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Protein

Uracil phosphoribosyltransferase 2

Gene

SPAC1399.04c

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 conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.By similarity

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 1 (SPAC1B3.01c), Uracil phosphoribosyltransferase 2 (SPAC1399.04c), Putative uracil phosphoribosyltransferase urg2 (urg2)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 8715-phospho-alpha-D-ribose 1-diphosphateBy similarity
Binding sitei113 – 11315-phospho-alpha-D-ribose 1-diphosphateBy similarity
Binding sitei134 – 1341GTPBy similarity
Binding sitei140 – 14015-phospho-alpha-D-ribose 1-diphosphateBy similarity
Binding sitei204 – 2041Ribose-5-phosphateBy similarity
Binding sitei205 – 2051Uracil; via amide nitrogenBy similarity
Binding sitei211 – 21115-phospho-alpha-D-ribose 1-diphosphateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 804GTPBy similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00574; UER00636.

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil phosphoribosyltransferase 2 (EC:2.4.2.9)
Short name:
UPRTase 2
Alternative name(s):
UMP pyrophosphorylase 2
Gene namesi
ORF Names:SPAC1399.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1399.04c.
PomBaseiSPAC1399.04c.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Uracil phosphoribosyltransferase 2PRO_0000120787Add
BLAST

Proteomic databases

MaxQBiQ9HE15.

Interactioni

Protein-protein interaction databases

BioGridi279068. 29 interactions.
MINTiMINT-4703011.

Structurei

3D structure databases

ProteinModelPortaliQ9HE15.
SMRiQ9HE15. Positions 9-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 14895-phospho-alpha-D-ribose 1-diphosphate bindingBy similarity
Regioni210 – 2123Uracil bindingBy similarity

Sequence similaritiesi

Belongs to the UPRTase family.Curated

Phylogenomic databases

HOGENOMiHOG000262755.
InParanoidiQ9HE15.
KOiK00761.
OMAiMTIIRDV.
OrthoDBiEOG7BKD5H.
PhylomeDBiQ9HE15.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
InterProiIPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HE15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIPLEQPEN VVVLRQTMYL LSLMTILRDQ QTGHSEFVRT ANLIINMLMQ
60 70 80 90 100
EALSALPYKK CLIKTSSGGT YTGVQPARDI CGVSILRAGE SMEYGLAAAC
110 120 130 140 150
NYSVPVGKLL VQRDETTFEA KLMFCKLPKD AQDRLVLLLD PLLATGNSVI
160 170 180 190 200
LAIQTLINKG IPEENIVFVN LIACNEGITN VFAKFPKLRM VTASIDPELN
210 220
ANKYVVPGCG DFGDRYFGTC
Length:220
Mass (Da):24,155
Last modified:March 1, 2001 - v1
Checksum:iAE1756C4DD11C37C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC19743.1.
RefSeqiNP_593510.1. NM_001018944.1.

Genome annotation databases

EnsemblFungiiSPAC1399.04c.1; SPAC1399.04c.1:pep; SPAC1399.04c.
GeneIDi2542614.
KEGGispo:SPAC1399.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC19743.1.
RefSeqiNP_593510.1. NM_001018944.1.

3D structure databases

ProteinModelPortaliQ9HE15.
SMRiQ9HE15. Positions 9-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279068. 29 interactions.
MINTiMINT-4703011.

Proteomic databases

MaxQBiQ9HE15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1399.04c.1; SPAC1399.04c.1:pep; SPAC1399.04c.
GeneIDi2542614.
KEGGispo:SPAC1399.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1399.04c.
PomBaseiSPAC1399.04c.

Phylogenomic databases

HOGENOMiHOG000262755.
InParanoidiQ9HE15.
KOiK00761.
OMAiMTIIRDV.
OrthoDBiEOG7BKD5H.
PhylomeDBiQ9HE15.

Enzyme and pathway databases

UniPathwayiUPA00574; UER00636.

Miscellaneous databases

PROiQ9HE15.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
InterProiIPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
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 nameiUPP2_SCHPO
AccessioniPrimary (citable) accession number: Q9HE15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 83 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

Allosteric enzyme, 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.