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Literature summary for 7.1.2.2 extracted from

  • Vermeer, L.S.; Reat, V.; Hemminga, M.A.; Milon, A.
    Structural properties of a peptide derived from H+-V-ATPase subunit a (2009), Biochim. Biophys. Acta, 1788, 1204-1212.
    View publication on PubMed

Localization

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
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Saccharomyces cerevisiae
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ADP + phosphate + H+/out
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
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Saccharomyces cerevisiae ADP + phosphate + H+/out
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?

Subunits

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

Synonyms Comment Organism
H+-V-ATPase
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Saccharomyces cerevisiae
V-ATPase
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Saccharomyces cerevisiae
vacuolar H+-ATPase
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
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Saccharomyces cerevisiae