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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 7.1.1.7

Accepted Name
Ubiquinol oxidase (electrogenic, proton-motive force generating).
Alternative Name(s)
Cytochrome bd-I oxidase.
Reaction catalysed
2 ubiquinol + O(2)(Side 2) + 4 H(+)(Side 2) <=> 2 ubiquinone + 2 H(2)O(Side 2) + 4 H(+)(Side 1)
Comment(s)
  • This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water.
  • The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1.
  • The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism.
  • Cf. EC 7.1.1.3.
  • Formerly EC 1.10.3.14.
Cross-references
BRENDA7.1.1.7
EC2PDB7.1.1.7
ExplorEnz7.1.1.7
PRIAM enzyme-specific profiles7.1.1.7
KEGG Ligand Database for Enzyme Nomenclature7.1.1.7
IUBMB Enzyme Nomenclature7.1.1.7
IntEnz7.1.1.7
MEDLINEFind literature relating to 7.1.1.7
MetaCyc7.1.1.7
UniProtKB/Swiss-Prot
P0ABK0, CYDA_ECOL6;  P0ABJ9, CYDA_ECOLI;  P0ABK1, CYDA_SHIFL;  
P0ABK4, CYDB_ECO57;  P0ABK3, CYDB_ECOL6;  P0ABK2, CYDB_ECOLI;  
Q2YKD6, CYDX_BRUA2;  P56100, CYDX_ECOLI;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.-.-.-