| IED ID | IndEnz0002008327 |
| Enzyme Type ID | protease008327 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase Fragment |
| Gene Name | oct1 BC1G_12067 |
| Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | RRLATASTQYRESRPVPVDNSAPGAKRDDRTLRQIFDSPNFWAEFSQSSKQSYNRPAVGLFQNRYLVNPQGFEVFANTSLRKAQRIVDKVLSASTVEEYRHVARELDRLSDLLCRVIDLSDFVRATHPNAAIQAAASRAYAKMFEYMNILNTTTGLDKQLEIAMATPEIVAGWTEEEVVVADILRKDFAKSAIDLPRAQRERFVALSQEISEIGPEFVDYMTPAKPYLTFESSKLKGMDPVLVRQYTTWGQTKIPTIGGAAAAAIRSVQNEDVRKEIFMATRTASRNTVYKLEELMRKRAELAKLSRYESYSHLALGDKMAKSPASVSQFLEALSKDNNQIVEGEVSELLKFKMSNSHGSSPGLQPWDKDYYMSQILASVRSHSRNSDFLSAYFSLGTVMQGLSRLFTRLYGVRLAPHETMPGETWNSDVRRLDVISETDGHVAVLYCDLFSRPGKSPNPAHFTLRCSREITTPELEEASSLSQNGLFKTNEEAANDGMATSRASGVLKQLPTIALICDFVTMSGKSSRPALLSFNEVQTLFHEMGHAIHSILGRTSLQNVSGTRCATDFAELPSVLMEHFAADPSVLSLFARHYETDQPLPYEMVAEKLALDKRFEGSDTENQIILSMLDLAYHSDLPLSPSFSSTQIYHSLQQKHGALPVDPPGTCWQGFFGHLFGYGSTYYSYLFDRVLARRIWQVVFKDGEAGGSIQRDNGEKMKEEVLKWGGGRDPWKCLAGVLDDGRVENGDEKAMAIVGSWGVKE |
| Enzyme Length | 762 |
| Uniprot Accession Number | A6SHZ5 |
| Absorption | |
| Active Site | ACT_SITE 544; /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); Erroneous initiation (1); Metal binding (3); Non-terminal residue (1); Region (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;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 | 85,181 |
| Kinetics | |
| Metal Binding | METAL 543; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 547; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 550; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |