EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.24.B18 | mitochondrial inner membrane | integral, active at the matrix side of the inner membrane | Saccharomyces cerevisiae | 5743 | - |
3.4.24.B18 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.B18 | additional information | a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B18 | protein + H2O | Saccharomyces cerevisiae | quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability | peptides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.B18 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.24.B18 | proteolytic degradation of proteins | mechanism, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, intermolecular catalytic role of SRH domain at the C-terminus of the AAA domain, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B18 | protein + H2O | activity depends on oligomerisation | Saccharomyces cerevisiae | peptides | - |
? | |
3.4.24.B18 | protein + H2O | quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability | Saccharomyces cerevisiae | peptides | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.24.B18 | More | subunits span the membrane twice, activity depends on oligomerisation, the enzyme consists of a AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic domain, and a Walker-type P-loop ATPase domain | Saccharomyces cerevisiae |
3.4.24.B18 | oligomer | x * 70000-80000, homooligomeric | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.24.B18 | M41.003 | Merops-ID | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.B18 | ATP | dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family | Saccharomyces cerevisiae |