UPP_YEAST
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 03-AUG-2022, entry version 177.
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};
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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; 65.
DR DIP; DIP-1323N; -.
DR IntAct; P18562; 17.
DR MINT; P18562; -.
DR STRING; 4932.YHR128W; -.
DR iPTMnet; P18562; -.
DR MaxQB; P18562; -.
DR PaxDb; P18562; -.
DR PRIDE; P18562; -.
DR TopDownProteomics; P18562; -.
DR EnsemblFungi; YHR128W_mRNA; YHR128W; YHR128W.
DR GeneID; 856529; -.
DR KEGG; sce:YHR128W; -.
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; TYATRMP; -.
DR BioCyc; MetaCyc:YHR128W-MON; -.
DR BioCyc; YEAST:YHR128W-MON; -.
DR UniPathway; UPA00574; UER00636.
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 SUPFAM; SSF53271; SSF53271; 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
