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A1UY21 (TYPH_BURMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:BMASAVP1_1276
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length440 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 caution

The sequence ABM49234.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Thymidine phosphorylase HAMAP-Rule MF_01628
PRO_0000335772

Sequences

Sequence LengthMass (Da)Tools
A1UY21 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: DDC26DDD6E433A42

FASTA44045,403
        10         20         30         40         50         60 
MTFLPQEFIR KVRDRAPLDT ADVARFVQGV TAGDVTEGQI AAFAMAVYFN ELPLSARIAL 

        70         80         90        100        110        120 
TLAQRDSGDV LDWRGARLNG PVVDKHSTGG VGDLTSLVIG PMVAACGGYV PMISGRGLGH 

       130        140        150        160        170        180 
TGGTLDKLEA IPGYDVAPSV DMLRRVVRDA GLAIVGQTAQ LAPADKRIYA VRDVTATVES 

       190        200        210        220        230        240 
ISLITASILS KKLAAGVGAL AMDVKVGSGA FMPSAEQSAE LARSIVDVGN GAGMRTAATL 

       250        260        270        280        290        300 
TDMNQALAPC AGNAIEVRCA IDFLTGAARP ARLEAVSFAL AAQMLTMGGL AADAHDARRR 

       310        320        330        340        350        360 
LRAVLESGAA AERFARMVAA LGGPADLVER PERHLPRAAA AAPVAAARAG WIERIDARAL 

       370        380        390        400        410        420 
GLAVVGLGGG RAKIGDTLDY SVGLSALAEL GERVEAGQPL ATVHARDADS AAQATDAVRR 

       430        440 
AYRIGAEPPA QTRVVHAVIE 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SAVP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000525 Genomic DNA. Translation: ABM49234.1. Different initiation.
RefSeqYP_990874.1. NC_008784.1.

3D structure databases

ProteinModelPortalA1UY21.
SMRA1UY21. Positions 3-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320388.BMASAVP1_1276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM49234; ABM49234; BMASAVP1_1276.
GeneID4678192.
KEGGbmv:BMASAVP1_1276.
PATRIC19151844. VBIBurMal134057_1201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000047313.
KOK00758.
OrthoDBEOG61ZTGG.

Enzyme and pathway databases

BioCycBMAL320388:GHFL-4807-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_BURMS
AccessionPrimary (citable) accession number: A1UY21
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 52 of the entry and version 2 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