| IED ID | IndEnz0002009636 |
| Enzyme Type ID | protease009636 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase |
| Gene Name | OCT1 LELG_04645 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MRSGSRLSNYLVRLSGRVSFTQKRSLTNVKLPSNVNYERLKAAFDSDEHTLNGKNNNNEGKLFSKTALFQGQKDGSASTGLFKNSYLTSPQGLVQFSKKSKLQAQTLVDEMTRDVLTHQGKLDYIKKLDQLSDILCRTIDVAEFIRVVHDDQKWVDAAQQTHEIIFEYMNQLNTNVELYANLVKILEDKDLISQLSDEEIKVGEYLRQDFERSGIHMDPQSRDQFVSLTQEISIMGSHFNNESSSLKSDWISITSNEFSAIEDRFIQSEVMRASALYPGKKESGTYYIPLASAIPYRIMIQCGSGNLRKKMWIGLHEASDEQVQVLNHFVAYRALLAKMLGYDSYAHYQLEHKMAKKPENVLSFLTNLQENLKNSQVLKELRALSALQQGYSLLSDEELIRQIKPWDRDFLLKSFEAKKLSSTENGEKASTDTSTSTTTSTTTTDSTTTTATFSNSTDSVAIKRLCEYFSIGTVIAGLSKLFSALYNISFVVEPTVKGEVWNEKRVRKLNVLNNSNGETMGYLYLDFCSPKVFPSHFTVVCLRQLNKAESVSEHGDMVQLSKDYQLPVVALVCNFTSGNPTLLSLDQVDTIFHEMGHAMHSMIGRTQLHNLSGTRCATDFVEIPSVLMESFSKDPRVLSEIGCHYRTGEPVPINLLEQAQSQRSALEACETFVQSKMAMLDQELHSKEIVELLRQGLEAINSTEIYHQVERDLEIFADEWSTWHGKFPHLFSYGAVYYSYLLDRAIANVLWQKLFAKDPWSRDAGIKYKEEILKWGGTKDPWACLADALQMEELRKGDAHAMQIIGENSKL |
| Enzyme Length | 811 |
| Uniprot Accession Number | A5E4V6 |
| Absorption | |
| Active Site | ACT_SITE 594; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.; EC=3.4.24.59; |
| DNA Binding | |
| EC Number | 3.4.24.59 |
| Enzyme Function | FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Metal binding (3); Region (1); Transit peptide (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 91,934 |
| Kinetics | |
| Metal Binding | METAL 593; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 597; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 600; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |