8-oxo-dGTP diphosphatase

Details

Name
8-oxo-dGTP diphosphatase
Synonyms
  • 3.6.1.55
  • 7,8-dihydro-8-oxoguanine-triphosphatase
  • 8-oxo-dGTPase
  • dGTP pyrophosphohydrolase
  • Mutator protein MutT
Gene Name
mutT
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020547|8-oxo-dGTP diphosphatase
MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGI
TPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANE
PVIAKLKRL
Number of residues
129
Molecular Weight
14926.99
Theoretical pI
4.72
GO Classification
Functions
8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / 8-oxo-dGDP phosphatase activity / 8-oxo-GDP phosphatase activity / magnesium ion binding / manganese ion binding
Processes
DNA repair / DNA replication
General Function
Manganese ion binding
Specific Function
Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0020548|8-oxo-dGTP diphosphatase (mutT)
ATGAAAAAGCTGCAAATTGCGGTAGGTATTATTCGCAACGAGAACAATGAAATCTTTATA
ACGCGTCGCGCAGCAGATGCGCACATGGCGAATAAACTGGAGTTTCCCGGCGGTAAAATT
GAAATGGGTGAAACGCCGGAACAGGCGGTGGTGCGTGAACTTCAGGAAGAAGTCGGGATT
ACCCCCCAACATTTTTCGCTATTTGAAAAACTGGAATATGAATTCCCGGACAGGCATATA
ACACTGTGGTTTTGGCTGGTCGAACGCTGGGAAGGGGAGCCGTGGGGTAAAGAAGGGCAA
CCCGGTGAGTGGATGTCGCTGGTCGGTCTTAATGCCGATGATTTTCCGCCAGCCAATGAA
CCGGTAATTGCGAAGCTTAAACGTCTGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP08337
UniProtKB Entry NameMUTT_ECOLI
GenBank Protein ID42071
GenBank Gene IDX04831
General References
  1. Akiyama M, Horiuchi T, Sekiguchi M: Molecular cloning and nucleotide sequence of the mutT mutator of Escherichia coli that causes A:T to C:G transversion. Mol Gen Genet. 1987 Jan;206(1):9-16. [Article]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
  3. 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]
  4. 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]
  5. Schmidt MG, Rollo EE, Grodberg J, Oliver DB: Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli. J Bacteriol. 1988 Aug;170(8):3404-14. [Article]
  6. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
  7. Bhatnagar SK, Bessman MJ: Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase. J Biol Chem. 1988 Jun 25;263(18):8953-7. [Article]
  8. Bhatnagar SK, Bullions LC, Bessman MJ: Characterization of the mutT nucleoside triphosphatase of Escherichia coli. J Biol Chem. 1991 May 15;266(14):9050-4. [Article]
  9. Maki H, Sekiguchi M: MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature. 1992 Jan 16;355(6357):273-5. [Article]
  10. Ito R, Hayakawa H, Sekiguchi M, Ishibashi T: Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools. Biochemistry. 2005 May 3;44(17):6670-4. [Article]
  11. Abeygunawardana C, Weber DJ, Gittis AG, Frick DN, Lin J, Miller AF, Bessman MJ, Mildvan AS: Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase. Biochemistry. 1995 Nov 21;34(46):14997-5005. [Article]
  12. Lin J, Abeygunawardana C, Frick DN, Bessman MJ, Mildvan AS: Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action. Biochemistry. 1997 Feb 11;36(6):1199-211. [Article]
  13. Nakamura T, Meshitsuka S, Kitagawa S, Abe N, Yamada J, Ishino T, Nakano H, Tsuzuki T, Doi T, Kobayashi Y, Fujii S, Sekiguchi M, Yamagata Y: Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base. J Biol Chem. 2010 Jan 1;285(1):444-52. doi: 10.1074/jbc.M109.066373. Epub 2009 Oct 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB020238-oxo-dGMPexperimentalunknownDetails