CATH Domain 1wpkA01

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	1WPK
External Links	PDBSum Proteopedia
Method	SOLUTION NMR
Organism	Escherichia
Primary Citation	The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein Takinowaki, H., Matsuda, Y., Yoshida, T., Kobayashi, Y., Ohkubo, T. Protein Sci.