Difference between revisions of "Part:BBa K3144004"
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<partinfo>BBa_K3144004 short</partinfo> | <partinfo>BBa_K3144004 short</partinfo> | ||
| − | 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. | + | 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. It belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases. |
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===Usage and Biology=== | ===Usage and Biology=== | ||
| + | V-PPase consists of a single polypeptide and exists as a dimmer of subunits of 71–80 kDa. | ||
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Revision as of 10:29, 20 October 2019
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. It belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE 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).