CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.210 | Cytochrome C Oxidase; Chain A |
|
1.20.210.10 | Cytochrome c oxidase-like, subunit I domain |
Domain Context
CATH Clusters
| Superfamily | Cytochrome c oxidase-like, subunit I domain |
| Functional Family | Cytochrome oxidase subunit I |
Enzyme Information
| 1.9.3.1 |
Cytochrome-c oxidase.
based on mapping to UniProt P0ABI8
4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O.
-!- The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. -!- Several bacteria appear to contain analogous oxidases.
|
| 1.10.3.- |
With oxygen as acceptor.
based on mapping to UniProt P0ABI8
|
| 1.10.3.10 |
Ubiquinol oxidase (H(+)-transporting).
based on mapping to UniProt P0ABI8
2 ubiquinol + O(2) + n H(+)(Side 1) = 2 ubiquinone + 2 H(2)O + n H(+)(Side 2).
-!- This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. -!- The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo(3) oxidase it is 2, while for the bd-II oxidase it is 1. -!- Cf. EC 1.10.3.14.
|
UniProtKB Entries (1)
| P0ABJ1 |
CYOA_ECOLI
Escherichia coli K-12
Cytochrome bo(3) ubiquinol oxidase subunit 2
|
PDB Structure
| PDB | 1FFT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
Nat.Struct.Biol.
|
