Detail Information for IndEnz0002006203
IED ID IndEnz0002006203
Enzyme Type ID protease006203
Protein Name Probable mitochondrial-processing peptidase subunit beta, mitochondrial
EC 3.4.24.64
Beta-MPP
Complex III subunit I
Core protein I
Cytochrome b-c1 complex subunit 1, mitochondrial
Ubiquinol-cytochrome c oxidoreductase core protein 1
Gene Name MPPbeta At3g02090 F1C9.12
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MAMKNLLSLARRSQRRLFLTQATRSSSSFSAIDSVPASASPTALSPPPPHLMPYDHAAEIIKNKIKKLENPDKRFLKYASPHPILASHNHILSAPETRVTTLPNGLRVATESNLSAKTATVGVWIDAGSRFESDETNGTAHFLEHMIFKGTDRRTVRALEEEIEDIGGHLNAYTSREQTTYYAKVLDSNVNQALDVLADILQNSKFEEQRINRERDVILREMQEVEGQTDEVVLDHLHATAFQYTPLGRTILGPAQNVKSITREDLQNYIKTHYTASRMVIAAAGAVKHEEVVEQVKKLFTKLSSDPTTTSQLVANEPASFTGSEVRMIDDDLPLAQFAVAFEGASWTDPDSVALMVMQTMLGSWNKNVGGGKHVGSDLTQRVAINEIAESIMAFNTNYKDTGLFGVYAVAKADCLDDLSYAIMYEVTKLAYRVSDADVTRARNQLKSSLLLHMDGTSPIAEDIGRQLLTYGRRIPTAELFARIDAVDASTVKRVANKYIYDKDIAISAIGPIQDLPDYNKFRRRTYWNRY
Enzyme Length 531
Uniprot Accession Number Q42290
Absorption
Active Site ACT_SITE 144; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; ACT_SITE 214; /evidence=ECO:0000305
Activity Regulation ACTIVITY REGULATION: Binding to the alpha subunit 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}.; FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000250|UniProtKB:P07256}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Chain (1); Metal binding (3); Region (1); Sequence conflict (1); Transit peptide (1)
Keywords Alternative splicing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Oxidoreductase;Protease;Reference proteome;Transit peptide;Zinc
Interact With Q9LDU5
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}. Mitochondrion inner membrane {ECO:0000269|PubMed:18189341}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07256}; Matrix side {ECO:0000250|UniProtKB:P07256}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11743115; 11870776; 12185496; 14730085; 15028209; 15047896; 15215502; 15276431; 15496452; 15618420; 15829605; 16113211; 16242667; 16254930; 16287169; 16626458; 16635983; 16679420; 17151019; 17217466; 17376161; 17432890; 18431481; 18775970; 20018591; 20118269; 21798944; 24529374;
Motif
Gene Encoded By
Mass 59,160
Kinetics
Metal Binding METAL 141; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 145; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 221; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P10507
Rhea ID
Cross Reference Brenda