ung uracil-DNA glycosylase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: ung
Official Full Name: uracil-DNA glycosylase
Primary source: ECOCYC:EG11058
Locus tag: b2580
See related: ASAP:ABE-0008495
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: ECK2578
Summary: UDG and Ndk form a complex (Goswami, 2006). [More information is available at EcoGene: EG11058]. Uracil can be generated in DNA as a result of misincorporation by DNA polymerase, spontaneous deamination of cytosine, and deamination of cytosine induced by bisulfite or nitrous acid. [More information is available at EcoCyc: EG11058].
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Genomic context

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Sequence:: NC_000913.3 (2716754..2717443)

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

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
Title: In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
A mutant uracil DNA glycosylase distinguishes between cytosine and 5-methylcytosine.
Title: A mutant of uracil DNA glycosylase that distinguishes between cytosine and 5-methylcytosine.
Contrasting effects of mutating active site residues, aspartic acid 64 and histidine 187 of Escherichia coli uracil-DNA glycosylase on uracil excision and interaction with an inhibitor protein
Title: Contrasting effects of mutating active site residues, aspartic acid 64 and histidine 187 of Escherichia coli uracil-DNA glycosylase on uracil excision and interaction with an inhibitor protein.
oligonucleotide substrates containing two uracil residues in defined positions were used to characterize one-dimensional search of DNA by Escherichia coli Ung.
Title: Mechanism of translocation of uracil-DNA glycosylase from Escherichia coli between distributed lesions.
The significance of the Ung residency on the AP-site in the uracil excision repair pathway in E. coli.
Title: Analysis of the impact of a uracil DNA glycosylase attenuated in AP-DNA binding in maintenance of the genomic integrity in Escherichia coli.
for the human and Escherichia coli UNG enzymes, discrimination of thymine and uracil is initiated by thermally induced opening of T*A and U*A base pairs and not by active participation of the enzyme
Title: Enzymatic capture of an extrahelical thymine in the search for uracil in DNA.
N-terminus verified by Edman degradation on mature peptide
Title: Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase and its gene (ung).
influence of the ung, dug, and dut genes in preventing uracil residues from accumulating in E. coli DNA was quantitatively determined
Title: Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance.
A synthetic DNA duplex of uracil DNA glycosylase contains an excellent isostere of uracil but lacks hydrogen bonds and acceptor groups; it attains a metastable unstacked state that mimics a previously detected intermediate on the uracil-flipping pathway.
Title: Recognition of an unnatural difluorophenyl nucleotide by uracil DNA glycosylase.
The structure of native and modified uracil DNA glycosylase from E. coli in solution was studied by synchrotron small-angle X-ray scattering.
Title: [Structure of Escherichia coli uracil DNA glycosylase and its complexes with nonhydrolyzable substrate analogues in solution observed by synchrotron small-angle X-ray scattering].

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables uracil DNA N-glycosylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables uracil DNA N-glycosylase activity	IDA Inferred from Direct Assay more info	PubMed
enables uracil 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	IEA Inferred from Electronic Annotation more info
involved_in base-excision repair, AP site formation via deaminated base removal	IBA Inferred from Biological aspect of Ancestor more info
involved_in base-excision repair, AP site formation via deaminated base removal	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: uracil-DNA glycosylase

NP_417075.1

EC 3.2.2.27

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

2716754..2717443

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417075.1 uracil-DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417075.1

Status: PROVISIONAL

UniProtKB/Swiss-Prot

Q8FF08

UniProtKB/TrEMBL

A0A2X1N865, A0A5B9APQ3, A0A6C9QIE5

Conserved Domains (2) summary

PRK05254
Location:4 → 220

PRK05254; uracil-DNA glycosylase; Provisional

cd10027
Location:62 → 66

UDG-F1-like; motif A [structural motif]