ID UPP_PYRFU Reviewed; 232 AA. AC Q8U1G7; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 26-FEB-2020, entry version 91. DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218}; DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218}; GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=PF1241; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D- CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01218}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. CC {ECO:0000255|HAMAP-Rule:MF_01218}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. CC {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; CC UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP- CC Rule:MF_01218}. 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; AE009950; AAL81365.1; -; Genomic_DNA. DR RefSeq; WP_011012384.1; NZ_CP023154.1. DR SMR; Q8U1G7; -. DR STRING; 186497.PF1241; -. DR PRIDE; Q8U1G7; -. DR EnsemblBacteria; AAL81365; AAL81365; PF1241. DR GeneID; 41713046; -. DR KEGG; pfu:PF1241; -. DR PATRIC; fig|186497.12.peg.1303; -. DR eggNOG; arCOG04128; Archaea. DR eggNOG; COG0035; LUCA. DR HOGENOM; CLU_067096_2_0_2; -. DR KO; K00761; -. DR OMA; TYATRMP; -. DR OrthoDB; 85528at2157; -. DR BioCyc; PFUR186497:G1FZR-1271-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006223; P:uracil salvage; IEA:InterPro. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01218_A; Upp_A; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR034331; Upp_A. DR InterPro; IPR005765; Ura_phspho_trans. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01091; upp; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..232 FT /note="Uracil phosphoribosyltransferase" FT /id="PRO_0000120924" FT NP_BIND 38..42 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT REGION 140..148 FT /note="5-phospho-alpha-D-ribose 1-diphosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT REGION 209..211 FT /note="Uracil binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 87 FT /note="5-phospho-alpha-D-ribose 1-diphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 112 FT /note="5-phospho-alpha-D-ribose 1-diphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 204 FT /note="Uracil; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 210 FT /note="5-phospho-alpha-D-ribose 1-diphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" SQ SEQUENCE 232 AA; 26164 MW; CE7E6ADD397A42E0 CRC64; MIEDKRWGGV YSFEDSPYIM EILTELRDKD TDSIKFRKGL VKLGRYMGYE ITKTMDVEKV KVETPLEETE GIIVKDRRNV VIITVLRAAI PFMEGLIKVF EHARVGIVSA ARGKPPKFEI EMNYIKIPQI TPEDTVIVAD PMIATGSTLL RVLEEVKKYG TPKRTLVVGV LAAPEGITRI KEKFPEVEIF VAKIDRELND KGYILPGLGD AGDRAFGEPV KITTLPQVHY IE //