CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.360 | Flavodoxin domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.360 |
| Functional Family | NAD(P)H-dependent FMN reductase |
Enzyme Information
| 1.5.1.38 |
FMN reductase (NADPH).
based on mapping to UniProt P80644
FMNH(2) + NADP(+) = FMN + NADPH.
-!- The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not. -!- The enzyme often forms a two-component system with monooxygenases such as luciferase. -!- Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor. -!- While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity. -!- Formerly EC 1.5.1.29 and EC 1.6.8.1.
|
UniProtKB Entries (1)
| P80644 |
SSUE_ECOLI
Escherichia coli K-12
FMN reductase (NADPH)
|
PDB Structure
| PDB | 6DQP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Not as easy as pi : An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.
Protein Sci.
|
