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CATH domain | Related DB codes (homologues) |
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3.40.50.150 : Rossmann fold | S00637,S00639,S00262,S00291,S00412,D00075,D00076,D00079,D00080,D00082,D00083,D00823 |
Enzyme Name | UniProtKB | KEGG |
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| P14751 | P23192 |
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Protein name | Modification methylase RsrI | Modification methylase MboII | site-specific DNA-methyltransferase (adenine-specific)modification methylaserestriction-modification system |
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Synonyms | M.RsrIEC 2.1.1.72Adenine-specific methyltransferase RsrI | M.MboIIEC 2.1.1.72Adenine-specific methyltransferase MboIIDNA MTase MboIIA |
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Pfam | PF01555 (N6_N4_Mtase) [Graphical view]
| PF01555 (N6_N4_Mtase) [Graphical view]
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UniProtKB:Accession Number | P14751 | P23192 |
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Entry name | MTR1_RHOSH | MTM2_MORBO |
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Activity | S-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. |
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Subunit |
| Homodimer. |
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Subcellular location |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00019 | C00821 | C00021 | C03391 |
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Compound | S-Adenosyl-L-methionine | DNA adenine | S-Adenosyl-L-homocysteine | DNA 6-methylaminopurine |
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Type | amino acids,amine group,nucleoside,sulfonium ion | amine group,nucleic acids | amino acids,amine group,nucleoside,sulfide group | amine group,nucleic acids |
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ChEBI | 67040
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| 16680 57856
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PubChem | 34755
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| 439155 25246222
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| | | | | | | | | | | |
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1eg2A |  |  |  |  |  |  |  | Analogue:MTA | Unbound | Unbound | Unbound |
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1g60A |  |  |  |  |  |  |  | Bound:SAM | Unbound | Unbound | Unbound |
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1g60B |  |  |  |  |  |  |  | Bound:SAM | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[2] | Fig.1 | 1 |
references | [1] |
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PubMed ID | 1511884 |
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Journal | Gene |
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Year | 1992 |
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Volume | 118 |
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Pages | 5-11 |
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Authors | Kaszubska W, Webb HK, Gumport RI |
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Title | Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli. |
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[2] |
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PubMed ID | 11024175 |
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Journal | Nucleic Acids Res |
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Year | 2000 |
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Volume | 28 |
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Pages | 3950-61 |
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Authors | Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME |
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Title | Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases. |
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Related PDB | 1eg2 |
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[3] |
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PubMed ID | 11024176 |
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Journal | Nucleic Acids Res |
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Year | 2000 |
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Volume | 28 |
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Pages | 3962-71 |
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Authors | Szegedi SS, Reich NO, Gumport RI |
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Title | Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase. |
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[4] |
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PubMed ID | 11024177 |
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Journal | Nucleic Acids Res |
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Year | 2000 |
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Volume | 28 |
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Pages | 3972-81 |
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Authors | Szegedi SS, Gumport RI |
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Title | DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases. |
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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.
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created | updated |
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2002-09-03 | 2009-02-26 |
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