Identification
Name:Mutator mutT protein
Synonyms:
  • 7,8-dihydro-8-oxoguanine-triphosphatase
  • 8-oxo-dGTPase
  • dGTP pyrophosphohydrolase
Gene Name:mutT
Enzyme Class:
Biological Properties
General Function:Replication, recombination and repair
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
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.08-oxo-dGTP+1.0Thumb1.0Thumb+1.08-oxo-dGMP+1.0Thumb
1.08-oxo-dGTP + 1.0Water → 1.0Hydrogen ion + 1.08-oxo-dGMP + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB010442'-Deoxyguanosine 5'-monophosphateMetaboCard
ECMDB232348-oxo-dGMPMetaboCard
ECMDB232338-oxo-dGTPMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB21206Dihydroneopterin monophosphateMetaboCard
ECMDB01144Dihydroneopterin triphosphateMetaboCard
ECMDB01397Guanosine monophosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleoside-triphosphate diphosphatase activity
pyrophosphatase activity
Process
cellular macromolecule metabolic process
DNA metabolic process
DNA repair
macromolecule metabolic process
metabolic process
Gene Properties
Blattner:b0099
Gene OrientationClockwise
Centisome Percentage:2.39
Left Sequence End111044
Right Sequence End111433
Gene Sequence:
>390 bp
ATGAAAAAGCTGCAAATTGCGGTAGGTATTATTCGCAACGAGAACAATGAAATCTTTATA
ACGCGTCGCGCAGCAGATGCGCACATGGCGAATAAACTGGAGTTTCCCGGCGGTAAAATT
GAAATGGGTGAAACGCCGGAACAGGCGGTGGTGCGTGAACTTCAGGAAGAAGTCGGGATT
ACCCCCCAACATTTTTCGCTATTTGAAAAACTGGAATATGAATTCCCGGACAGGCATATA
ACACTGTGGTTTTGGCTGGTCGAACGCTGGGAAGGGGAGCCGTGGGGTAAAGAAGGGCAA
CCCGGTGAGTGGATGTCGCTGGTCGGTCTTAATGCCGATGATTTTCCGCCAGCCAATGAA
CCGGTAATTGCGAAGCTTAAACGTCTGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:129
Protein Molecular Weight:14927
Protein Theoretical pI:5
PDB File:1PUS
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Mutator mutT protein
MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGI
TPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANE
PVIAKLKRL
References
External Links:
ResourceLink
Uniprot ID:P08337
Uniprot Name:MUTT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321980
PDB ID:1PUS
Ecogene ID:EG10626
Ecocyc:EG10626
ColiBase:b0099
Kegg Gene:b0099
EchoBASE ID:EB0621
CCDB:MUTT_ECOLI
BacMap:16128092
General Reference:
  • Abeygunawardana, C., Weber, D. J., Gittis, A. G., Frick, D. N., Lin, J., Miller, A. F., Bessman, M. J., Mildvan, A. S. (1995). "Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase." Biochemistry 34:14997-15005. Pubmed: 7578113
  • Akiyama, M., Horiuchi, T., Sekiguchi, M. (1987). "Molecular cloning and nucleotide sequence of the mutT mutator of Escherichia coli that causes A:T to C:G transversion." Mol Gen Genet 206:9-16. Pubmed: 3033442
  • Bhatnagar, S. K., Bessman, M. J. (1988). "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 263:8953-8957. Pubmed: 3288626
  • Bhatnagar, S. K., Bullions, L. C., Bessman, M. J. (1991). "Characterization of the mutT nucleoside triphosphatase of Escherichia coli." J Biol Chem 266:9050-9054. Pubmed: 1851162
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Lin, J., Abeygunawardana, C., Frick, D. N., Bessman, M. J., Mildvan, A. S. (1997). "Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action." Biochemistry 36:1199-1211. Pubmed: 9063868
  • Maki, H., Sekiguchi, M. (1992). "MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis." Nature 355:273-275. Pubmed: 1309939
  • 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. (2010). "Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base." J Biol Chem 285:444-452. Pubmed: 19864691
  • Schmidt, M. G., Rollo, E. E., Grodberg, J., Oliver, D. B. (1988). "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli." J Bacteriol 170:3404-3414. Pubmed: 2841285
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901