A0A5S9I2J1 · A0A5S9I2J1_PSEHK
- ProteinCytochrome c oxidase subunit 1
- GeneCOX1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids153 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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] + 8 H+(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H+(out) + 2 H2OThis reaction proceeds in the forward direction.
4 RHEA-COMP:10350 + 8 H+ (in)CHEBI:15378+ CHEBI:15379 = 4 RHEA-COMP:14399 + 4 H+ (out)CHEBI:15378+ 2 CHEBI:15377
Cofactor
Protein has several cofactor binding sites:
Pathway
Energy metabolism; oxidative phosphorylation.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial respiratory chain complex IV | |
Molecular Function | cytochrome-c oxidase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | electron transport coupled proton transport | |
Biological Process | mitochondrial electron transport, cytochrome c to oxygen |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c oxidase subunit 1
- EC number
Gene names
Encoded on
- Mitochondrion
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Leuciscidae > Pseudaspininae > Pseudaspius
Accessions
- Primary accessionA0A5S9I2J1
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 68-94 | Helical | ||||
Sequence: LTIFSLHLAGVSSILGAVNFITTIINM | ||||||
Transmembrane | 106-133 | Helical | ||||
Sequence: LFVWSVLVTAVLLLLSLPVLAAGITMLL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-43 | |||||
Sequence: FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEA | ||||||
Chain | PRO_5024909131 | 44-153 | Cytochrome c oxidase subunit 1 | |||
Sequence: GAGTGWTVYPPLAGNLAHTGASVDLTIFSLHLAGVSSILGAVNFITTIINMKPPAISQYQTPLFVWSVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-153 | Cytochrome oxidase subunit I profile | ||||
Sequence: FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHTGASVDLTIFSLHLAGVSSILGAVNFITTIINMKPPAISQYQTPLFVWSVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL |
Sequence similarities
Belongs to the heme-copper respiratory oxidase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length153
- Mass (Da)16,139
- Last updated2020-04-22 v1
- Checksum6DFEC252042359C9
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: F | ||||||
Non-terminal residue | 153 | |||||
Sequence: L |