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 |