| IED ID | IndEnz0002013356 |
| Enzyme Type ID | protease013356 |
| Protein Name |
Cytochrome b-c1 complex subunit Rieske, mitochondrial EC 7.1.1.8 Complex III subunit 5 Cytochrome b-c1 complex subunit 5 Rieske iron-sulfur protein RISP Rieske protein UQCRFS1 Ubiquinol-cytochrome c reductase iron-sulfur subunit Cleaved into: Cytochrome b-c1 complex subunit 9 Su9 Subunit 9 8 kDa subunit 9 Complex III subunit IX Cytochrome b-c1 complex subunit 11 UQCRFS1 mitochondrial targeting sequence UQCRFS1 MTS Ubiquinol-cytochrome c reductase 8 kDa protein |
| Gene Name | UQCRFS1 |
| Organism | Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Platyrrhini (New World monkeys) Atelidae Atelinae Lagothrix (woolly monkeys) Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey) |
| Enzyme Sequence | MLPVAALSGPFAPVLSATSRGVXXXXXXXXXXXXXATPEPPVLDPKRPILSRESLSGQAARRPLVASVGLNVPASVRYSHTDIKVPDFSDYRRSEVLDKTKSSRESSDARKGFSYLVTAATAVGVTYAAKSIVTQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTQKEIEQEAAVELSQLRDPQHDLDRVKKPEWMILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPTYEFTGDDMVIVG |
| Enzyme Length | 274 |
| Uniprot Accession Number | Q69BJ8 |
| 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:0000250|UniProtKB:P08067}; |
| DNA Binding | |
| EC Number | 7.1.1.8 |
| Enzyme Function | FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]: 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. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity). {ECO:0000250|UniProtKB:P08067, ECO:0000250|UniProtKB:P47985}.; FUNCTION: [Cytochrome b-c1 complex subunit 9]: Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer. One of the fragments, called subunit 9, corresponds to its mitochondrial targeting sequence (MTS) (By similarity). The proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-derived fragments may prevent newly imported UQCRFS1 to be processed and assembled into complex III and is detrimental for the complex III structure and function (By similarity). {ECO:0000250|UniProtKB:P13272, ECO:0000250|UniProtKB:P47985, ECO:0000250|UniProtKB:Q9CR68}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Disulfide bond (1); Domain (1); Metal binding (5); Topological domain (2); Transmembrane (1) |
| Keywords | 2Fe-2S;Disulfide bond;Electron transport;Iron;Iron-sulfur;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Respiratory chain;Transit peptide;Translocase;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5ZLR5}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer. Several fragments are generated during UQCRFS1 insertion, most probably due to the endogenous matrix-processing peptidase (MPP) activity of the 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, which are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively. The action of the protease is also necessary for the clearance of the UQCRFS1 fragments. {ECO:0000250|UniProtKB:Q9CR68}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,775 |
| Kinetics | |
| Metal Binding | METAL 217; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000250|UniProtKB:P13272; METAL 219; /note=Iron-sulfur (2Fe-2S); via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P13272; METAL 236; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000250|UniProtKB:P13272; METAL 239; /note=Iron-sulfur (2Fe-2S); via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P13272; METAL 241; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000250|UniProtKB:P13272 |
| Rhea ID | RHEA:11484 |
| Cross Reference Brenda |