CATH Classification

Domain Context

CATH Clusters

Superfamily Uracil-DNA glycosylase-like domain
Functional Family G/U mismatch-specific DNA glycosylase

Enzyme Information
Double-stranded uracil-DNA glycosylase.
based on mapping to UniProt P0A9H1
Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil.
-!- No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N(4)-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing Escherichia coli. -!- Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. -!- Uracil-DNA glycosylase (EC and double-stranded uracil-DNA glycosylase (EC form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA.

UniProtKB Entries (1)

Escherichia coli K-12
G/U mismatch-specific DNA glycosylase

PDB Structure

External Links
Organism Escherichia
Primary Citation
Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct.
Barrett, T.E., Savva, R., Barlow, T., Brown, T., Jiricny, J., Pearl, L.H.