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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 2 (URA10), Orotate phosphoribosyltransferase 1 (URA5)
  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)DescriptionActionsGraphical viewLength
Binding sitei305-phosphoribose 1-diphosphateBy similarity1
Binding sitei1065-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity1
Binding sitei1075-phosphoribose 1-diphosphateBy similarity1
Binding sitei1105-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity1
Binding sitei1125-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity1
Binding sitei136OrotateBy similarity1
Binding sitei164OrotateBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001108041 – 226Orotate phosphoribosyltransferase 1Add BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei213PhosphoserineCombined sources1
Modified residuei225PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13298.
PRIDEiP13298.
TopDownProteomicsiP13298.

PTM databases

iPTMnetiP13298.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

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

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 18Combined sources12
Beta strandi21 – 28Combined sources8
Beta strandi30 – 32Combined sources3
Beta strandi34 – 39Combined sources6
Helixi41 – 43Combined sources3
Helixi47 – 63Combined sources17
Beta strandi69 – 73Combined sources5
Turni75 – 77Combined sources3
Helixi78 – 92Combined sources15
Helixi95 – 97Combined sources3
Beta strandi101 – 105Combined sources5
Beta strandi118 – 121Combined sources4
Beta strandi127 – 131Combined sources5
Beta strandi136 – 138Combined sources3
Helixi139 – 150Combined sources12
Beta strandi154 – 163Combined sources10
Beta strandi166 – 168Combined sources3
Helixi178 – 186Combined sources9
Beta strandi190 – 195Combined sources6
Helixi196 – 203Combined sources8
Turni204 – 206Combined sources3
Helixi209 – 222Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13298.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 39Orotate bindingBy similarity2
Regioni76 – 775-phosphoribose 1-diphosphate bindingBy similarity2
Regioni132 – 1405-phosphoribose 1-diphosphate bindingBy similarity9

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000076056.
HOGENOMiHOG000037974.
InParanoidiP13298.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG092C4SG4.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti150N → S in CAA32901 (PubMed:2651891).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP13298.

Proteomic databases

MaxQBiP13298.
PRIDEiP13298.
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.
OMAiMKAYQRQ.
OrthoDBiEOG092C4SG4.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP13298.
PROiP13298.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE. 1 hit.
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...

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: November 2, 2016
This is version 156 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.