B0FWC7 · COX1_AEDAE
- ProteinCytochrome c oxidase subunit 1
- Genemt:CoI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids514 (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
Protein has several cofactor binding sites:
Note: Binds 2 heme A groups non-covalently per subunit.
Note: Binds a copper B center.
Pathway
Energy metabolism; oxidative phosphorylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 44 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 60 | Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue | ||||
Sequence: H | ||||||
Binding site | 239 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 243 | O2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 289 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 290 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 367 | Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 2 | ||||
Sequence: H | ||||||
Binding site | 368 | Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 2 | ||||
Sequence: D | ||||||
Binding site | 375 | Fe (UniProtKB | ChEBI) of heme a3 (UniProtKB | ChEBI); high-spin; axial binding residue | ||||
Sequence: H | ||||||
Binding site | 377 | Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | 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
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c oxidase subunit 1
- EC number
- Alternative names
Gene names
Encoded on
- Mitochondrion
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Nematocera > Culicoidea > Culicidae > Culicinae > Aedini > Aedes > Stegomyia
Accessions
- Primary accessionB0FWC7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 16-36 | Helical | ||||
Sequence: TLYFIFGVWSGMVGTSLSILI | ||||||
Transmembrane | 55-75 | Helical | ||||
Sequence: VIVTAHAFIMIFFMVMPIMIG | ||||||
Transmembrane | 101-117 | Helical | ||||
Sequence: FWMLPPSLTLLLSSSMV | ||||||
Transmembrane | 144-164 | Helical | ||||
Sequence: LAIFSLHLAGISSILGAVNFI | ||||||
Transmembrane | 182-202 | Helical | ||||
Sequence: LFVWSVVITAILLLLSLPVLA | ||||||
Transmembrane | 233-253 | Helical | ||||
Sequence: LFWFFGHPEVYILILPGFGMI | ||||||
Transmembrane | 267-287 | Helical | ||||
Sequence: FGTLGMIYAMLTIGLLGFIVW | ||||||
Transmembrane | 304-324 | Helical | ||||
Sequence: FTSATMIIAVPTGIKIFSWLA | ||||||
Transmembrane | 337-357 | Helical | ||||
Sequence: LLWSLGFVFLFTVGGLTGVVL | ||||||
Transmembrane | 379-399 | Helical | ||||
Sequence: VLSMGAVFAIMAGFIHWYPLL | ||||||
Transmembrane | 415-435 | Helical | ||||
Sequence: MMFIGVNLTFFPQHFLGLAGM | ||||||
Transmembrane | 451-471 | Helical | ||||
Sequence: IISSLGSTISLFAVIFFLFII |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000347262 | 1-514 | Cytochrome c oxidase subunit 1 | |||
Sequence: MSRQWLFSTNHKDIGTLYFIFGVWSGMVGTSLSILIRAELSHPGMFIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLSSSMVENGAGTGWTVYPPLSSGTAHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITLDRLPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPIGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIITQESGKKETFGTLGMIYAMLTIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWSLGFVFLFTVGGLTGVVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGMVMNPSWLKAQFSMMFIGVNLTFFPQHFLGLAGMPRRYSDFPDSYLTWNIISSLGSTISLFAVIFFLFIIWESMITQRTPSFPMQLSSSIEWYHTLPPAEHTYSELPLLSSNF | ||||||
Cross-link | 239↔243 | 1'-histidyl-3'-tyrosine (His-Tyr) | ||||
Sequence: HPEVY |
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).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length514
- Mass (Da)56,966
- Last updated2008-09-02 v2
- Checksum019CDFE533655F10
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 171 | in Ref. 1; ABY51624 | ||||
Sequence: R → W |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EU352212 EMBL· GenBank· DDBJ | ABY51624.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AF380835 EMBL· GenBank· DDBJ | AAK56378.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF390098 EMBL· GenBank· DDBJ | AAK73349.2 EMBL· GenBank· DDBJ | mRNA | ||
AY056596 EMBL· GenBank· DDBJ | AAL25639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY056597 EMBL· GenBank· DDBJ | AAL25640.1 EMBL· GenBank· DDBJ | Genomic DNA |