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Literature summary for 2.1.1.225 extracted from
- Trm13p, the tRNA:Xm4 modification enzyme from Saccharomyces cerevisiae is a member of the Rossmann-fold MTase superfamily: prediction of structure and active site (2010), J. Mol. Model., 16, 599-606.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q12383 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Trm13p belongs to the RFM superfamily of MTases despite the absence of a significant sequence similarity to previously characterized members of this superfamily. The model reveals residues potentially responsible for cofactor binding, tRNA binding, and catalysis of the 2'-O-methylation reaction. The model suggests a presence of one to three disulfide bonds and/or metal ion binding site next to the substrate binding pocket | Saccharomyces cerevisiae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trm13p | - |
Saccharomyces cerevisiae |
| tRNA:Xm4 modification enzyme | - |
Saccharomyces cerevisiae |
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