P00412 · COX2_MAIZE
- ProteinCytochrome c oxidase subunit 2
- GeneCOX2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids260 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic activity
- 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out)This reaction proceeds in the forward direction.
4 RHEA-COMP:10350 + CHEBI:15379 + 8 H+ (in)CHEBI:15378= 4 RHEA-COMP:14399 + 2 CHEBI:15377 + 4 H+ (out)CHEBI:15378
Cofactor
Note: Binds a dinuclear copper A center per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 189 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 224 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 224 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 226 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 226 | Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 1 | ||||
Sequence: E | ||||||
Binding site | 228 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 228 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 232 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 235 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Molecular Function | copper ion binding | |
Molecular Function | cytochrome-c oxidase activity | |
Biological Process | electron transport chain |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c oxidase subunit 2
- EC number
- Alternative names
Gene names
Encoded on
- Mitochondrion
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionP00412
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-43 | Mitochondrial intermembrane | ||||
Sequence: MILRLLECRFFTIALCDAAEPWQLGFQDAATPMMQGIIDLHHD | ||||||
Transmembrane | 44-64 | Helical | ||||
Sequence: IFFFLILILVFVLWMLVRALW | ||||||
Topological domain | 65-84 | Mitochondrial matrix | ||||
Sequence: HFNEQTNPIPQRIVHGTTIE | ||||||
Transmembrane | 85-105 | Helical | ||||
Sequence: IIWTIFPSVILLFIAIPSFAL | ||||||
Topological domain | 106-260 | Mitochondrial intermembrane | ||||
Sequence: LYSMDGVLVDPAITIKAIGHQWYWTYEYSDYNSSDEQSLTFDSYMIPEDDLELGQLRLLEVDNRVVVPAKTHLRMIVTSADVLHSWAVPSLGVKCDAVPGRLNLTSILVQREGVYYGQCSEICGTNHAFMPIVVEAVTLKDYADWVSNQLILQTN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000183629 | 1-260 | Cytochrome c oxidase subunit 2 | |||
Sequence: MILRLLECRFFTIALCDAAEPWQLGFQDAATPMMQGIIDLHHDIFFFLILILVFVLWMLVRALWHFNEQTNPIPQRIVHGTTIEIIWTIFPSVILLFIAIPSFALLYSMDGVLVDPAITIKAIGHQWYWTYEYSDYNSSDEQSLTFDSYMIPEDDLELGQLRLLEVDNRVVVPAKTHLRMIVTSADVLHSWAVPSLGVKCDAVPGRLNLTSILVQREGVYYGQCSEICGTNHAFMPIVVEAVTLKDYADWVSNQLILQTN |
Proteomic databases
Interaction
Subunit
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).
Structure
Sequence
- Sequence statusComplete
- Length260
- Mass (Da)29,680
- Last updated1996-10-01 v4
- Checksum2F90F35CFB1A702F
RNA Editing
Edited at positions 5 11 26 56 57 87 95 129 130 150 156 161 184 188 196 207 213 235
Keywords
- Coding sequence diversity