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    mutT 8-oxo-dGTP diphosphatase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944824, updated on 3-Dec-2024

    Summary

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    Official Symbol
    mutT
    Official Full Name
    8-oxo-dGTP diphosphatase
    Primary source
    ECOCYC:EG10626
    Locus tag
    b0099
    See related
    ASAP:ABE-0000346
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0100; nudA
    Summary
    Nudix hydrolase. [More information is available at EcoGene: EG10626]. dGTP pyrophosphohydrolase (MutT) can catalyze the hydrolysis of all eight canonical nucleotides, but it shows a marked preference for dGTP. [More information is available at EcoCyc: EG10626].
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    Genomic context

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    Sequence:
    NC_000913.3 (111044..111433)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene SecA translation regulator Neighboring gene protein translocation ATPase Neighboring gene DNA gyrase inhibitor YacG Neighboring gene cell division factor ZapD Neighboring gene dephospho-CoA kinase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Dual divalent cation requirement of the MutT dGTPase. Kinetic and magnetic resonance studies of the metal and substrate complexes. Frick DN, et al. J Biol Chem, 1994 Jan 21. PMID 8294428
    2. Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase. Harris TK, et al. Biochemistry, 2000 Feb 22. PMID 10677214
    3. Mut-Test to detect substances suppressing spontaneous mutation due to oxidative damage. Yonezawa Y, et al. Mutat Res, 2001 Jan 25. PMID 11152968
    4. Counteraction by MutT protein of transcriptional errors caused by oxidative damage. Taddei F, et al. Science, 1997 Oct 3. PMID 9311918
    5. An exchange of single amino acid between the phosphohydrolase modules of Escherichia coli MutT and Mycobacterium smegmatis MutT1 switches their cleavage specificities. Emam EAF, et al. DNA Repair (Amst), 2024 Jul. PMID 38776712

    See all (54) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. An exchange of single amino acid between the phosphohydrolase modules of Escherichia coli MutT and Mycobacterium smegmatis MutT1 switches their cleavage specificities.
      Title: An exchange of single amino acid between the phosphohydrolase modules of Escherichia coli MutT and Mycobacterium smegmatis MutT1 switches their cleavage specificities.
    2. Degradation of the Escherichia coli Essential Proteins DapB and Dxr Results in Oxidative Stress, which Contributes to Lethality through Incomplete Base Excision Repair.
      Title: Degradation of the Escherichia coli Essential Proteins DapB and Dxr Results in Oxidative Stress, which Contributes to Lethality through Incomplete Base Excision Repair.
    3. The study investigated the role of MutT on transcription fidelity and find no increase in epigenetic switch frequency in the absence of MutT function.
      Title: Removal of 8-oxo-GTP by MutT hydrolase is not a major contributor to transcriptional fidelity.
    4. MutT mutation increased the point-mutation rate 150-fold.
      Title: Mutation rate dynamics in a bacterial population reflect tension between adaptation and genetic load.
    5. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure.
      Title: Molecular actions of Escherichia coli MutT for control of spontaneous mutagenesis.
    6. The mutT defect does not elevate chromosomal fragmentation in Escherichia coli because of the surprisingly low levels of MutM/MutY-recognized DNA modifications.
      Title: The mutT defect does not elevate chromosomal fragmentation in Escherichia coli because of the surprisingly low levels of MutM/MutY-recognized DNA modifications.
    7. N-terminus verified by Edman degradation on complete protein
      Title: 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.
    8. MutT hydrolyzes four types of 8-oxoGua (8-oxo-7,8-dihydroguanine)-containing nucleoside diphosphates and triphosphates to the related monophosphates, thereby preventing misincorporation of 8-oxoGua into DNA and RNA.
      Title: Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools.
    9. These results indicate that mutT plays important roles in mutagenesis induced by 2-OH-dATP and 8-OH-dGTP in vivo.
      Title: Mutagenesis by damaged deoxyribonucleotides and its prevention by MutT-type hydrolyzing enzymes.
    10. transient state kinetic analysis of the reaction pathway of mutT; findings confirm an iso kinetic mechanism and explain the preferred hydrolysis of 8-oxo-dGTP
      Title: Transient state kinetic studies of the MutT-catalyzed nucleoside triphosphate pyrophosphohydrolase reaction.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 8-oxo-GDP phosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 8-oxo-GDP phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 8-oxo-GDP phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 8-oxo-dGDP phosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 8-oxo-dGDP phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 8-oxo-dGDP phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    NOT enables ATP diphosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables manganese ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within DNA repair EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in DNA repair IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in DNA repair IC
    Inferred by Curator
    more info
    		 PubMed 
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in dGDP catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in dGTP catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in nucleotide-excision repair IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    8-oxo-dGTP diphosphatase
    NP_414641.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      111044..111433
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414641.1 8-oxo-dGTP diphosphatase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414641.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6D0IYI2, A0A8T6BV79
      Conserved Domains (1) summary
      PRK10776
      Location:1 → 129
      PRK10776; 8-oxo-dGTP diphosphatase MutT
    Nucleotide Protein
    Heading Accession and Version

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