CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1960 | SSo0622-like fold |
|
3.30.1960.10 | tRNA wybutosine-synthesizing-like |
Domain Context
CATH Clusters
| Superfamily | tRNA wybutosine-synthesizing-like |
| Functional Family |
Enzyme Information
| 2.1.1.282 |
tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))- methyltransferase.
based on mapping to UniProt Q9YDV3
S-adenosyl-L-methionine + 7-((3S)-(3-amino-3-carboxypropyl))-4- demethylwyosine(37) in tRNA(Phe) = S-adenosyl-L-homocysteine + 7-((3S)- (3-amino-3-carboxypropyl))wyosine(37) in tRNA(Phe).
-!- The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs. -!- These modifications are important for translational reading-frame maintenance. -!- The enzyme is found in all eukaryotes and in some archaea, but not in bacteria. -!- The eukaryotic enzyme is involved in the biosynthesis of wybutosine.
|
UniProtKB Entries (1)
| Q9YDV3 |
TYW3_AERPE
Aeropyrum pernix K1
TRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase
|
PDB Structure
| PDB | 2DVK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of Hypothetical protein from Aeropyrum pernix
To be Published
|
