| IED ID | IndEnz0002007357 |
| Enzyme Type ID | protease007357 |
| Protein Name |
Mitochondrial metalloendopeptidase OMA1 EC 3.4.24.- |
| Gene Name | OMA1 YKR087C YKR407 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MLRNIIRFKGFGKGTSGGFLKPVSFRVQLTRCYRYDNGPSYRRFNNGEYSQKSSFKSILLDKSSRKYLALLFGGCSLFYYTHLDKAPVSDRSRFIWVSRPLELTIGNYTYKSIWRQTQQEILPPQHPLSIKIENIFMKIVEAAYKDPSVDNSLLDGIKWEIHVVNDPTASPNAFVLPGGKVFIFSSILPICANDDGIATVLAHEFAHQLARHTAENLSKAPIYSLLGLVLYTVTGAHAINNILLDGFLRMPASRQMETEADYIGLMIMSRACFQPQESIKVWERMANFEKQMNRGGVVNMEFLSTHPASTRRIENMSKWLPKANEIYEQSDCSSMGNYYKSFFSM |
| Enzyme Length | 345 |
| Uniprot Accession Number | P36163 |
| Absorption | |
| Active Site | ACT_SITE 204; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:24648523" |
| Activity Regulation | ACTIVITY REGULATION: Protease activity is induced in response to various mitochondrial stress, such as changes in membrane potential, oxidative stress or chronic hyperpolarization, and depends on its C-terminal region. {ECO:0000269|PubMed:24648523}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Protease that is part of the quality control system in the inner membrane of mitochondria (PubMed:12963738, PubMed:22219186, PubMed:24648523, PubMed:27325672). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OXA1 and COX1 (PubMed:12963738, PubMed:22219186, PubMed:24648523). Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins (PubMed:12963738, PubMed:27325672). Cleaves the misfolded multi-pass membrane protein OXA1 (PubMed:12963738). Involved in quality control of cytochrome oxidase assembly: mediates the cleavage of COX1 in cells lacking COA2 (PubMed:22219186). Required for the stability of the respiratory supercomplexes (PubMed:26365306). Required for TOR signaling (PubMed:27325672). {ECO:0000269|PubMed:12963738, ECO:0000269|PubMed:22219186, ECO:0000269|PubMed:24648523, ECO:0000269|PubMed:26365306, ECO:0000269|PubMed:27325672}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Frameshift (2); Metal binding (3); Mutagenesis (7); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Disulfide bond;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Protease;Reference proteome;Thioester bond;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:12963738}; Single-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Forms a redox-dependent disulfide bond, which plays a structural role and regulates its conformational stability and activity. {ECO:0000269|PubMed:31044600}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10375630; 15772085; 17360454; 19841065; 21300850; 22808334; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,328 |
| Kinetics | |
| Metal Binding | METAL 203; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 207; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 257; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |