CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.10 | DNA Methylphosphotriester Repair Domain |
|
3.40.10.10 | DNA Methylphosphotriester Repair Domain |
Domain Context
CATH Clusters
| Superfamily | DNA Methylphosphotriester Repair Domain |
| Functional Family | DNA-3-methyladenine glycosylase 2 |
Enzyme Information
| 2.1.1.63 |
Methylated-DNA--[protein]-cysteine S-methyltransferase.
based on mapping to UniProt P06134
(1) DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine. (2) DNA (containing 4-O-methylthymine) + protein L-cysteine = DNA (without 4-O-methylthymine) + protein S-methyl-L-cysteine.
-!- This protein is involved in the repair of methylated DNA. -!- Unlike EC 3.2.2.20 and EC 3.2.2.21, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. -!- Since the methyl transfer is irreversible, the enzyme can only catalyze a single turnover.
|
| 2.1.1.n11 |
Methylphosphotriester-DNA--[protein]-cysteine S-methyltransferase.
based on mapping to UniProt P06134
DNA (containing Sp-methylphosphotriester) + protein L-cysteine = DNA (without Sp-methylphosphotriester) + protein S-methyl-L-cysteine.
-!- This protein is involved in the repair of Sp diastereomers of DNA methylphosphotriester lesions. -!- This enzyme catalyzes only one turnover and therefore is not strictly catalytic. -!- The enzyme from the bacterium Escherichia coli also has the activity of EC 2.1.1.63 while the enzyme from Bacillus subtilis does not.
|
UniProtKB Entries (1)
| P06134 |
ADA_ECOLI
Escherichia coli K-12
Bifunctional transcriptional activator/DNA repair enzyme Ada
|
PDB Structure
| PDB | 1ADN |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada.
Biochemistry
|
