Detail Information for IndEnz0002001842
IED ID IndEnz0002001842
Enzyme Type ID protease001842
Protein Name Mitochondrial intermediate peptidase
MIP
EC 3.4.24.59
Gene Name OCT1 MIP1 YKL134C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (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 ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MLRTIILKAGSNASIPSPSRQNKLLRFFATAGAVSRTSPGSIKKIFDDNSYWRNINGQDANNSKISQYLFKKNKTGLFKNPYLTSPDGLRKFSQVSLQQAQELLDKMRNDFSESGKLTYIMNLDRLSDTLCRVIDLCEFIRSTHPDDAFVRAAQDCHEQMFEFMNVLNTDVSLCNILKSVLNNPEVSSKLSAEELKVGKILLDDFEKSGIYMNPDVREKFIQLSQEISLVGQEFINHTDYPGSNSVKIPCKDLDNSKVSTFLLKQLNKDVKGQNYKVPTFGYAAYALLKSCENEMVRKKLWTALHSCSDKQVKRLSHLIKLRAILANLMHKTSYAEYQLEGKMAKNPKDVQDFILTLMNNTIEKTANELKFIAELKAKDLKKPLTTNTDEILKLVRPWDRDYYTGKYFQLNPSNSPNAKEISYYFTLGNVIQGLSDLFQQIYGIRLEPAITDEGETWSPDVRRLNVISEEEGIIGIIYCDLFERNGKTSNPAHFTVCCSRQIYPSETDFSTIQVGENPDGTYFQLPVISLVCNFSPILIASKKSLCFLQLSEVETLFHEMGHAMHSMLGRTHMQNISGTRCATDFVELPSILMEHFAKDIRILTKIGKHYGTGETIQADMLQRFMKSTNFLQNCETYSQAKMAMLDQSFHDEKIISDIDNFDVVENYQALERRLKVLVDDQSNWCGRFGHLFGYGATYYSYLFDRTIASKIWYALFEDDPYSRKNGDKFKKHLLKWGGLKDPWKCIADVLECPMLEKGGSDAMEFIAQSHKS
Enzyme Length 772
Uniprot Accession Number P35999
Absorption
Active Site ACT_SITE 559; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation ACTIVITY REGULATION: Stimulated by Fe(2+). {ECO:0000269|PubMed:10332043}.
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. {ECO:0000269|PubMed:7593000, ECO:0000269|PubMed:8035833}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Mutagenesis (14); Sequence conflict (2); 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:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:8831696}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11283351; 12191769; 1518864; 16554755; 17445721; 19536198; 19837041; 19930686; 20489023; 21525245; 22172993; 22984266; 23212899; 23479443; 24943357; 25435547; 27669165; 27693354; 28821623; 7586024; 7674944; 9535840;
Motif
Gene Encoded By
Mass 88,183
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 587; /note=Zinc; catalytic; /evidence=ECO:0000305
Rhea ID
Cross Reference Brenda