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
- Functionsphosphorylase activity / pyrimidine-nucleoside phosphorylase activity / thymidine phosphorylase activityProcessescellular response to DNA damage stimulus / pyrimidine nucleobase metabolic process / thymidine metabolic processComponentscytosol / 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
Resource Link UniProtKB ID P07650 UniProtKB Entry Name TYPH_ECOLI GenBank Protein ID 537222 GenBank Gene ID U14003 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]