_001951963.1; NC_010814.1. DR ProteinModelPortal; B3EAK5; -. DR STRING; 398767.Glov_1727; -. DR EnsemblBacteria; ACD95443; ACD95443; Glov_1727. DR GeneID; 6369258; -. DR KEGG; glo:Glov_1727; -. DR PATRIC; 21995129; VBIGeoLov31523_1670. DR eggNOG; COG0504; -. DR HOGENOM; HOG000077515; -. DR KO; K01937; -. DR OMA; SVNIKYI; -. DR OrthoDB; EOG6RC3NR; -. DR BioCyc; GLOV398767:GH32-1753-MONOMER; -. DR UniPathway; UPA00159; UER00277. 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; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 535 CTP synthase. FT /FTId=PRO_1000139463. FT DOMAIN 292 534 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT REGION 1 253 Aminator domain. FT ACT_SITE 381 381 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 507 507 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 509 509 {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 535 AA; 59767 MW; B86BADC1F55A3205 CRC64; MKTKFIFITG GVVSSIGKGL AAASLGALLE SRGLRVTMQK LDPYINVDPG TMSPFQHGEV FVTDDGAETD LDLGHYERYT SARLSKKSNF TTGQVYFSVI DKERRGDYLG GTVQVIPHIT DEIKSKIIEN AKGADVAIVE VGGTVGDIES LPFLEAIRQF RFDRGAGNTL YVHVTLVPYI RTAGEMKTKP TQHSVMELRK IGIQPDILLC RCDRELPQDM KKKISLFCNV EESCVIPSVD SEHIYAVPLA LNKERLDEQV VEKLNIWTKQ PDLTPWQDVV ETLRHPSHGE VRIAIVGKYV NLTESYKSLA EALTHGGIAN DCRVYLKYVD AEKIEENGVE GWLDDVDGVL VPGGFGERGT EGKVLAIEYA RTRQIPFFGI CLGMQMAAIE FARNVCGLAK ACSTEFKNDC KEPVIHLMEE QKSVNKKGGT MRLGACPCTV TKGTKAFDAY NEADISERHR HRYEFNNTYR ELMTTKGLVL SGINQQKDLV EIIELPDHPW FLACQFHPEF KSKPLVPHPL FRAFIGASLT HRNQR //