CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.140 | Butyryl-CoA Dehydrogenase, subunit A; domain 3 |
|
1.20.140.10 | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
| Functional Family | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial |
Enzyme Information
| 1.3.8.7 |
Medium-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P11310
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
-!- One of several enzymes that catalyze the first step in fatty acids beta-oxidation. -!- The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds. -!- The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds. -!- cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9. -!- Formerly EC 1.3.2.2 and EC 1.3.99.3.
|
UniProtKB Entries (1)
| P13804 |
ETFA_HUMAN
Homo sapiens
Electron transfer flavoprotein subunit alpha, mitochondrial
|
PDB Structure
| PDB | 1T9G |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain Acyl-CoA dehydrogenase complex
J.Biol.Chem.
|