Function and Biology Details
Reactions catalysed:
Quinol + 2 ferricytochrome c(Side 2) = quinone + 2 ferrocytochrome c(Side 2) + 2 H(+)(Side 2)
Release of N-terminal targeting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero icosamer (preferred)
PDBe Complex ID:
PDB-CPX-179430 (preferred)
Entry contents:
10 distinct polypeptide molecules
Macromolecules (10 distinct):
Cytochrome b
Molecule details ›
Chains: C, N
Length: 385 amino acids
Theoretical weight: 43.41 KDa
Source organism: Yarrowia lipolytica
UniProt:
Sequence domains:
Length: 385 amino acids
Theoretical weight: 43.41 KDa
Source organism: Yarrowia lipolytica
UniProt:
- Canonical:
Q9B6D0 (Residues: 1-385; Coverage: 100%)
Sequence domains:
Cytochrome b-c1 complex subunit Rieske, mitochondrial
Molecule details ›
Chains: E, P
Length: 225 amino acids
Theoretical weight: 24.56 KDa
Source organism: Yarrowia lipolytica
UniProt:
Sequence domains:
Length: 225 amino acids
Theoretical weight: 24.56 KDa
Source organism: Yarrowia lipolytica
UniProt:
- Canonical: Q6CI02 (Residues: 1-225; Coverage: 100%)
Sequence domains:
Cytochrome b-c1 complex subunit 7
Ubiquinol-cytochrome C reductase hinge domain-containing protein
mitochondrial processing peptidase
Cytochrome b-c1 complex subunit 2, mitochondrial
quinol--cytochrome-c reductase
Cytochrome b-c1 complex subunit 8
Complex III subunit 9
Cytochrome b-c1 complex subunit 10
