CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.20 | Dihydropteroate synthase-like |
Domain Context
CATH Clusters
| Superfamily | Dihydropteroate synthase-like |
| Functional Family | 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase |
Enzyme Information
| 2.1.1.258 |
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase.
based on mapping to UniProt Q46389
A [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate.
-!- Catalyzes the transfer of a methyl group from the N(5) group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. -!- Involved, together with EC 1.2.7.4 and EC 2.3.1.169, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
|
UniProtKB Entries (1)
| Q46389 |
ACSE_MOOTH
Moorella thermoacetica
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase
|
PDB Structure
| PDB | 2OGY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.
J.Biol.Chem.
|
