EzCatDB: D00079
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DB codeD00079
RLCP classification3.747.6300.267 : Transfer
CATH domainDomain 13.40.50.150 : Rossmann foldCatalytic domain
Domain 21.10.1020.10 : Adenine-specific Methyltransferase; domain 2
E.C.2.1.1.72

CATH domainRelated DB codes (homologues)
3.40.50.150 : Rossmann foldS00637,S00639,S00262,S00261,S00291,S00412,D00075,D00076,D00080,D00082,D00083,D00823

Enzyme Name
UniProtKBKEGG

P04043
Protein nameModification methylase DpnIIAsite-specific DNA-methyltransferase (adenine-specific)
modification methylase
restriction-modification system
SynonymsM.DpnIIA
EC 2.1.1.72
Adenine-specific methyltransferase DpnIIA
M.DpnII 1
PfamPF02086 (MethyltransfD12)
[Graphical view]


UniProtKB:Accession NumberP04043
Entry nameMTD21_STRPN
ActivityS-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00019C00821C00021C03391
CompoundS-Adenosyl-L-methionineDNA adenineS-Adenosyl-L-homocysteineDNA 6-methylaminopurine
Typeamino acids,amine group,nucleoside,sulfonium ionamine group,nucleic acidsamino acids,amine group,nucleoside,sulfide groupamine group,nucleic acids
ChEBI67040

16680
57856

PubChem34755

439155
25246222

            
2dpmA01Bound:SAMUnboundUnboundUnbound
2dpmA02UnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residues
         
2dpmA01ASP 194
2dpmA02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.1572-1573

references
[1]
PubMed ID9862809
JournalStructure
Year1998
Volume6
Pages1563-75
AuthorsTran PH, Korszun ZR, Cerritelli S, Springhorn SS, Lacks SA
TitleCrystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.
Related PDB2dpm
Related UniProtKBP04043

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.

createdupdated
2002-08-142009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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