Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
plasma membrane | - |
Escherichia coli | 5886 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + 4 H+[side 2] | Escherichia coli | - |
ATP + H2O + 4 H+[side 1] | - |
r | |
ATP + H2O + 4 H+[side 1] | Escherichia coli | - |
ADP + phosphate + 4 H+[side 2] | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6E6 | epsilon subunit | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + 4 H+[side 2] | - |
Escherichia coli | ATP + H2O + 4 H+[side 1] | - |
r | |
ATP + H2O + 4 H+[side 1] | - |
Escherichia coli | ADP + phosphate + 4 H+[side 2] | - |
r |
Synonyms | Comment | Organism |
---|---|---|
FoF1-ATP synthase | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme uses the proton motive force across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate proton motive force | Escherichia coli |