4 GO Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004427 | IPR004131 |
| GO:0009678 | IPR004131 |
| GO:0015992 | IPR004131 |
| GO:0016020 | IPR004131 |
4 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004427 | IPR004131 |
| GO:0009678 | IPR004131 |
| GO:0015992 | IPR004131 |
| GO:0016020 | IPR004131 |
| Type: | Family | Name: | Pyrophosphate-energised proton pump |
| Description: | Two types of proteins that hydrolyse inorganic pyrophosphate (PPi), very different in both amino acid sequence and structure, have been characterised to date: soluble and membrane-bound proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse PPi to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes [, ]. The latter type is represented by this group of proteins. H+-PPases () are also called vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps []. In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the V-PPase (V is for vacuolar) [].Two distinct biochemical subclasses of H+-PPases have been characterised to date: K+-stimulated and K+-insensitive [, ]. | Short Name: | PPase-energised_H-pump |
| GO Term | Gene Name |
|---|---|
| GO:0004427 | IPR004131 |
| GO:0009678 | IPR004131 |
| GO:0015992 | IPR004131 |
| GO:0016020 | IPR004131 |
| GO Term | Gene Name |
|---|---|
| GO:0004427 | IPR004131 |
| GO:0009678 | IPR004131 |
| GO:0015992 | IPR004131 |
| GO:0016020 | IPR004131 |
