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 | Succinate dehydrogenase flavoprotein subunit |
Enzyme Information
| 1.3.5.1 |
Succinate dehydrogenase (quinone).
based on mapping to UniProt P0AC41
Succinate + a quinone = fumarate + a quinol.
-!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4.
|
UniProtKB Entries (1)
| P07014 |
SDHB_ECOLI
Escherichia coli K-12
Succinate dehydrogenase iron-sulfur subunit
|
PDB Structure
| PDB | 2ACZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.
J.Biol.Chem.
|
