CATH Classification

Domain Context

CATH Clusters

Superfamily Uracil-DNA glycosylase-like domain
Functional Family Uracil DNA glycosylase

Enzyme Information

3.2.2.27
Uracil-DNA glycosylase.
based on mapping to UniProt P20536
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
-!- 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)

P20536
UNG_VACCC
Vaccinia virus Copenhagen
Uracil-DNA glycosylase

PDB Structure

PDB 4OD8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit d4 in complex with the a20 N-terminal domain.
Contesto-Richefeu, C., Tarbouriech, N., Brazzolotto, X., Betzi, S., Morelli, X., Burmeister, W.P., Iseni, F.
Plos Pathog.