CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1240 | Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1 |
|
1.10.1240.10 | Methionine synthase domain |
Domain Context
CATH Clusters
| Superfamily | Methionine synthase domain |
| Functional Family | Methionine synthase |
Enzyme Information
| 2.1.1.13 |
Methionine synthase.
based on mapping to UniProt P13009
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.
-!- The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). -!- Reactivation by reductive methylation is catalyzed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. -!- For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8. -!- In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2). -!- Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, which acts only on the triglutamate.
|
UniProtKB Entries (1)
| P13009 |
METH_ECOLI
Escherichia coli K-12
Methionine synthase
|
PDB Structure
| PDB | 3BUL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor.
Proc.Natl.Acad.Sci.Usa
|