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
- Functions8-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 bindingProcessesDNA 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
- NUDIX (PF00293)
- 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
Resource Link UniProtKB ID P08337 UniProtKB Entry Name MUTT_ECOLI GenBank Protein ID 42071 GenBank Gene ID X04831 - General References
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- 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]
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- 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]
- 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]
- 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]
- Maki H, Sekiguchi M: MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature. 1992 Jan 16;355(6357):273-5. [Article]
- 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]
- 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]
- 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]
- 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]