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Q5QXT8 (TYPH_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine phosphorylase

EC=2.4.2.4
Alternative name(s):
TdRPase
Gene names
Name:deoA
Ordered Locus Names:IL1882
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01628

Catalytic activity

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01628

Pathway

Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. HAMAP-Rule MF_01628

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01628

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Thymidine phosphorylase HAMAP-Rule MF_01628
PRO_0000059057

Sequences

Sequence LengthMass (Da)Tools
Q5QXT8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 455514E5C219023A

FASTA44647,392
        10         20         30         40         50         60 
MFLAQEVIRK KRDAVSLSDT DIQQFVNGIC DDSVSEGQIA ALAMAIYFRG MSAQEKTALT 

        70         80         90        100        110        120 
VAMRDSGDVL DWRQDNLNGP VLDKHSTGGV GDVVSLMLGP IVAACGGYVP MISGRGLGHT 

       130        140        150        160        170        180 
GGTLDKFDAI PGYQTAPDNR RFRDTVKQAG VAIIGQTGRL APADSRFYAT RDVTATVESI 

       190        200        210        220        230        240 
PLITASILAK KLAEGLDGLV MDVKAGNGAF MPGYDESREL AQSLVSVGRK LGVETTALIT 

       250        260        270        280        290        300 
DMNQALGSAA GNAVEVQLAV DYLTGKRRDK RLHQVTKALS AELLVSGNLA KSTDQAEVMV 

       310        320        330        340        350        360 
ENVLGSGLAA ERFAKMVGSL GGPHDFLEKS DQYLPQANLR KPLKLPAEYH GLYLSEVNTR 

       370        380        390        400        410        420 
ELGMAVVCLG GGRRKADDKL DLSVGMTDIL TVGSKVDSES VIATVHASNE SDWQEAADSI 

       430        440 
LKALSFSSTP PEPDSVIYER IAGETE 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82714.1.
RefSeqYP_156263.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXT8.
SMRQ5QXT8. Positions 1-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82714; AAV82714; IL1882.
GeneID3173985.
KEGGilo:IL1882.
PATRIC22141884. VBIIdiLoi21852_1891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000047313.
KOK00758.
OMACGLAVPM.
OrthoDBEOG61ZTGG.
ProtClustDBPRK05820.

Enzyme and pathway databases

BioCycILOI283942:GI0U-1892-MONOMER.
UniPathwayUPA00578; UER00638.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_01628. Thymid_phosp.
InterProIPR000312. 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]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYPH_IDILO
AccessionPrimary (citable) accession number: Q5QXT8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways