CATH Classification

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 1U8B
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada.
He, C., Hus, J.C., Sun, L.J., Zhou, P., Norman, D.P., Dotsch, V., Wei, H., Gross, J.D., Lane, W.S., Wagner, G., Verdine, G.L.
Mol.Cell