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 |
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| PubChem |
34755 34755 |
25246222 439155 25246222 439155 |
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| 2dpmA01 |
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Bound:SAM | Unbound | Unbound | Unbound | |
| 2dpmA02 |
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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 |
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|
ASP 194 | ||||
| 2dpmA02 |
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| 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], According to the literature [1], |
| Created | Updated |
|---|---|
| 2002-08-14 | 2009-02-26 |