ID UPP_YEAST Reviewed; 216 AA. AC P18562; D3DL77; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Uracil phosphoribosyltransferase; DE Short=UPRTase; DE EC=2.4.2.9 {ECO:0000269|PubMed:1913872, ECO:0000269|PubMed:2189783}; DE AltName: Full=UMP pyrophosphorylase; GN Name=FUR1; OrderedLocusNames=YHR128W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP MUTAGENESIS OF ARG-26; ILE-106 AND GLU-173. RC STRAIN=ATCC 28383 / FL100 / VTT C-80102; RX PubMed=2189783; DOI=10.1016/0378-1119(90)90026-n; RA Kern L., de Montigny J., Jund R., Lacroute F.; RT "The FUR1 gene of Saccharomyces cerevisiae: cloning, structure and RT expression of wild-type and mutant alleles."; RL Gene 88:149-157(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ARG-99, AND RP INDUCTION. RX PubMed=1913872; DOI=10.1007/bf00309592; RA Kern L., de Montigny J., Lacroute F., Jund R.; RT "Regulation of the pyrimidine salvage pathway by the FUR1 gene product of RT Saccharomyces cerevisiae."; RL Curr. Genet. 19:333-337(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26109 / X2180 / NCYC 826; RX PubMed=7929558; DOI=10.1083/jcb.127.1.129; RA Clark S.W., Meyer D.I.; RT "ACT3: a putative centractin homologue in S. cerevisiae is required for RT proper orientation of the mitotic spindle."; RL J. Cell Biol. 127:129-138(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091229; DOI=10.1126/science.8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., RA Waterston R., Wilson R., Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [7] RP IDENTIFICATION OF PROBABLE INITIATION SITE. RX PubMed=12748633; DOI=10.1038/nature01644; RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.; RT "Sequencing and comparison of yeast species to identify genes and RT regulatory elements."; RL Nature 423:241-254(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D- CC ribose 1-diphosphate (PRPP) to UMP and diphosphate in the pyrimidine CC salvage pathway. {ECO:0000269|PubMed:1913872, CC ECO:0000269|PubMed:2189783}. 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:0000269|PubMed:1913872, ECO:0000269|PubMed:2189783}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13019; CC Evidence={ECO:0000305|PubMed:2189783}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. CC {ECO:0000250}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. {ECO:0000250}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; CC UMP from uracil: step 1/1. {ECO:0000305|PubMed:2189783}. CC -!- INTERACTION: CC P18562; P27515: URK1; NbExp=3; IntAct=EBI-20122, EBI-20151; CC -!- INDUCTION: Induced by uracil. {ECO:0000269|PubMed:1913872}. CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA34611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAB19947.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAB68405.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAT93101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA56207.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M36485; AAA34611.1; ALT_INIT; Genomic_DNA. DR EMBL; S57516; AAB19947.2; ALT_INIT; Genomic_DNA. DR EMBL; X79811; CAA56207.1; ALT_INIT; Genomic_DNA. DR EMBL; U10398; AAB68405.1; ALT_INIT; Genomic_DNA. DR EMBL; AY693082; AAT93101.1; ALT_INIT; Genomic_DNA. DR EMBL; BK006934; DAA06821.1; -; Genomic_DNA. DR PIR; JH0147; JH0147. DR RefSeq; NP_011996.2; NM_001179258.1. DR AlphaFoldDB; P18562; -. DR SMR; P18562; -. DR BioGRID; 36561; 70. DR DIP; DIP-1323N; -. DR IntAct; P18562; 17. DR MINT; P18562; -. DR STRING; 4932.YHR128W; -. DR iPTMnet; P18562; -. DR MaxQB; P18562; -. DR PaxDb; 4932-YHR128W; -. DR PeptideAtlas; P18562; -. DR TopDownProteomics; P18562; -. DR EnsemblFungi; YHR128W_mRNA; YHR128W; YHR128W. DR GeneID; 856529; -. DR KEGG; sce:YHR128W; -. DR AGR; SGD:S000001170; -. DR SGD; S000001170; FUR1. DR VEuPathDB; FungiDB:YHR128W; -. DR eggNOG; KOG4203; Eukaryota. DR GeneTree; ENSGT01020000230412; -. DR HOGENOM; CLU_067096_1_1_1; -. DR InParanoid; P18562; -. DR OMA; DIANRWV; -. DR OrthoDB; 1202986at2759; -. DR BioCyc; MetaCyc:YHR128W-MONOMER; -. DR BioCyc; YEAST:YHR128W-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR BioGRID-ORCS; 856529; 2 hits in 10 CRISPR screens. DR PRO; PR:P18562; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P18562; Protein. DR GO; GO:0005737; C:cytoplasm; IC:SGD. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IDA:SGD. DR GO; GO:0008655; P:pyrimidine-containing compound salvage; IDA:SGD. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR PANTHER; PTHR10285:SF171; URACIL PHOSPHORIBOSYLTRANSFERASE HOMOLOG; 1. DR PANTHER; PTHR10285; URIDINE KINASE; 1. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; PRTase-like; 1. PE 1: Evidence at protein level; KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..216 FT /note="Uracil phosphoribosyltransferase" FT /id="PRO_0000120788" FT BINDING 32 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 41 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 75..78 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 77 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 102 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 110 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 131 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 137..145 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 137 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 201 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 207..209 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000250|UniProtKB:Q26998" FT BINDING 208 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MUTAGEN 26 FT /note="R->S: In FUR1-8; causes resistance to 5-fluorouracil FT (5FU)." FT /evidence="ECO:0000269|PubMed:2189783" FT MUTAGEN 99 FT /note="R->S: In FUR1-5; causes resistance to 5-fluorouracil FT (5FU)." FT /evidence="ECO:0000269|PubMed:1913872" FT MUTAGEN 106 FT /note="I->N: In FUR1-7; causes resistance to 5-fluorouracil FT (5FU)." FT /evidence="ECO:0000269|PubMed:2189783" FT MUTAGEN 173 FT /note="E->G: In FUR1-9; causes resistance to 5-fluorouracil FT (5FU)." FT /evidence="ECO:0000269|PubMed:2189783" FT CONFLICT 104 FT /note="Missing (in Ref. 2; AAB19947)" FT /evidence="ECO:0000305" SQ SEQUENCE 216 AA; 24594 MW; E02179D26A53732A CRC64; MSSEPFKNVY LLPQTNQLLG LYTIIRNKNT TRPDFIFYSD RIIRLLVEEG LNHLPVQKQI VETDTNENFE GVSFMGKICG VSIVRAGESM EQGLRDCCRS VRIGKILIQR DEETALPKLF YEKLPEDISE RYVFLLDPML ATGGSAIMAT EVLIKRGVKP ERIYFLNLIC SKEGIEKYHA AFPEVRIVTG ALDRGLDENK YLVPGLGDFG DRYYCV //