| IED ID | IndEnz0002012437 |
| Enzyme Type ID | protease012437 |
| Protein Name |
Cytochrome b-c1 complex subunit Rieske, mitochondrial EC 7.1.1.8 Complex III subunit 5 Rieske iron-sulfur protein RISP Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit |
| Gene Name | RIP1 YEL024W |
| 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 | MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG |
| Enzyme Length | 215 |
| Uniprot Accession Number | P08067 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:2538628}; |
| DNA Binding | |
| EC Number | 7.1.1.8 |
| Enzyme Function | 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 (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable). {ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2538628, ECO:0000305|PubMed:11880631, ECO:0000305|PubMed:30598556}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Helix (5); Metal binding (4); Mutagenesis (17); Propeptide (1); Region (1); Topological domain (2); Transit peptide (1); Transmembrane (1); Turn (5) |
| Keywords | 2Fe-2S;3D-structure;Direct protein sequencing;Disulfide bond;Electron transport;Iron;Iron-sulfur;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Respiratory chain;Transit peptide;Translocase;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. |
| Modified Residue | |
| Post Translational Modification | PTM: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1. {ECO:0000269|PubMed:6309810, ECO:0000269|PubMed:8206223}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (5); X-ray crystallography (8) |
| Cross Reference PDB | 1EZV; 1KB9; 1KYO; 1P84; 2IBZ; 3CX5; 3CXH; 4PD4; 6GIQ; 6HU9; 6T0B; 6T15; 6YMX; |
| Mapped Pubmed ID | 10508156; 10591527; 10692548; 10971589; 11148026; 11245784; 11343898; 11522251; 11532444; 11556808; 11726495; 11805837; 12069575; 12206886; 12206910; 12377760; 12477387; 12627947; 12767232; 12782631; 12788490; 12837937; 14561769; 14592463; 14622010; 14670597; 14718526; 15039445; 15288805; 15456898; 15519305; 15759116; 15807653; 16843540; 16908520; 16962558; 17043137; 17337272; 18038116; 18093133; 18258809; 18366324; 18452702; 18454936; 18471987; 18501197; 18727146; 18779372; 18793174; 18839289; 19168025; 19236481; 19254687; 19325183; 19478336; 19563757; 19660431; 19810688; 19952509; 20111601; 20150421; 20335015; 20398659; 20955007; 20959106; 20979343; 21148204; 21471218; 21549177; 2163487; 21655263; 2168894; 21716720; 21807901; 21978667; 21993350; 22017868; 22137892; 22138626; 22306284; 22575765; 22705944; 22927643; 22985600; 23007649; 23116202; 23148267; 23172229; 23201476; 23212899; 23269318; 23276920; 23837470; 23983899; 24220496; 24421313; 24882724; 24893593; 2537289; 25640729; 25683140; 25880855; 26024642; 26504246; 26608359; 2844766; 29343425; 31988523; 32291341; 33016568; 6282857; 8394320; 8900149; 8999925; 9535897; 9565619; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,365 |
| Kinetics | |
| Metal Binding | METAL 159; /note="Iron-sulfur (2Fe-2S)"; /evidence="ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4"; METAL 161; /note="Iron-sulfur (2Fe-2S); via pros nitrogen"; /evidence="ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4"; METAL 178; /note="Iron-sulfur (2Fe-2S)"; /evidence="ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4"; METAL 181; /note="Iron-sulfur (2Fe-2S); via pros nitrogen"; /evidence="ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4" |
| Rhea ID | RHEA:11484 |
| Cross Reference Brenda |