Part:BBa_K3144004

AVP channel from Vigna radiata

Chain A, Pyrophosphate-energized vacuolar membrane proton pump from Vigna radiata (Mung bean). Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H+-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H+-ATPase on the same membrane. V-PPase belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases.

Usage and Biology

V-PPase consists of a single polypeptide and exists as a dimmer of subunits of 71–80 kDa.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal BsaI site found at 2019
  

References

1. Wada, Y. Mutagenic Analysis of Functional Residues in Putative Substrate- binding Site and Acidic Domains of Vacuolar H ؉ -Pyrophosphatase * clude essential common motifs shared among the P-type. 276, 7654–7660 (2001).

2. Silva, P. & Gerós, H. Regulation by salt of vacuolar H + -ATPase and H + -pyrophosphatase activities and Na + /H + exchange. Plant Signal. Behav. 4, 718–726 (2009).