IED ID | IndEnz0002010593 |
Enzyme Type ID | protease010593 |
Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase |
Gene Name | OCT1 SCY_3247 |
Organism | Saccharomyces cerevisiae (strain YJM789) (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 YJM789) (Baker's yeast) |
Enzyme Sequence | MLRTIILKAGSNASIPSLSRQNKLLRFFATAGAVSRTSPGSIKKIFDDNSYWRNINGQDANNSKISQYLFKKNKTGLFKNPYLTSPDGLRKFSQVSLQQAQELLDKMRNDFSESGKLTYIMNLDRLSDTLCRVIDLCEFIRSTHPDDAFVRAAQDCHEQMFEFMNVLNTDVSLCNMLKSVLNNPEVSSKLSAEELKVGKILLDDFEKSGIYMNPDVREKFIQLSQEISLVGQEFINHTDYPGSNSVKIPCKDLDNSKVSTFLLKQLNKDVKGQNYKVPTFGYAAYALLKSCENEMVRKKLWTALHSCSDKQVKRLSHLIKLRAILANLMHKTSYAEYQLEGKMAKNPKDVQDFILTLMNNTIEKTANELKFIAELKAKDLKKPLTTNTDEILKLVRPWDRDYYTGKYFQLNPSNSPSAKEISYYFTLGNVIQGLSDLFQQIYGIRLEPAITDEGETWSPDVRRLNVISEEEGIIGIIYCDLFERNGKTSNPAHFTVCCSRQIYPSETDFSTIQVGENPDGTYFQLPVISLVCNFSPILIASKKSLCFLQLSEVETLFHEMGHAMHSMLGRTHMQNISGTRCATDFVELPSILMEHFAKDIRILTKIGKHYGTGETIQADMLQRFMKSTNFLQNCETYSQAKMAMLDQSFHDEKIISDIDNFDVVENYQALERRLKVLVDDQSNWCGRFGHLFGYGATYYSYLFDRTIASKIWYALFEDDPYSRKNGDKFKKHLLKWGGLKDPWKCIADVLECPMLEKGGSDAMEFIAQSHKS |
Enzyme Length | 772 |
Uniprot Accession Number | A6ZZI7 |
Absorption | |
Active Site | ACT_SITE 559; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | ACTIVITY REGULATION: Stimulated by Fe(2+). {ECO:0000250}. |
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. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism. |
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. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 88,190 |
Kinetics | |
Metal Binding | METAL 558; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 562; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 565; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |