CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

3.2.2.28
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 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) 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)

P0A9H1
MUG_ECOLI
Escherichia coli K-12
G/U mismatch-specific DNA glycosylase

PDB Structure

PDB 1MWJ
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal Structure of a thwarted mismatch glycosylase DNA repair complex
Barrett, T.E., Scharer, O., Savva, R., Brown, T., Jiricny, J., Verdine, G.L., Pearl, L.H.
Embo J.