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Protein

Orotate phosphoribosyltransferase

Gene

ura5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (ura5)
  2. Orotidine 5'-phosphate decarboxylase (ura4)
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 sitei25 – 2515-phosphoribose 1-diphosphateBy similarity
Binding sitei98 – 9815-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei99 – 9915-phosphoribose 1-diphosphateBy similarity
Binding sitei102 – 10215-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei104 – 10415-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei128 – 1281OrotateBy similarity
Binding sitei156 – 1561OrotateBy similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

ReactomeiR-SPO-500753. Pyrimidine biosynthesis.
UniPathwayiUPA00070; UER00119.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotate phosphoribosyltransferase (EC:2.4.2.10)
Short name:
OPRT
Short name:
OPRTase
Gene namesi
Name:ura5
ORF Names:SPBC725.15
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC725.15.
PomBaseiSPBC725.15. ura5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Orotate phosphoribosyltransferasePRO_0000110800Add
BLAST

Proteomic databases

MaxQBiO94331.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi277681. 65 interactions.
MINTiMINT-4683300.

Structurei

3D structure databases

ProteinModelPortaliO94331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 342Orotate bindingBy similarity
Regioni71 – 7225-phosphoribose 1-diphosphate bindingBy similarity
Regioni124 – 13295-phosphoribose 1-diphosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000037974.
InParanoidiO94331.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG76X69W.
PhylomeDBiO94331.

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.

O94331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYKLELLRR ALEHNVLKFG TFTLKSGRKS PYFFNSGNFT HGADLCALAE
60 70 80 90 100
AYAETIIAMN VDFDVIFGPA YKGISLAAIT AVKLYEKTGK SYGFAYNRKE
110 120 130 140 150
AKSHGEGGNL VGAEMEGKKV LLLDDVITAG TAIREAISFL EPKHVKLAGI
160 170 180 190 200
VLLLDRQERL DPEVNESTIG RLKKELNLPV SSILTLDDIV DFTKSDLTAA
210
ESKAMDAYRQ QYQAK
Length:215
Mass (Da):23,716
Last modified:May 1, 1999 - v1
Checksum:i2ECCE404DEC08DFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22187.1.
PIRiT40667.
RefSeqiNP_595495.1. NM_001021406.2.

Genome annotation databases

EnsemblFungiiSPBC725.15.1; SPBC725.15.1:pep; SPBC725.15.
GeneIDi2541166.
KEGGispo:SPBC725.15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22187.1.
PIRiT40667.
RefSeqiNP_595495.1. NM_001021406.2.

3D structure databases

ProteinModelPortaliO94331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277681. 65 interactions.
MINTiMINT-4683300.

Proteomic databases

MaxQBiO94331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC725.15.1; SPBC725.15.1:pep; SPBC725.15.
GeneIDi2541166.
KEGGispo:SPBC725.15.

Organism-specific databases

EuPathDBiFungiDB:SPBC725.15.
PomBaseiSPBC725.15. ura5.

Phylogenomic databases

HOGENOMiHOG000037974.
InParanoidiO94331.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG76X69W.
PhylomeDBiO94331.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00119.
ReactomeiR-SPO-500753. Pyrimidine biosynthesis.

Miscellaneous databases

NextBioi20802279.
PROiO94331.

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

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiPYRE_SCHPO
AccessioniPrimary (citable) accession number: O94331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 1999
Last modified: December 9, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.