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Protein

Orotate phosphoribosyltransferase 1

Gene

URA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).By similarity

Catalytic activityi

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes UMP from orotate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Orotate phosphoribosyltransferase 1 (URA5), Orotate phosphoribosyltransferase 2 (URA10)
  2. Orotidine 5'-phosphate decarboxylase (URA3)
This subpathway is part of the pathway UMP biosynthesis via de novo 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 orotate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 3015-phosphoribose 1-diphosphateBy similarity
Binding sitei106 – 10615-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei107 – 10715-phosphoribose 1-diphosphateBy similarity
Binding sitei110 – 11015-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei112 – 11215-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei136 – 1361OrotateBy similarity
Binding sitei164 – 1641OrotateBy similarity

GO - Molecular functioni

  • orotate phosphoribosyltransferase activity Source: SGD

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: SGD
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • pyrimidine ribonucleoside biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

BioCyciYEAST:YML106W-MONOMER.
BRENDAi2.4.2.10. 984.
UniPathwayiUPA00070; UER00119.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotate phosphoribosyltransferase 1 (EC:2.4.2.10)
Short name:
OPRT 1
Short name:
OPRTase 1
Gene namesi
Name:URA5
Synonyms:PYR5
Ordered Locus Names:YML106W
ORF Names:YM8339.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML106W.
SGDiS000004574. URA5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Orotate phosphoribosyltransferase 1PRO_0000110804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei225 – 2251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13298.
PeptideAtlasiP13298.
TopDownProteomicsiP13298.

PTM databases

iPTMnetiP13298.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi35037. 70 interactions.
DIPiDIP-4859N.
IntActiP13298. 4 interactions.
MINTiMINT-548974.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1812Combined sources
Beta strandi21 – 288Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 396Combined sources
Helixi41 – 433Combined sources
Helixi47 – 6317Combined sources
Beta strandi69 – 735Combined sources
Turni75 – 773Combined sources
Helixi78 – 9215Combined sources
Helixi95 – 973Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi136 – 1383Combined sources
Helixi139 – 15012Combined sources
Beta strandi154 – 16310Combined sources
Beta strandi166 – 1683Combined sources
Helixi178 – 1869Combined sources
Beta strandi190 – 1956Combined sources
Helixi196 – 2038Combined sources
Turni204 – 2063Combined sources
Helixi209 – 22214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PRYX-ray2.35A1-226[»]
2PRZX-ray1.90A/B/C/D1-226[»]
2PS1X-ray1.75A/B1-226[»]
4WMLX-ray1.73A2-226[»]
4WN3X-ray1.80A1-226[»]
ProteinModelPortaliP13298.
SMRiP13298. Positions 3-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13298.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 392Orotate bindingBy similarity
Regioni76 – 7725-phosphoribose 1-diphosphate bindingBy similarity
Regioni132 – 14095-phosphoribose 1-diphosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000076056.
HOGENOMiHOG000037974.
InParanoidiP13298.
KOiK00762.
OMAiATAIAYH.
OrthoDBiEOG76X69W.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIMLEDYQK NFLELAIECQ ALRFGSFKLK SGRESPYFFN LGLFNTGKLL
60 70 80 90 100
SNLATAYAIA IIQSDLKFDV IFGPAYKGIP LAAIVCVKLA EIGGSKFQNI
110 120 130 140 150
QYAFNRKEAK DHGEGGIIVG SALENKRILI IDDVMTAGTA INEAFEIISN
160 170 180 190 200
AKGQVVGSII ALDRQEVVST DDKEGLSATQ TVSKKYGIPV LSIVSLIHII
210 220
TYLEGRITAE EKSKIEQYLQ TYGASA
Length:226
Mass (Da):24,664
Last modified:February 1, 1996 - v2
Checksum:iECF3A01EB35BC03F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501N → S in CAA32901 (PubMed:2651891).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14795 Genomic DNA. Translation: CAA32901.1.
Z49210 Genomic DNA. Translation: CAA89112.1.
AY693160 Genomic DNA. Translation: AAT93179.1.
X65783 Genomic DNA. Translation: CAA46665.1.
BK006946 Genomic DNA. Translation: DAA09792.1.
PIRiS53966. XJBY5.
RefSeqiNP_013601.1. NM_001182468.1.

Genome annotation databases

EnsemblFungiiYML106W; YML106W; YML106W.
GeneIDi854865.
KEGGisce:YML106W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14795 Genomic DNA. Translation: CAA32901.1.
Z49210 Genomic DNA. Translation: CAA89112.1.
AY693160 Genomic DNA. Translation: AAT93179.1.
X65783 Genomic DNA. Translation: CAA46665.1.
BK006946 Genomic DNA. Translation: DAA09792.1.
PIRiS53966. XJBY5.
RefSeqiNP_013601.1. NM_001182468.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PRYX-ray2.35A1-226[»]
2PRZX-ray1.90A/B/C/D1-226[»]
2PS1X-ray1.75A/B1-226[»]
4WMLX-ray1.73A2-226[»]
4WN3X-ray1.80A1-226[»]
ProteinModelPortaliP13298.
SMRiP13298. Positions 3-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35037. 70 interactions.
DIPiDIP-4859N.
IntActiP13298. 4 interactions.
MINTiMINT-548974.

PTM databases

iPTMnetiP13298.

Proteomic databases

MaxQBiP13298.
PeptideAtlasiP13298.
TopDownProteomicsiP13298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML106W; YML106W; YML106W.
GeneIDi854865.
KEGGisce:YML106W.

Organism-specific databases

EuPathDBiFungiDB:YML106W.
SGDiS000004574. URA5.

Phylogenomic databases

GeneTreeiENSGT00550000076056.
HOGENOMiHOG000037974.
InParanoidiP13298.
KOiK00762.
OMAiATAIAYH.
OrthoDBiEOG76X69W.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00119.
BioCyciYEAST:YML106W-MONOMER.
BRENDAi2.4.2.10. 984.

Miscellaneous databases

EvolutionaryTraceiP13298.
NextBioi977789.
PROiP13298.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the URA5 gene of Saccharomyces cerevisiae."
    de Montigny J., Belarbi A., Hubert J.-C., Lacroute F.
    Mol. Gen. Genet. 215:455-462(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Stirling C.J.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-226.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYRE_YEAST
AccessioniPrimary (citable) accession number: P13298
Secondary accession number(s): D6W0H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two genes coding for OPRT in yeast.
Present with 39300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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