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Protein

Thymidine phosphorylase

Gene

deoA

Organism
Escherichia coli (strain SE11)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.UniRule annotation

Catalytic activityi

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

Pathway:idTMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes dTMP from thymine.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Thymidine phosphorylase (deoA)
  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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciECOL409438:GHUU-4760-MONOMER.
UniPathwayiUPA00578; UER00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine phosphorylaseUniRule annotation (EC:2.4.2.4UniRule annotation)
Alternative name(s):
TdRPaseUniRule annotation
Gene namesi
Name:deoAUniRule annotation
Ordered Locus Names:ECSE_4657
OrganismiEscherichia coli (strain SE11)
Taxonomic identifieri409438 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Thymidine phosphorylasePRO_1000186258Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB6I6M9.
SMRiB6I6M9. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiDWVVDAY.
OrthoDBiEOG61ZTGG.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPiMF_01628. Thymid_phosp.
InterProiIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR017872. Pyrmidine_PPase_CS.
IPR000053. Thymidine/pyrmidine_PPase.
IPR013465. Thymidine_Pase.
[Graphical view]
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B6I6M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD
60 70 80 90 100
MTMPERVSLT MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP
110 120 130 140 150
MVAACGGYIP MISGRGLGHT GGTLDKLESI PGFDIFPDDN RFREIIKDVG
160 170 180 190 200
VAIIGQTSSL APADKRFYAT RDITATVDSI PLITASILAK KLAEGLDALV
210 220 230 240 250
MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT DMNQVLASSA
260 270 280 290 300
GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL
310 320 330 340 350
QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF
360 370 380 390 400
VSEMDTRALG MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA
410 420 430 440
VIHAKDENSW QEAAKAVKAA IKLADKAPES TPTVYRRISE
Length:440
Mass (Da):47,180
Last modified:December 16, 2008 - v1
Checksum:iB3BDF83C9275D2F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG80181.1.
RefSeqiWP_000477811.1. NC_011415.1.

Genome annotation databases

EnsemblBacteriaiBAG80181; BAG80181; ECSE_4657.
KEGGiecy:ECSE_4657.
PATRICi18428066. VBIEscCol83070_4847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG80181.1.
RefSeqiWP_000477811.1. NC_011415.1.

3D structure databases

ProteinModelPortaliB6I6M9.
SMRiB6I6M9. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAG80181; BAG80181; ECSE_4657.
KEGGiecy:ECSE_4657.
PATRICi18428066. VBIEscCol83070_4847.

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiDWVVDAY.
OrthoDBiEOG61ZTGG.

Enzyme and pathway databases

UniPathwayiUPA00578; UER00638.
BioCyciECOL409438:GHUU-4760-MONOMER.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPiMF_01628. Thymid_phosp.
InterProiIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR017872. Pyrmidine_PPase_CS.
IPR000053. Thymidine/pyrmidine_PPase.
IPR013465. Thymidine_Pase.
[Graphical view]
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
    Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
    DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SE11.

Entry informationi

Entry nameiTYPH_ECOSE
AccessioniPrimary (citable) accession number: B6I6M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: July 22, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

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 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.