DB code: S00261

RLCP classification 3.747.6300.267 : Transfer
CATH domain 3.40.50.150 : Rossmann fold Catalytic domain
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 S00291 S00412 D00075 D00076 D00079 D00080 D00082 D00083 D00823

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P14751 Modification methylase RsrI
M.RsrI
EC 2.1.1.72
Adenine-specific methyltransferase RsrI
PF01555 (N6_N4_Mtase)
[Graphical View]
P23192 Modification methylase MboII
M.MboII
EC 2.1.1.72
Adenine-specific methyltransferase MboII
DNA MTase MboIIA
PF01555 (N6_N4_Mtase)
[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
P14751 MTR1_RHOSH S-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine.
P23192 MTM2_MORBO 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
1eg2A Analogue:MTA Unbound Unbound Unbound
1g60A Bound:SAM Unbound Unbound Unbound
1g60B Bound:SAM Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eg2A ASP 65
1g60A ASP 30
1g60B ASP 30

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.1 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 1511884
Journal Gene
Year 1992
Volume 118
Pages 5-11
Authors Kaszubska W, Webb HK, Gumport RI
Title Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 11024175
Journal Nucleic Acids Res
Year 2000
Volume 28
Pages 3950-61
Authors Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME
Title Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.
Related PDB 1eg2
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11024176
Journal Nucleic Acids Res
Year 2000
Volume 28
Pages 3962-71
Authors Szegedi SS, Reich NO, Gumport RI
Title Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11024177
Journal Nucleic Acids Res
Year 2000
Volume 28
Pages 3972-81
Authors Szegedi SS, Gumport RI
Title DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases.
Related PDB
Related UniProtKB

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.

Created Updated
2002-09-03 2009-02-26