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P18562 (UPP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uracil phosphoribosyltransferase

Short name=UPRTase
EC=2.4.2.9
Alternative name(s):
UMP pyrophosphorylase
Gene names
Name:FUR1
Ordered Locus Names:YHR128W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

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

Enzyme regulation

Allosterically activated by GTP By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.

Induction

Induced by uracil. Ref.2

Sequence similarities

Belongs to the UPRTase family.

Sequence caution

The sequence AAA34611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAB19947.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAB68405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAT93101.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA56207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

URK1P275154EBI-20122,EBI-20151

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Uracil phosphoribosyltransferase
PRO_0000120788

Regions

Region137 – 14595-phospho-alpha-D-ribose 1-diphosphate binding By similarity
Region207 – 2093Uracil binding By similarity

Sites

Binding site411GTP By similarity
Binding site771GTP By similarity
Binding site8515-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site1021GTP By similarity
Binding site11015-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site1311GTP By similarity
Binding site13715-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site2011Ribose-5-phosphate By similarity
Binding site2021Uracil; via amide nitrogen By similarity
Binding site20815-phospho-alpha-D-ribose 1-diphosphate By similarity

Amino acid modifications

Modified residue821Phosphoserine Ref.8

Experimental info

Mutagenesis261R → S in FUR1-8; causes resistance to 5-fluorouracil (5FU). Ref.1
Mutagenesis991R → S in FUR1-5; causes resistance to 5-fluorouracil (5FU). Ref.2
Mutagenesis1061I → N in FUR1-7; causes resistance to 5-fluorouracil (5FU). Ref.1
Mutagenesis1731E → G in FUR1-9; causes resistance to 5-fluorouracil (5FU). Ref.1
Sequence conflict1041Missing in AAB19947. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18562 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: E02179D26A53732A

FASTA21624,594
        10         20         30         40         50         60 
MSSEPFKNVY LLPQTNQLLG LYTIIRNKNT TRPDFIFYSD RIIRLLVEEG LNHLPVQKQI 

        70         80         90        100        110        120 
VETDTNENFE GVSFMGKICG VSIVRAGESM EQGLRDCCRS VRIGKILIQR DEETALPKLF 

       130        140        150        160        170        180 
YEKLPEDISE RYVFLLDPML ATGGSAIMAT EVLIKRGVKP ERIYFLNLIC SKEGIEKYHA 

       190        200        210 
AFPEVRIVTG ALDRGLDENK YLVPGLGDFG DRYYCV 

« Hide

References

« Hide 'large scale' references
[1]"The FUR1 gene of Saccharomyces cerevisiae: cloning, structure and expression of wild-type and mutant alleles."
Kern L., de Montigny J., Jund R., Lacroute F.
Gene 88:149-157(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ARG-26; ILE-106 AND GLU-173.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]"Regulation of the pyrimidine salvage pathway by the FUR1 gene product of Saccharomyces cerevisiae."
Kern L., de Montigny J., Lacroute F., Jund R.
Curr. Genet. 19:333-337(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ARG-99, INDUCTION.
[3]"ACT3: a putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle."
Clark S.W., Meyer D.I.
J. Cell Biol. 127:129-138(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26109 / X2180 / NCYC 826.
[4]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[8]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJH0147.
RefSeqNP_011996.2. NM_001179258.1.

3D structure databases

ProteinModelPortalP18562.
SMRP18562. Positions 6-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36561. 21 interactions.
DIPDIP-1323N.
IntActP18562. 16 interactions.
MINTMINT-377162.
STRING4932.YHR128W.

Proteomic databases

PaxDbP18562.
PeptideAtlasP18562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR128W; YHR128W; YHR128W.
GeneID856529.
KEGGsce:YHR128W.

Organism-specific databases

CYGDYHR128w.
SGDS000001170. FUR1.

Phylogenomic databases

eggNOGCOG0035.
GeneTreeENSGT00510000047272.
HOGENOMHOG000262755.
KOK00761.
OMAPKLFYEK.
OrthoDBEOG7BKD5H.

Enzyme and pathway databases

BioCycMetaCyc:YHR128W-MONOMER.
YEAST:YHR128W-MONOMER.
UniPathwayUPA00574; UER00636.

Gene expression databases

GenevestigatorP18562.

Family and domain databases

ProtoNetSearch...

Other

NextBio982301.
PROP18562.

Entry information

Entry nameUPP_YEAST
AccessionPrimary (citable) accession number: P18562
Secondary accession number(s): D3DL77
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2006
Last modified: March 19, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways