| Accession | TIGR01104 |
| Name | V_PPase |
| Function | V-type H(+)-translocating pyrophosphatase |
| Trusted Cutoff | 651.90 |
| Domain Trusted Cutoff | 651.90 |
| Noise Cutoff | 283.60 |
| Domain Noise Cutoff | 283.60 |
| Isology Type | equivalog |
| EC Number | 3.6.1.1 |
| HMM Length | 697 |
| Mainrole Category | Transport and binding proteins |
| Subrole Category | Cations and iron carrying compounds |
| Gene Ontology Term | GO:0005887: integral to plasma membrane cellular_component |
| | GO:0009678: hydrogen-translocating pyrophosphatase activity molecular_function |
| | GO:0015992: proton transport biological_process |
| Author | Ujwal ML, Haft DH, Paulsen IT |
| Entry Date | Jan 9 2001 4:00PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model describes proton pyrophosphatases from eukaryotes (predominantly plants), archaea and bacteria. It is an integral membrane protein and is suggested to have about 15 membrane spanning domains. Proton translocating inorganic pyrophosphatase, like H(+)-ATPase, acidifies the vacuoles and is pivotal to the vacuolar secondary active transport systems in plants. |
| References | RM 10556526
RT A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps.
RA Drozdowicz YM, Lu YP, Patel V, Fitz-Gibbon S, Miller JH, Rea PA.
RL FEBS Lett 1999 Nov 5;460(3):505-12
DR HAMAP; MF_01130; 22 of 31 |
