CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family |
Enzyme Information
| 2.1.1.74 |
Methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase (FADH(2)-oxidizing).
based on mapping to UniProt Q5SID2
5,10-methylenetetrahydrofolate + uracil(54) in tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA + FAD.
-!- Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. -!- One almost universal post-translational modification is the conversion of U54 into ribothymidine in the T-Psi-C loop, and this modification is found in most species studied to date. -!- Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and FADH(2) to supply the atoms for methylation of U54, EC 2.1.1.35 uses S-adenosyl-L-methionine. -!- Formerly EC 2.1.2.12.
|
UniProtKB Entries (1)
| Q5SID2 |
TRMFO_THET8
Thermus thermophilus HB8
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO
|
PDB Structure
| PDB | 3G5Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase
Proc.Natl.Acad.Sci.USA
|
