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 18-SEP-2013, entry version 61. DE RecName: Full=Uracil phosphoribosyltransferase; DE EC=2.4.2.9; DE AltName: Full=UMP pyrophosphorylase; DE AltName: Full=UPRTase; GN Name=upp; 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 RT P. horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha- CC D-ribose 1-diphosphate (PRPP) to UMP and diphosphate (By CC similarity). CC -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: Binds 1 Mg(2+) ion per subunit. The magnesium is bound CC as Mg-PRPP (By similarity). CC -!- ENZYME REGULATION: Allosterically activated by GTP (By CC similarity). CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uracil: step 1/1. CC -!- SIMILARITY: Belongs to the UPRTase family. 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; NP_578970.1; NC_003413.1. DR ProteinModelPortal; Q8U1G7; -. DR SMR; Q8U1G7; 14-217. DR STRING; 186497.PF1241; -. DR PRIDE; Q8U1G7; -. DR EnsemblBacteria; AAL81365; AAL81365; PF1241. DR GeneID; 1469113; -. DR KEGG; pfu:PF1241; -. DR eggNOG; COG0035; -. DR HOGENOM; HOG000262755; -. DR KO; K00761; -. DR OMA; YEVTRDM; -. DR ProtClustDB; PRK00129; -. DR UniPathway; UPA00574; UER00636. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:HAMAP. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006223; P:uracil salvage; IEA:InterPro. DR HAMAP; MF_01218_A; Upp_A; 1; -. DR InterPro; IPR005765; Ura_phspho_trans. DR TIGRFAMs; TIGR01091; upp; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Glycosyltransferase; KW GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 232 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120924. FT NP_BIND 38 42 GTP (By similarity). FT REGION 140 148 5-phospho-alpha-D-ribose 1-diphosphate FT binding (By similarity). FT REGION 209 211 Uracil binding (By similarity). FT BINDING 87 87 5-phospho-alpha-D-ribose 1-diphosphate FT (By similarity). FT BINDING 112 112 5-phospho-alpha-D-ribose 1-diphosphate FT (By similarity). FT BINDING 204 204 Uracil; via amide nitrogen (By FT similarity). FT BINDING 210 210 5-phospho-alpha-D-ribose 1-diphosphate FT (By similarity). 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 //