ID Q6CM66_KLULA Unreviewed; 213 AA. AC Q6CM66; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 24-JAN-2024, entry version 136. DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial {ECO:0000256|RuleBase:RU004494}; DE EC=7.1.1.8 {ECO:0000256|RuleBase:RU004494}; GN ORFNames=KLLA0_E22573g {ECO:0000313|EMBL:CAH00060.1}; OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH00060.1, ECO:0000313|Proteomes:UP000000598}; RN [1] {ECO:0000313|EMBL:CAH00060.1, ECO:0000313|Proteomes:UP000000598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / RC WM37 {ECO:0000313|Proteomes:UP000000598}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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:0000256|RuleBase:RU004494}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|RuleBase:RU004494}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000256|RuleBase:RU004494}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU004495}. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein. CC {ECO:0000256|RuleBase:RU004494}. CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family. CC {ECO:0000256|ARBA:ARBA00010651}. 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; CR382125; CAH00060.1; -; Genomic_DNA. DR RefSeq; XP_454973.1; XM_454973.1. DR AlphaFoldDB; Q6CM66; -. DR STRING; 284590.Q6CM66; -. DR PaxDb; 284590-Q6CM66; -. DR GeneID; 2894414; -. DR KEGG; kla:KLLA0_E22573g; -. DR eggNOG; KOG1671; Eukaryota. DR HOGENOM; CLU_055690_0_1_1; -. DR InParanoid; Q6CM66; -. DR OMA; KRTWLIA; -. DR Proteomes; UP000000598; Chromosome E. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC. DR CDD; cd03470; Rieske_cytochrome_bc1; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR Gene3D; 1.20.5.270; Ubiquinol cytochrome reductase, transmembrane domain; 1. DR InterPro; IPR037008; bc1_Rieske_TM_sf. 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 PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 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 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Electron transport {ECO:0000256|RuleBase:RU004494}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Mitochondrion {ECO:0000256|RuleBase:RU004495}; KW Reference proteome {ECO:0000313|Proteomes:UP000000598}; KW Respiratory chain {ECO:0000256|RuleBase:RU004495}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Transport {ECO:0000256|RuleBase:RU004494}. FT DOMAIN 144..212 FT /note="Rieske" FT /evidence="ECO:0000259|PROSITE:PS51296" SQ SEQUENCE 213 AA; 22975 MW; 8D19EA3C8F4136A9 CRC64; MLGLRNGLKT GLKSVAPARL ISTSAVAAKS TYRTPDFGDY IKENNDADKG RSYAYFMVGS LGLLSSAGAK STVETFIASM SASADVLAMA KVEVNLAAIP EGKNVVVKWQ GKPVFIRHRT DHEIQEANSV DMSALKDPQT DSDRVQKPEW LVMLGICTHL GCVPIGESGD FGGWFCPCHG SHYDISGRIR KGPAPLNLEI PQYEFDGENL IVG //