Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
vacuolar membrane | V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d | Saccharomyces cerevisiae | 5774 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Saccharomyces cerevisiae | - |
ADP + phosphate + H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Saccharomyces cerevisiae | ADP + phosphate + H+/out | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d. Proton translocation takes place at the interface of subunit a and the rotating c, c', and c'' subunits. NMR structure determination, 3D structure of a peptide derived from the putative transmembrane segment 7 of subunit a from H+-V-ATPase determined by solution state NMR in SDS solution. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738. The secondary structure of the peptide depends on the pH and the type of detergent used, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
H+-V-ATPase | - |
Saccharomyces cerevisiae |
V-ATPase | - |
Saccharomyces cerevisiae |
vacuolar H+-ATPase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |