EzCatDB: S00261
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DB codeS00261
RLCP classification3.747.6300.267 : Transfer
CATH domainDomain 13.40.50.150 : Rossmann foldCatalytic domain
E.C.2.1.1.72

CATH domainRelated DB codes (homologues)
3.40.50.150 : Rossmann foldS00637,S00639,S00262,S00291,S00412,D00075,D00076,D00079,D00080,D00082,D00083,D00823

Enzyme Name
UniProtKBKEGG

P14751P23192
Protein nameModification methylase RsrIModification methylase MboIIsite-specific DNA-methyltransferase (adenine-specific)
modification methylase
restriction-modification system
SynonymsM.RsrI
EC 2.1.1.72
Adenine-specific methyltransferase RsrI
M.MboII
EC 2.1.1.72
Adenine-specific methyltransferase MboII
DNA MTase MboIIA
PfamPF01555 (N6_N4_Mtase)
[Graphical view]
PF01555 (N6_N4_Mtase)
[Graphical view]


UniProtKB:Accession NumberP14751P23192
Entry nameMTR1_RHOSHMTM2_MORBO
ActivityS-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine.S-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine.
Subunit
Homodimer.
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

25246222
439155

            
1eg2AAnalogue:MTAUnboundUnboundUnbound
1g60ABound:SAMUnboundUnboundUnbound
1g60BBound:SAMUnboundUnboundUnbound

Active-site residues
resource
literature [2]
pdbCatalytic residues
         
1eg2AASP 65
1g60AASP 30
1g60BASP 30

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.11

references
[1]
PubMed ID1511884
JournalGene
Year1992
Volume118
Pages5-11
AuthorsKaszubska W, Webb HK, Gumport RI
TitlePurification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli.
[2]
PubMed ID11024175
JournalNucleic Acids Res
Year2000
Volume28
Pages3950-61
AuthorsScavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME
TitleStructure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.
Related PDB1eg2
[3]
PubMed ID11024176
JournalNucleic Acids Res
Year2000
Volume28
Pages3962-71
AuthorsSzegedi SS, Reich NO, Gumport RI
TitleSubstrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase.
[4]
PubMed ID11024177
JournalNucleic Acids Res
Year2000
Volume28
Pages3972-81
AuthorsSzegedi SS, Gumport RI
TitleDNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases.

comments
This methylase recognizes the double-stranded sequence [G-A-A-T-T-C], causes specific methylation on 6-amino group of Adenine on both strands, and protects the DNA from cleavage by the RsrI endonuclease.
According to the literature [2], Asp65 acts as a general base, which can activate the acceptor group, the amino group of adenine. This activated group in turn makes a nucleophilic attack on the methyl group of the SAM molecule.

createdupdated
2002-09-032009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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