Thymidine phosphorylase

Details

Name
Thymidine phosphorylase
Synonyms
  • 2.4.2.4
  • TdRPase
  • tpp
  • ttg
Gene Name
deoA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020583|Thymidine phosphorylase
MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLT
MAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHT
GGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSI
PLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLT
DMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKL
QAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALG
MAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAA
IKLADKAPESTPTVYRRISE
Number of residues
440
Molecular Weight
47206.655
Theoretical pI
5.0
GO Classification
Functions
phosphorylase activity / pyrimidine-nucleoside phosphorylase activity / thymidine phosphorylase activity
Processes
cellular response to DNA damage stimulus / pyrimidine nucleobase metabolic process / thymidine metabolic process
Components
cytosol / membrane
General Function
Thymidine phosphorylase activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020584|Thymidine phosphorylase (deoA)
TTGTTTCTCGCACAAGAAATTATTCGTAAAAAACGTGATGGTCATGCGCTGAGCGATGAA
GAAATTCGTTTCTTTATCAACGGTATTCGCGACAACACTATCTCCGAAGGGCAGATTGCC
GCCCTCGCGATGACCATTTTCTTCCACGATATGACAATGCCTGAGCGTGTCTCGCTGACC
ATGGCGATGCGAGATTCAGGAACCGTTCTCGACTGGAAAAGCCTGCATCTGAATGGCCCG
ATTGTTGATAAACACTCCACCGGTGGCGTCGGCGATGTGACTTCGCTGATGTTGGGGCCG
ATGGTCGCAGCCTGCGGCGGCTATATTCCGATGATCTCTGGTCGCGGCCTCGGTCATACT
GGCGGTACGCTCGACAAACTGGAATCCATCCCTGGCTTCGACATTTTCCCGGATGACAAC
CGTTTCCGCGAAATTATTAAAGACGTCGGCGTGGCGATTATCGGTCAGACCAGTTCACTG
GCTCCGGCTGATAAACGTTTCTACGCGACCCGTGATATTACCGCAACCGTGGACTCCATC
CCGCTGATCACCGCCTCTATTCTGGCGAAGAAACTTGCGGAAGGTCTGGACGCGCTGGTG
ATGGACGTGAAAGTGGGTAGCGGCGCGTTTATGCCGACCTACGAACTCTCTGAAGCCCTT
GCCGAAGCGATTGTTGGCGTGGCTAACGGCGCTGGCGTGCGCACCACCGCGCTGCTCACC
GACATGAATCAGGTACTGGCCTCCAGTGCAGGTAACGCGGTTGAAGTTCGTGAAGCGGTG
CAGTTCCTGACGGGTGAATATCGTAACCCGCGTCTGTTTGATGTCACGATGGCGCTGTGC
GTGGAGATGCTGATCTCCGGCAAACTGGCGAAAGATGACGCCGAAGCGCGCGCGAAATTG
CAGGCGGTGCTGGACAACGGTAAAGCGGCAGAAGTCTTTGGTCGTATGGTAGCGGCACAA
AAAGGCCCGACCGACTTCGTTGAGAACTACGCGAAGTATCTGCCGACAGCGATGCTGACG
AAAGCAGTCTATGCTGATACCGAAGGTTTTGTCAGTGAAATGGATACCCGCGCGCTGGGG
ATGGCAGTGGTTGCAATGGGCGGCGGACGCCGTCAGGCATCTGACACCATCGATTACAGC
GTCGGCTTTACTGATATGGCGCGTCTGGGCGACCAGGTAGACGGTCAGCGTCCGCTGGCG
GTTATCCACGCGAAAGACGAAAACAACTGGCAGGAAGCGGCGAAAGCGGTGAAAGCGGCA
ATTAAACTTGCCGATAAAGCACCGGAAAGCACACCAACTGTCTATCGCCGTATCAGCGAA
TAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP07650
UniProtKB Entry NameTYPH_ECOLI
GenBank Protein ID537222
GenBank Gene IDU14003
General References
  1. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Valentin-Hansen P, Hammer K, Love Larsen JE, Svendsen I: The internal regulated promoter of the deo operon of Escherichia coli K-12. Nucleic Acids Res. 1984 Jul 11;12(13):5211-24. [Article]
  5. Valentin-Hansen P, Hammer-Jespersen K, Boetius F, Svendsen I: Structure and function of the intercistronic regulatory deoC-deoA element of Escherichia coli K-12. EMBO J. 1984 Jan;3(1):179-83. [Article]
  6. Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE: Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. J Biol Chem. 1990 Aug 15;265(23):14016-22. [Article]
  7. Pugmire MJ, Cook WJ, Jasanoff A, Walter MR, Ealick SE: Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J Mol Biol. 1998 Aug 14;281(2):285-99. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03462ThymineexperimentalunknownDetails