| IED ID | IndEnz0002008055 |
| Enzyme Type ID | protease008055 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase |
| Gene Name | OCT1 KLLA0B12397g |
| Organism | Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Kluyveromyces Kluyveromyces lactis (Yeast) (Candida sphaerica) Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) |
| Enzyme Sequence | MLRTVSVGRQYVQRYFGHCLIVNSVRHSSSATVNRLKQPLRRVFDDDSHWRALNHSNYKLNESKGRKFGLRSTSDLETGLFQNSYLKSANGLVEFTQHSFEKAKELVQKIHSIETQDEMKYYIKDLDQLSDVLCRVIDLCEFIRATHPDKKFVQTAQQCHEKMFEIMNILNTDVRLCDLLTQCLRESDVLGLDSEEIRTGKILLEDFEKSGIYMKPEIREKFIQLSQEISVIGQDFINNTEYVRSNYIKISCELMDAHVNKMVCSQMKKDITGEYYKVPTYGYIPHTLLRTCSDEVIRMKIWTEMHSCSDAQIERLTKLISLRVELAKLLGSQNFAQYQLHGKMAKTPENVSGFLESLVHSTRIKAASELKPLAVLKSELTGTQTPHTSEEVLELMKPWDRDYYGSIQALAQRRSSSLDNGESISSSFSLGVVMQGLSDLFEKIYGIKLVPATPKTGETWSPDVRRIDVVDEHDGLIGVMYCDLFEREGKTPNPAHFTVCCSRNMYLNEADTSTIQVGVNSNGQKFQLPVISLVCDFRWVEVNMGDGKHQQMCLLQLNEIETLFHEMGHAMHSMLGRTQLQNVSGTRCATDFVELPSILMEHFARDTRVLSSISSHYKTGKSLDVEVLKNHQLENQFLQNCETFSQIKMSFLDQELHNLDHTTDGSIDVIAIYHRLERRLAVLPDDQSNWCGKFGHLFGYGASYYSYLFDRAIASKIWDHLFEQDPFNRTNGTKFKEGLLQWGGSRDPWYLLSQVLDEPRLAKGDEWGMRYIGDVKTGM |
| Enzyme Length | 779 |
| Uniprot Accession Number | Q6CVF7 |
| Absorption | |
| Active Site | ACT_SITE 566; /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); Metal binding (3); 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 | 89,380 |
| Kinetics | |
| Metal Binding | METAL 565; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 569; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 572; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |