Detail Information for IndEnz0002006461
IED ID IndEnz0002006461
Enzyme Type ID protease006461
Protein Name Probable mitochondrial-processing peptidase subunit beta
EC 3.4.24.64
Beta-MPP
PEP
Gene Name qcr1 SPBP23A10.15c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MLRLQNLPKLVRRFATTALPKTETTTLKNGLTVATEHHPYAQTATVLVGVDAGSRAETAKNNGAAHFLEHLAFKGTKNRSQKALELEFENTGAHLNAYTSREQTVYYAHAFKNAVPNAVAVLADILTNSSISASAVERERQVILREQEEVDKMADEVVFDHLHATAYQGHPLGRTILGPKENIESLTREDLLQYIKDNYRSDRMIISSAGSISHEELVKLAEKYFGHLEPSAEQLSLGAPRGLKPRFVGSEIRARDDDSPTANIAIAVEGMSWKHPDYFTALVMQAIIGNWDRAMGASPHLSSRLSTIVQQHQLANSFMSFSTSYSDTGLWGIYLVTENLGRIDDLVHFTLQNWARLTVATRAEVERAKAQLRASLLLSLDSTTAIAEDIGRQLLTTGRRMSPQEVDLRIGQITEKDVARVASEMIWDKDIAVSAVGSIEGLLDYNRIRSSISMNRW
Enzyme Length 457
Uniprot Accession Number Q9P7X1
Absorption
Active Site ACT_SITE 69; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Activity Regulation ACTIVITY REGULATION: Binding to mas2 is required for catalytic activity. {ECO:0000250|UniProtKB:P10507}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000250|UniProtKB:P10507};
DNA Binding
EC Number 3.4.24.64
Enzyme Function FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity). {ECO:0000250|UniProtKB:P10507, ECO:0000250|UniProtKB:Q03346}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Sequence conflict (4); 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|UniProtKB:P10507}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20473289; 23697806; 30099677;
Motif
Gene Encoded By
Mass 50,737
Kinetics
Metal Binding METAL 66; /note=Zinc; via tele nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 70; /note=Zinc; via tele nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 146; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Rhea ID
Cross Reference Brenda