CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
| Superfamily | Aldolase class I |
| Functional Family | Pyruvate formate-lyase-activating enzyme |
Enzyme Information
| 1.97.1.4 |
[Formate-C-acetyltransferase]-activating enzyme.
based on mapping to UniProt P0A9N4
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
-!- A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH(2) to AdoMet with concomitant cleavage of the latter. -!- The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.
|
UniProtKB Entries (1)
| P0A9N4 |
PFLA_ECOLI
Escherichia coli K-12
Pyruvate formate-lyase 1-activating enzyme
|
PDB Structure
| PDB | 3CB8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
Proc.Natl.Acad.Sci.Usa
|
