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Protein

Thymidine phosphorylase

Gene

Tymp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity).By similarity

Catalytic activityi

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.

Pathwayi: dTMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes dTMP from thymine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Thymidine phosphorylase (Tymp)
  2. no protein annotated in this organism
This subpathway is part of the pathway dTMP 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 dTMP from thymine, the pathway dTMP biosynthesis via salvage pathway and in Pyrimidine metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-RNO-73614. Pyrimidine salvage.
R-RNO-73621. Pyrimidine catabolism.
UniPathwayiUPA00578; UER00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine phosphorylase (EC:2.4.2.4)
Short name:
TP
Alternative name(s):
TdRPase
Gene namesi
Name:Tymp
Synonyms:Ecgf1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1305756. Tymp.

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075244.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003190991 – 476Thymidine phosphorylaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphothreonineCombined sources1
Modified residuei475PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5FVR2.
PRIDEiQ5FVR2.

PTM databases

iPTMnetiQ5FVR2.
PhosphoSitePlusiQ5FVR2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000032394.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039935.

Chemistry databases

BindingDBiQ5FVR2.

Structurei

3D structure databases

ProteinModelPortaliQ5FVR2.
SMRiQ5FVR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IIV8. Eukaryota.
COG0213. LUCA.
GeneTreeiENSGT00390000009250.
HOGENOMiHOG000047313.
HOVERGENiHBG000082.
InParanoidiQ5FVR2.
KOiK00758.
OMAiQMVASIM.
OrthoDBiEOG091G08UG.
PhylomeDBiQ5FVR2.
TreeFamiTF332198.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
InterProiView protein in InterPro
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR000053. Thymidine/pyrmidine_PPase.
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiView protein in Pfam
PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiView protein in SMART
SM00941. PYNP_C. 1 hit.
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02644. Y_phosphoryl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5FVR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPGTPPPL APETAGADSG GGSGEHRQLP ELIRLKRNGG HLSEADIRNF
60 70 80 90 100
VHALMDGRAQ DTQIGAMLMA IRLQGMDLEE TSVLTQALAE SGQQLEWPKA
110 120 130 140 150
WHQQLVDKHS TGGVGDKVSL VLAPALAACG CKVPMISGRS LGHTGGTLDK
160 170 180 190 200
LESIPGFSVT QSPEQMLQIL EEVGCCIVGQ SEKLVPADGI LYAARDVTAT
210 220 230 240 250
VDSVPLITAS ILSKKAVEGL STLVVDVKFG GAAVFPDQEK ARELAKMLVR
260 270 280 290 300
VGMGLGLQVA AALTAMDNPL GRNVGHTLEV EEALLCLDGA GPPDLRDLVI
310 320 330 340 350
RLGGAILWLS GQAETQDQGA ARVAAALDDG SALHRFQLML SAQGVDPGLA
360 370 380 390 400
RALCSGSPTQ RRQLLPHARK QEELLSPADG IVECVRALPL ACVLHELGAG
410 420 430 440 450
RSRAGQPIRP GVGAELLVDV GQWLSRGTPW LRVHLDGPAL SSQQRRTLLG
460 470
ALVLSDRAPF KAPSPFAELV LPPTTP
Length:476
Mass (Da):49,901
Last modified:March 1, 2005 - v1
Checksum:i1BB6068E2D94D24A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089830 mRNA. Translation: AAH89830.1.
RefSeqiNP_001012122.1. NM_001012122.1.
UniGeneiRn.219088.

Genome annotation databases

EnsembliENSRNOT00000040541; ENSRNOP00000039935; ENSRNOG00000032394.
GeneIDi315219.
KEGGirno:315219.

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.

Entry informationi

Entry nameiTYPH_RAT
AccessioniPrimary (citable) accession number: Q5FVR2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2005
Last modified: June 7, 2017
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families