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 | 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 | 1MWI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions.
Cell(Cambridge,Mass.)
|
