CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.150 | Vaccinia Virus protein VP39 |
Domain Context
CATH Clusters
| Superfamily | Vaccinia Virus protein VP39 |
| Functional Family | tRNA wybutosine-synthesizing protein 4 |
Enzyme Information
| 2.1.1.290 |
tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase.
based on mapping to UniProt Q08282
S-adenosyl-L-methionine + 7-((3S)-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) = S-adenosyl-L-homocysteine + 7-((3S)-3-amino-3- (methoxycarbonyl)propyl)wyosine(37) in tRNA(Phe).
-!- The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. -!- The modification is important for translational reading-frame maintenance. -!- In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) as substrate. -!- The enzyme also has the activity of EC 2.3.1.231.
|
| 2.3.1.231 |
tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)- methoxycarbonyltransferase.
based on mapping to UniProt Q08282
S-adenosyl-L-methionine + 7-((3S)-3-amino-3- (methoxycarbonyl)propyl)wyosine(37) in tRNA(Phe) + CO(2) = S-adenosyl-L- homocysteine + wybutosine(37) in tRNA(Phe).
-!- The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. -!- The modification is important for translational reading-frame maintenance. -!- In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-(methoxycarbonyl)propyl)wyosine(37) in tRNA(Phe) as substrate. -!- The enzyme also has the activity of EC 2.1.1.290.
|
UniProtKB Entries (1)
| Q08282 |
TYW4_YEAST
Saccharomyces cerevisiae S288C
TRNA wybutosine-synthesizing protein 4
|
PDB Structure
| PDB | 2ZZK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.
Nucleic Acids Res.
|
