Q9I426 · CYOB_PSEAE
- ProteinCytochrome bo(3) ubiquinol oxidase subunit 1
- GenecyoB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids658 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Cytochrome bo3 ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron and generating a proton motive force. All the redox centers of this enzyme complex are located within the largest subunit, subunit I. Protons are probably pumped via D- and K- channels found in this subunit.
Miscellaneous
Ubiquinol oxidase catalyzes the terminal step in the electron transport chain.
Catalytic activity
- 2 a ubiquinol + n H+(in) + O2 = 2 a ubiquinone + n H+(out) + 2 H2O
2 a ubiquinol RHEA-COMP:9566 + n H+ (in)CHEBI:15378+ CHEBI:15379 = 2 a ubiquinone RHEA-COMP:9565 + n H+ (out)CHEBI:15378+ 2 CHEBI:15377
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper B ion per subunit.
Note: Binds 1 low-spin heme b per subunit.
Note: Binds 1 high-spin heme o per subunit, also named heme o3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 71 | a ubiquinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 75 | a ubiquinone (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 98 | a ubiquinone (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 106 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 170 | heme b (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 284 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 288 | Fe(II)-heme o (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 333 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 334 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 411 | Fe(II)-heme o (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 419 | Fe (UniProtKB | ChEBI) of Fe(II)-heme o (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 421 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 481 | heme b (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 482 | heme b (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | respirasome | |
Molecular Function | cytochrome bo3 ubiquinol oxidase activity | |
Molecular Function | cytochrome-c oxidase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor | |
Biological Process | aerobic respiration | |
Biological Process | electron transport coupled proton transport | |
Biological Process | respiratory electron transport chain |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome bo(3) ubiquinol oxidase subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9I426
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-14 | Periplasmic | ||||
Sequence: MFGKLTLSAVPYHE | ||||||
Transmembrane | 15-35 | Helical | ||||
Sequence: PIVMVTLAVVALLGLGVVGAI | ||||||
Topological domain | 36-56 | Cytoplasmic | ||||
Sequence: TYYRKWTYLWTEWLTSVDHKK | ||||||
Transmembrane | 57-77 | Helical | ||||
Sequence: IGVMYIVVALVMLVRGFADAI | ||||||
Topological domain | 78-101 | Periplasmic | ||||
Sequence: MMRGQLALAEGANHGYLPPEHYDQ | ||||||
Transmembrane | 102-122 | Helical | ||||
Sequence: IFTAHGVIMIIFMAMPFMTGL | ||||||
Topological domain | 123-135 | Cytoplasmic | ||||
Sequence: MNLAVPLQIGARD | ||||||
Transmembrane | 136-156 | Helical | ||||
Sequence: VAFPFLNSLSFWLLVVSAMLV | ||||||
Topological domain | 157-189 | Periplasmic | ||||
Sequence: NVSLGLGEFARTGWVAYPPLSELAYSPGVGVDY | ||||||
Transmembrane | 190-210 | Helical | ||||
Sequence: YIWALQISGMGTLLTGINFLV | ||||||
Topological domain | 211-232 | Cytoplasmic | ||||
Sequence: TVFKMRTPGMKLMQMPIFTWTC | ||||||
Transmembrane | 233-253 | Helical | ||||
Sequence: TFANILIVASFPILTAALGLL | ||||||
Topological domain | 254-277 | Periplasmic | ||||
Sequence: SLDRYLDMHFFTNELGGNAMMYIN | ||||||
Transmembrane | 278-298 | Helical | ||||
Sequence: LFWAWGHPEVYILILPAFGIF | ||||||
Topological domain | 299-315 | Cytoplasmic | ||||
Sequence: SEVTATFAGKRMFGYKS | ||||||
Transmembrane | 316-336 | Helical | ||||
Sequence: MVWASAAITFLGFTVWLHHFF | ||||||
Topological domain | 337-346 | Periplasmic | ||||
Sequence: TMGSGGDVNG | ||||||
Transmembrane | 347-367 | Helical | ||||
Sequence: FFGVATMLISIPTGVKLFNWL | ||||||
Topological domain | 368-380 | Cytoplasmic | ||||
Sequence: FTIYKGRLRFSTP | ||||||
Transmembrane | 381-401 | Helical | ||||
Sequence: ILWTLGFMVTFTIGGMTGVLL | ||||||
Topological domain | 402-423 | Periplasmic | ||||
Sequence: AIPGADFLLHNSLFLIAHFHNT | ||||||
Transmembrane | 424-444 | Helical | ||||
Sequence: IIGGAVFGYLAGFAFWFPKAF | ||||||
Topological domain | 445-456 | Cytoplasmic | ||||
Sequence: GFTLDEKWGKRS | ||||||
Transmembrane | 457-477 | Helical | ||||
Sequence: FWCWLVGFYMAFMPLYILGFM | ||||||
Topological domain | 478-493 | Periplasmic | ||||
Sequence: GMTRRLNHYDNPLWKP | ||||||
Transmembrane | 494-514 | Helical | ||||
Sequence: YLVVAFFGAVLIFCGIACQLI | ||||||
Topological domain | 515-594 | Cytoplasmic | ||||
Sequence: QLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFS | ||||||
Transmembrane | 595-615 | Helical | ||||
Sequence: IAVFAFVFGFAAIWHIWWLMA | ||||||
Topological domain | 616-658 | Periplasmic | ||||
Sequence: VGFVGMIGSFIVRSYNQDVDYYVQPEEIEKIESARFQQLAKQV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000287755 | 1-658 | Cytochrome bo3 ubiquinol oxidase subunit 1 | |||
Sequence: MFGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQPEEIEKIESARFQQLAKQV | ||||||
Cross-link | 284↔288 | 1'-histidyl-3'-tyrosine (His-Tyr) | ||||
Sequence: HPEVY |
Proteomic databases
Interaction
Subunit
The cytochrome bo3 ubiquinol oxidase complex is a heterooctamer of two A chains, two B chains, two C chains and two D chains.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length658
- Mass (Da)73,934
- Last updated2001-03-01 v1
- ChecksumD7F82D87E9D682A1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG04707.1 EMBL· GenBank· DDBJ | Genomic DNA |