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Protein

Thymidine phosphorylase

Gene

deoA

Organism
Shewanella sediminis (strain HAW-EB3)
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

Pathwayi

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. pyrimidine-nucleoside phosphorylase activity Source: InterPro
  3. thymidine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyrimidine nucleobase metabolic process Source: InterPro
  2. thymidine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciSSED425104:GH7Q-3495-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:Ssed_3377
OrganismiShewanella sediminis (strain HAW-EB3)
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002015: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Thymidine phosphorylasePRO_1000088112Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi425104.Ssed_3377.

Structurei

3D structure databases

ProteinModelPortaliA8FYQ8.
SMRiA8FYQ8. 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.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
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.

A8FYQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLAQEIIRK KRNAEALSKE EIQFFVKGIT DNTVSEGQIA ALGMAVYFND
60 70 80 90 100
MNMDERIALT TSMRDSGTVL NWKSLDLDGP IIDKHSTGGV GDVISLMLGP
110 120 130 140 150
MAAACGGYVP MISGRGLGHT GGTLDKFDAI PGYQTEPDSA LFRKVVKEAG
160 170 180 190 200
VAIIGQTGDL VPADKRFYSI RDNTATVESI SLITASILSK KLAAGLDALA
210 220 230 240 250
MDVKVGSGAF MPTYEASEEL ARSITAVANG AGTKTTALLT DMNQVLASCA
260 270 280 290 300
GNAVEVKEAV DFLTGAYRNP RLYEVTMGLC AEMLQLGGIA SSEAEAREKL
310 320 330 340 350
NRVLDNGKAA EIFGRMISGL GGPADFIENT GLYLPESKII RPVYADQTGF
360 370 380 390 400
ASAMDTRELG LAVVTLGGGR RKPGDALDYS VGLTKVCALG DEISADKPIA
410 420 430 440
FIHAQTENAF AEAEAAVKKA IHVGETKPEK TPEIYRYIRE SDL
Length:443
Mass (Da):47,054
Last modified:November 13, 2007 - v1
Checksum:iB6520E5707EEF0CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37981.1.
RefSeqiWP_012143711.1. NC_009831.1.
YP_001475109.1. NC_009831.1.

Genome annotation databases

EnsemblBacteriaiABV37981; ABV37981; Ssed_3377.
GeneIDi5609955.
KEGGisse:Ssed_3377.
PATRICi23564544. VBISheSed62411_3588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37981.1.
RefSeqiWP_012143711.1. NC_009831.1.
YP_001475109.1. NC_009831.1.

3D structure databases

ProteinModelPortaliA8FYQ8.
SMRiA8FYQ8. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi425104.Ssed_3377.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV37981; ABV37981; Ssed_3377.
GeneIDi5609955.
KEGGisse:Ssed_3377.
PATRICi23564544. VBISheSed62411_3588.

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiDWVVDAY.
OrthoDBiEOG61ZTGG.

Enzyme and pathway databases

UniPathwayiUPA00578; UER00638.
BioCyciSSED425104:GH7Q-3495-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.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HAW-EB3.

Entry informationi

Entry nameiTYPH_SHESH
AccessioniPrimary (citable) accession number: A8FYQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: February 4, 2015
This is version 54 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.