CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1020 | Adenine-specific Methyltransferase; domain 2 |
|
1.10.1020.10 | Adenine-specific Methyltransferase, Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Adenine-specific Methyltransferase, Domain 2 |
| Functional Family | Site-specific DNA-methyltransferase (adenine-specific) |
Enzyme Information
| 2.1.1.72 |
Site-specific DNA-methyltransferase (adenine-specific).
based on mapping to UniProt P0AEE8
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.
-!- This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5). -!- See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
|
UniProtKB Entries (1)
| P0AEE8 |
DMA_ECOLI
Escherichia coli K-12
DNA adenine methylase
|
PDB Structure
| PDB | 2ORE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Two Alternative Conformations of S-Adenosyl-L-homocysteine Bound to Escherichia coli DNA Adenine Methyltransferase and the Implication of Conformational Changes in Regulating the Catalytic Cycle.
J.Biol.Chem.
|
