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 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC |
Enzyme Information
| 1.5.-.- |
Acting on the CH-NH group of donors.
based on mapping to UniProt Q8ZD36
|
| 2.1.1.61 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase.
based on mapping to UniProt Q8ZD36
S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2- thiouridylate.
-!- Specific for the terminal methyl group of 5-methylaminomethyl-2- thiouridylate.
|
UniProtKB Entries (1)
| Q8ZD36 |
MNMC_YERPE
Yersinia pestis
TRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
|
PDB Structure
| PDB | 3PVC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.
Bmc Struct.Biol.
|
