ID UCRI1_TOBAC Reviewed; 258 AA. AC P49729; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 117. DE RecName: Full=Cytochrome b-c1 complex subunit Rieske-1, mitochondrial; DE EC=7.1.1.8; DE AltName: Full=Complex III subunit 5-1; DE AltName: Full=Rieske iron-sulfur protein 1; DE Short=RISP1; DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 1; DE Flags: Precursor; Fragment; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX PubMed=1961737; DOI=10.1073/pnas.88.23.10716; RA Huang J.T., Struck F., Matzinger D.F., Levings C.S. III; RT "Functional analysis in yeast of cDNA coding for the mitochondrial Rieske RT iron-sulfur protein of higher plants."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10716-10720(1991). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a CC multisubunit transmembrane complex that is part of the mitochondrial CC electron transport chain which drives oxidative phosphorylation. The CC respiratory chain contains 3 multisubunit complexes succinate CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase CC (complex IV, CIV), that cooperate to transfer electrons derived from CC NADH and succinate to molecular oxygen, creating an electrochemical CC gradient over the inner membrane that drives transmembrane transport CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron CC transfer from ubiquinol to cytochrome c, linking this redox reaction to CC translocation of protons across the mitochondrial inner membrane, with CC protons being carried across the membrane as hydrogens on the quinol. CC In the process called Q cycle, 2 protons are consumed from the matrix, CC 4 protons are released into the intermembrane space and 2 electrons are CC passed to cytochrome c. The Rieske protein is a catalytic core subunit CC containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 CC conformational states during catalysis to transfer electrons from the CC quinol bound in the Q(0) site in cytochrome b to cytochrome c1. CC {ECO:0000250|UniProtKB:P08067}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:132124; EC=7.1.1.8; CC Evidence={ECO:0000250|UniProtKB:P08067}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00628}; CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and CC Rieske protein, 2 core protein subunits, and several low-molecular CC weight protein subunits. The complex exists as an obligatory dimer and CC forms supercomplexes (SCs) in the inner mitochondrial membrane with CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P08067}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P08067}. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein. CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M77225; AAA34112.1; -; mRNA. DR PIR; B41607; B41607. DR AlphaFoldDB; P49729; -. DR SMR; P49729; -. DR STRING; 4097.P49729; -. DR PaxDb; 4097-P49729; -. DR Proteomes; UP000790787; Unplaced. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:AgBase. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0008121; F:quinol-cytochrome-c reductase activity; IGI:AgBase. DR GO; GO:0009060; P:aerobic respiration; IGI:AgBase. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IGI:AgBase. DR CDD; cd03470; Rieske_cytochrome_bc1; 1. DR FunFam; 2.102.10.10:FF:000001; Cytochrome b-c1 complex subunit Rieske, mitochondrial; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR036922; Rieske_2Fe-2S_sf. DR InterPro; IPR014349; Rieske_Fe-S_prot. DR InterPro; IPR005805; Rieske_Fe-S_prot_C. DR InterPro; IPR004192; Rieske_TM. DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su. DR NCBIfam; TIGR01416; Rieske_proteo; 1. DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF02921; UCR_TM; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; ISP domain; 1. DR SUPFAM; SSF81502; ISP transmembrane anchor; 1. DR PROSITE; PS51296; RIESKE; 1. PE 2: Evidence at transcript level; KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Respiratory chain; Transit peptide; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT TRANSIT <1..46 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 47..258 FT /note="Cytochrome b-c1 complex subunit Rieske-1, FT mitochondrial" FT /id="PRO_0000030676" FT TOPO_DOM 47..95 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305" FT TRANSMEM 96..118 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 119..258 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT DOMAIN 161..256 FT /note="Rieske" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT BINDING 201 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT BINDING 203 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT BINDING 220 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT BINDING 223 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT DISULFID 206..222 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" FT NON_TER 1 SQ SEQUENCE 258 AA; 28192 MW; FDA51B570CCEDCAF CRC64; WPVRSAAPSS SAFISANHFS SDDDSSSPRS ISPSLASVFL HHTRGFSSNS VSPAHDMGLV PDLPPTVAAI KNPTSKIVYD EHNHERYPPG DPSKRAFAYF VLTGGRFVYA SLMRLLILKF VLSMSASKDV LALASLEVDL SSIEPGTTVT VKWRGKPVFI RRRTEDDISL ANSVDLGSLR DPQQDAERVK NPEWLVVIGV CTHLGCIPLP NAGDFGGWFC PCHGSHYDIS GRIRKGPAPY NLEVPTYSFL EENKLLIG //