| IED ID | IndEnz0002001111 |
| Enzyme Type ID | protease001111 |
| Protein Name |
Mitochondrial-processing peptidase subunit beta EC 3.4.24.64 BeMPP1 Beta-MPP |
| Gene Name | MPP1 |
| Organism | Blastocladiella emersonii (Aquatic fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Blastocladiomycota Blastocladiomycota incertae sedis Blastocladiomycetes Blastocladiales Blastocladiaceae Blastocladiella Blastocladiella emersonii (Aquatic fungus) |
| Enzyme Sequence | MLSAALRLTAKRNVRSLATASSSSYPGALLNVPKTQVTRLPNGLTVATESNPALATATVGVWIDSGSRAETKANNGVAHFLEHISFKGTKQRTQSGLEIEIENMGGHLNAYTSREQTVYYAKLFSQDVAKGVNILGDILQNSTLDPGAIDRERAVILREAEEVDKQVEEVVFDHLHAAAFPENALGYTILGPKENIQTLSQADLQAYIKNNYTADRMVVVGAGNVDHAELCKLAETNFGKLPQGSGKAKFVRPAFTGSDVRIRVDDMPTAHIALAVEGASWTSADHWPLLVASAMIGSYDRAAGNAHPSSKLAQIVAKHNLANSFTSFNTTYSDTGLWGIYIQSNNRDNLDDLAHFTVREWMRLATAPSEGEVAIAKQQLKTSLLLALDGTTPVAEEIGRQMLAYGRRLSPFEIDRLVDAVTVEDVKRVANEFIYDRDLAIVAVGPVECLPDYNRIRSAMNLLRY |
| Enzyme Length | 465 |
| Uniprot Accession Number | Q00302 |
| Absorption | |
| Active Site | ACT_SITE 82; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10507 |
| Activity Regulation | ACTIVITY REGULATION: Binding to the alpha subunit is required for catalytic activity. {ECO:0000250|UniProtKB:P10507}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000250|UniProtKB:P10507}; |
| DNA Binding | |
| EC Number | 3.4.24.64 |
| Enzyme Function | FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity). {ECO:0000250|UniProtKB:P10507, ECO:0000250|UniProtKB:Q03346}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Transit peptide (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P10507}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,683 |
| Kinetics | |
| Metal Binding | METAL 79; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P10507; METAL 83; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P10507; METAL 159; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P10507 |
| Rhea ID | |
| Cross Reference Brenda |