Function and Biology Details
Reaction catalysed:
a quinone + succinate = fumarate + a quinol.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Fumarate reductase/succinate dehydrogenase, transmembrane subunit
- Succinate dehydrogenase, cytochrome b556 subunit
- Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybS
- Succinate dehydrogenase, cytochrome b subunit, conserved site
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
- FAD/NAD(P)-binding domain superfamily
- Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
16 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-129184 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Succinate dehydrogenase [rhodoquinone] flavoprotein subunit 1, mitochondrial
Molecule details ›
Chains: A, E
Length: 645 amino acids
Theoretical weight: 71.39 KDa
Source organism: Ascaris suum
UniProt:
Sequence domains:
Structure domains:
Length: 645 amino acids
Theoretical weight: 71.39 KDa
Source organism: Ascaris suum
UniProt:
- Canonical:
Q33862 (Residues: 1-645; Coverage: 100%)
Sequence domains:
Structure domains:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Molecule details ›
Chains: B, F
Length: 282 amino acids
Theoretical weight: 31.67 KDa
Source organism: Ascaris suum
UniProt:
Sequence domains:
Structure domains:
Length: 282 amino acids
Theoretical weight: 31.67 KDa
Source organism: Ascaris suum
UniProt:
- Canonical: O44074 (Residues: 1-282; Coverage: 100%)
Sequence domains:
Structure domains:
Succinate dehydrogenase [ubiquinone] cytochrome b large subunit, mitochondrial
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit 1, mitochondrial
