DB code: D00079

RLCP classification 3.747.6300.267 : Transfer
CATH domain 3.40.50.150 : Rossmann fold Catalytic domain
1.10.1020.10 : Adenine-specific Methyltransferase; domain 2
E.C. 2.1.1.72
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.150 : Rossmann fold S00637 S00639 S00262 S00261 S00291 S00412 D00075 D00076 D00080 D00082 D00083 D00823

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P04043 Modification methylase DpnIIA
M.DpnIIA
EC 2.1.1.72
Adenine-specific methyltransferase DpnIIA
M.DpnII 1
PF02086 (MethyltransfD12)
[Graphical View]

KEGG enzyme name
site-specific DNA-methyltransferase (adenine-specific)
modification methylase
restriction-modification system

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04043 MTD21_STRPN S-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine. Homodimer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00019 C00821 C00021 C03391
E.C.
Compound S-Adenosyl-L-methionine DNA adenine S-Adenosyl-L-homocysteine DNA 6-methylaminopurine
Type amino acids,amine group,nucleoside,sulfonium ion amine group,nucleic acids amino acids,amine group,nucleoside,sulfide group amine group,nucleic acids
ChEBI 67040
67040
16680
57856
16680
57856
PubChem 34755
34755
25246222
439155
25246222
439155
2dpmA01 Bound:SAM Unbound Unbound Unbound
2dpmA02 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2dpmA01 ASP 194
2dpmA02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.1572-1573

References
[1]
Resource
Comments
Medline ID
PubMed ID 9862809
Journal Structure
Year 1998
Volume 6
Pages 1563-75
Authors Tran PH, Korszun ZR, Cerritelli S, Springhorn SS, Lacks SA
Title Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.
Related PDB 2dpm
Related UniProtKB P04043

Comments
This methylase recognizes the double-stranded sequence [G-A-T-C], causes specific methylation on A-2, and protects the DNA from cleavage by the DpnII endonuclease.
According to the literature [1], the catalysis of methyl transfer directly to adenine N6 is presumably mediated by the negative polarization of N6 by hydrogen bonding to Asp194 and Pro195.

Created Updated
2002-08-14 2009-02-26