mutY adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: mutY
Official Full Name: adenine DNA glycosylase
Primary source: ECOCYC:EG10627
Locus tag: b2961
See related: ASAP:ABE-0009720
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: ECK2956; micA
Summary: MutY serves as an adenine glycosylase mismatch repair enzyme in Escherichia coli which works to correct G-A mispairs to G-C base pairs. [More information is available at EcoCyc: EG10627].
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Genomic context

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Sequence:: NC_000913.3 (3103013..3104065)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
Studies indicate that the DNA repair gene MUTYH, which is a homologue of the E. coli gene mutY, is responsible for colorectal carcinoma (CRC).
Title: E. coli and colon cancer: is mutY a culprit?
MutY mutations reduced the point-mutation rate by 40-60%.
Title: Mutation rate dynamics in a bacterial population reflect tension between adaptation and genetic load.
ability of MUTYH and the variants to suppress mutations and complement for the absence of MutY in Escherichia coli was assessed using rifampicin resistance assays.
Title: Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.
V45A and Q182L mutants had reduced binding for A/G and A/8-oxoG mismatches and increased affinities towards T/G mismatch.
Title: Insights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity.
HPs and SSAs are a common finding in MAP patients. The detection of almost exclusively G:C-->T:A transversions in the K-ras gene of HPs/SSAs strongly suggests that these polyps are related causally to MYH deficiency.
Title: Hyperplastic polyps and sessile serrated adenomas as a phenotypic expression of MYH-associated polyposis.
Data show a lack of interaction of mutY with dnaX36 since the double dnaX36 mutY strains did not show any major changes in the frequency of G.CT.A transversions compared to the single dnaX36 strain.
Title: Role of accessory DNA polymerases in DNA replication in Escherichia coli: analysis of the dnaX36 mutator mutant.
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.
Mutant MutY(Delta26-134), which lacks the six-helix barrel domain, cannot complement the mutator phenotype of a mutY mutant in vivo. However, the mutant can still bind DNA and has weak catalytic activity at high enzyme concentrations.
Title: An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA.
catalytic analysis of Escherichia coli MutY DNA glycosylase
Title: Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 4 iron, 4 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables DNA N-glycosylase activity	IEA Inferred from Electronic Annotation more info
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables adenine/guanine mispair binding	IBA Inferred from Biological aspect of Ancestor more info
enables hydrolase activity, acting on glycosyl bonds	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidized purine DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables purine-specific mismatch base pair DNA N-glycosylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables purine-specific mismatch base pair DNA N-glycosylase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in base-excision repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in base-excision repair	IEA Inferred from Electronic Annotation more info
involved_in mismatch repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to stress	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: adenine DNA glycosylase

NP_417436.1

EC 3.2.2.31

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

NC_000913.3 Reference assembly

Range

3103013..3104065

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417436.1 adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417436.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A6C9Q9V6

Conserved Domains (1) summary

PRK10880
Location:1 → 350

PRK10880; adenine DNA glycosylase