CATH Classification

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
Nishimasu, H., Ishitani, R., Yamashita, K., Iwashita, C., Hirata, A., Hori, H., Nureki, O.
Proc.Natl.Acad.Sci.USA