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Protein

Uracil phosphoribosyltransferase

Gene

FUR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.2 Publications

Catalytic activityi

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.By similarity

Enzyme regulationi

Allosterically activated by GTP.By similarity

Pathwayi: UMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes UMP from uracil.
Proteins known to be involved in this subpathway in this organism are:
  1. Uracil phosphoribosyltransferase (FUR1)
This subpathway is part of the pathway UMP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from uracil, the pathway UMP biosynthesis via salvage pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei32GTPBy similarity1
Binding sitei41GTPBy similarity1
Binding sitei77GTPBy similarity1
Binding sitei855-phospho-alpha-D-ribose 1-diphosphateBy similarity1
Binding sitei102GTPBy similarity1
Binding sitei1105-phospho-alpha-D-ribose 1-diphosphateBy similarity1
Binding sitei131GTPBy similarity1
Binding sitei1375-phospho-alpha-D-ribose 1-diphosphateBy similarity1
Binding sitei201Ribose-5-phosphateBy similarity1
Binding sitei202Uracil; via amide nitrogenBy similarity1
Binding sitei2085-phospho-alpha-D-ribose 1-diphosphateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi75 – 78GTPBy similarity4

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • uracil phosphoribosyltransferase activity Source: SGD

GO - Biological processi

  • pyrimidine-containing compound salvage Source: SGD
  • UMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YHR128W-MONOMER.
YEAST:YHR128W-MONOMER.
UniPathwayiUPA00574; UER00636.

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil phosphoribosyltransferase (EC:2.4.2.9)
Short name:
UPRTase
Alternative name(s):
UMP pyrophosphorylase
Gene namesi
Name:FUR1
Ordered Locus Names:YHR128W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR128W.
SGDiS000001170. FUR1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26R → S in FUR1-8; causes resistance to 5-fluorouracil (5FU). 1 Publication1
Mutagenesisi99R → S in FUR1-5; causes resistance to 5-fluorouracil (5FU). 1 Publication1
Mutagenesisi106I → N in FUR1-7; causes resistance to 5-fluorouracil (5FU). 1 Publication1
Mutagenesisi173E → G in FUR1-9; causes resistance to 5-fluorouracil (5FU). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001207881 – 216Uracil phosphoribosyltransferaseAdd BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP18562.
PRIDEiP18562.
TopDownProteomicsiP18562.

PTM databases

iPTMnetiP18562.

Expressioni

Inductioni

Induced by uracil.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
URK1P275154EBI-20122,EBI-20151

Protein-protein interaction databases

BioGridi36561. 21 interactors.
DIPiDIP-1323N.
IntActiP18562. 16 interactors.
MINTiMINT-377162.

Structurei

3D structure databases

ProteinModelPortaliP18562.
SMRiP18562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 1455-phospho-alpha-D-ribose 1-diphosphate bindingBy similarity9
Regioni207 – 209Uracil bindingBy similarity3

Sequence similaritiesi

Belongs to the UPRTase family.Curated

Phylogenomic databases

GeneTreeiENSGT00510000047272.
HOGENOMiHOG000262755.
InParanoidiP18562.
KOiK00761.
OMAiRVITGWI.
OrthoDBiEOG092C4GPE.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.

Sequencei

Sequence statusi: Complete.

P18562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEPFKNVY LLPQTNQLLG LYTIIRNKNT TRPDFIFYSD RIIRLLVEEG
60 70 80 90 100
LNHLPVQKQI VETDTNENFE GVSFMGKICG VSIVRAGESM EQGLRDCCRS
110 120 130 140 150
VRIGKILIQR DEETALPKLF YEKLPEDISE RYVFLLDPML ATGGSAIMAT
160 170 180 190 200
EVLIKRGVKP ERIYFLNLIC SKEGIEKYHA AFPEVRIVTG ALDRGLDENK
210
YLVPGLGDFG DRYYCV
Length:216
Mass (Da):24,594
Last modified:September 5, 2006 - v2
Checksum:iE02179D26A53732A
GO

Sequence cautioni

The sequence AAA34611 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB19947 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB68405 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAT93101 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA56207 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti104Missing in AAB19947 (PubMed:1913872).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36485 Genomic DNA. Translation: AAA34611.1. Different initiation.
S57516 Genomic DNA. Translation: AAB19947.2. Different initiation.
X79811 Genomic DNA. Translation: CAA56207.1. Different initiation.
U10398 Genomic DNA. Translation: AAB68405.1. Different initiation.
AY693082 Genomic DNA. Translation: AAT93101.1. Different initiation.
BK006934 Genomic DNA. Translation: DAA06821.1.
PIRiJH0147.
RefSeqiNP_011996.2. NM_001179258.1.

Genome annotation databases

EnsemblFungiiYHR128W; YHR128W; YHR128W.
GeneIDi856529.
KEGGisce:YHR128W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36485 Genomic DNA. Translation: AAA34611.1. Different initiation.
S57516 Genomic DNA. Translation: AAB19947.2. Different initiation.
X79811 Genomic DNA. Translation: CAA56207.1. Different initiation.
U10398 Genomic DNA. Translation: AAB68405.1. Different initiation.
AY693082 Genomic DNA. Translation: AAT93101.1. Different initiation.
BK006934 Genomic DNA. Translation: DAA06821.1.
PIRiJH0147.
RefSeqiNP_011996.2. NM_001179258.1.

3D structure databases

ProteinModelPortaliP18562.
SMRiP18562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36561. 21 interactors.
DIPiDIP-1323N.
IntActiP18562. 16 interactors.
MINTiMINT-377162.

PTM databases

iPTMnetiP18562.

Proteomic databases

MaxQBiP18562.
PRIDEiP18562.
TopDownProteomicsiP18562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR128W; YHR128W; YHR128W.
GeneIDi856529.
KEGGisce:YHR128W.

Organism-specific databases

EuPathDBiFungiDB:YHR128W.
SGDiS000001170. FUR1.

Phylogenomic databases

GeneTreeiENSGT00510000047272.
HOGENOMiHOG000262755.
InParanoidiP18562.
KOiK00761.
OMAiRVITGWI.
OrthoDBiEOG092C4GPE.

Enzyme and pathway databases

UniPathwayiUPA00574; UER00636.
BioCyciMetaCyc:YHR128W-MONOMER.
YEAST:YHR128W-MONOMER.

Miscellaneous databases

PROiP18562.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiUPP_YEAST
AccessioniPrimary (citable) accession number: P18562
Secondary accession number(s): D3DL77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.