CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.190 | N-terminal domain of MutM-like DNA repair proteins |
|
3.20.190.10 | MutM-like, N-terminal |
Domain Context
CATH Clusters
| Superfamily | MutM-like, N-terminal |
| Functional Family | Putative Formamidopyrimidine-DNA glycosylase |
Enzyme Information
| 4.2.99.18 |
DNA-(apurinic or apyrimidinic site) lyase.
based on mapping to UniProt O80358
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
-!- 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. -!- This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.
|
| 3.2.2.23 |
DNA-formamidopyrimidine glycosylase.
based on mapping to UniProt O80358
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
-!- May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. -!- Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
|
UniProtKB Entries (1)
| O80358 |
FPG_ARATH
Arabidopsis thaliana
Formamidopyrimidine-DNA glycosylase
|
PDB Structure
| PDB | 3TWK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.
Dna Repair
|
