CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.470 | Uracil-DNA Glycosylase, subunit E |
|
3.40.470.10 | Uracil-DNA glycosylase-like domain |
Domain Context
CATH Clusters
| Superfamily | Uracil-DNA glycosylase-like domain |
| Functional Family |
Enzyme Information
| 3.2.2.27 |
Uracil-DNA glycosylase.
based on mapping to UniProt P12888
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 (2)
| P12888 |
UNG_EBVB9
Human herpesvirus 4 strain B95-8
Uracil-DNA glycosylase
|
| P14739 |
UNGI_BPPB2
Bacillus phage PBS2
Uracil-DNA glycosylase inhibitor
|
PDB Structure
| PDB | 2J8X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
New Insights on the Role of the Gamma-Herpesvirus Uracil-DNA Glycosylase Leucine Loop Revealed by the Structure of the Epstein-Barr Virus Enzyme in Complex with an Inhibitor Protein.
J.Mol.Biol.
|