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Information on EC 7.1.1.7 - quinol oxidase (electrogenic, proton-motive force generating) and Organism(s) Bacillus subtilis and UniProt Accession P94364

for references in articles please use BRENDA:EC7.1.1.7
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IUBMB Comments
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, ubiquinol oxidase (H+-transporting).
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Bacillus subtilis
UNIPROT: P94364
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
cytochrome bd-i, cytochrome bd quinol oxidase, cydabdc, cytochrome bd-i respiratory oxidase, cytochrome bd-i complex, cytochrome bd-i ubiquinol oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bd-I type oxidase
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cytochrome bd oxidase
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bd-I type oxidase
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cytochrome bd oxidase
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ubiquinol oxidase (electrogenic, proton-motive force generating)
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-
-
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ubiquinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
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-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
quinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
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, ubiquinol oxidase (H+-transporting).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Degli Esposti, M.; Rosas-Perez, T.; Servin-Garciduenas, L.E.; Bolanos, L.M.; Rosenblueth, M.; Martinez-Romero, E.
Molecular evolution of cytochrome bd oxidases across proteobacterial genomes
Genome Biol. Evol.
7
801-820
2015
Rhodopseudomonas palustris, Magnetospirillum fulvum, Rhodovulum sp. PH10, Pararhodospirillum photometricum, Rhodovulum sulfidophilum (A0A0D6AXR3), Escherichia coli (P0ABJ9), Escherichia coli (P0ABK2), Bacillus subtilis (P94364), Bacillus subtilis (P94365), Acetobacter pasteurianus (S6CX21), Acetobacter pasteurianus (S6D686), Rhodopseudomonas palustris HaA2, Bacillus subtilis 168 (P94364), Bacillus subtilis 168 (P94365), Acetobacter pasteurianus 386B (S6CX21), Acetobacter pasteurianus 386B (S6D686)
Manually annotated by BRENDA team