ID CYB_CHEMY Reviewed; 381 AA. AC Q9TEC1; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 12-AUG-2020, entry version 96. DE RecName: Full=Cytochrome b; DE AltName: Full=Complex III subunit 3; DE AltName: Full=Complex III subunit III; DE AltName: Full=Cytochrome b-c1 complex subunit 3; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit; GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia; OC Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10368956; DOI=10.1093/oxfordjournals.molbev.a026163; RA Kumazawa Y., Nishida M.; RT "Complete mitochondrial DNA sequences of the green turtle and blue-tailed RT mole skink: statistical evidence for archosaurian affinity of turtles."; RL Mol. Biol. Evol. 16:784-792(1999). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex CC (complex III or cytochrome b-c1 complex) that is part of the CC mitochondrial respiratory chain. The b-c1 complex mediates electron CC transfer from ubiquinol to cytochrome c. Contributes to the generation CC of a proton gradient across the mitochondrial membrane that is then CC used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00157}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000250|UniProtKB:P00157}; CC -!- SUBUNIT: The cytochrome bc1 complex contains 3 respiratory subunits CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and CC probably 6 low-molecular weight proteins. CC {ECO:0000250|UniProtKB:P00157}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00157}. CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs CC at about 566 nm. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE- CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}. CC -!- CAUTION: The full-length protein contains only eight transmembrane CC helices, not nine as predicted by bioinformatics tools. CC {ECO:0000250|UniProtKB:P00157}. 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; AB012104; BAA79209.1; -; Genomic_DNA. DR RefSeq; NP_008776.1; NC_000886.1. DR SMR; Q9TEC1; -. DR GeneID; 808644; -. DR KEGG; cmy:808644; -. DR CTD; 4519; -. DR KO; K00412; -. DR OrthoDB; 1125966at2759; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR SUPFAM; SSF81648; SSF81648; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1..381 FT /note="Cytochrome b" FT /id="PRO_0000060775" FT TRANSMEM 34..54 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 78..99 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 227..247 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 289..309 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 321..341 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT TRANSMEM 348..368 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00157" FT METAL 84 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000250|UniProtKB:P00157" FT METAL 98 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000250|UniProtKB:P00157" FT METAL 183 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000250|UniProtKB:P00157" FT METAL 197 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000250|UniProtKB:P00157" FT BINDING 202 FT /note="Ubiquinone" FT /evidence="ECO:0000250|UniProtKB:P00157" SQ SEQUENCE 381 AA; 42859 MW; DE980F3AFE9E17D7 CRC64; MATNLRKTHP MMKIINNLVI DLPSPSNISA WWNFGSLLAT CLALQIITGI FLAMHYSPDI SMAFSSIAHI TRDVQYGWLI RNMHANGASL FFMCIYLHIG RGIYYGSYLY KETWNTGIIL LLLVMATAFV GYVLPWGQMS FWGATVITNL LSAIPYIGNT LVQWIWGGFS VDNATLTRFF TFHFLLPFAI TGLTAVHLLF LHETGSNNPT GLNSNTDKIP FHPYFSYKDL LGLILMLTFL LTLTLFSPYL LGDPDNFTPA NPLSTPPHIK PEWYFLFAYA ILRSIPNKLG GVLALLFSIL ILFLMPTLHT SKQRTASFRP LTQILFWSLV ADLLVLTWIG GQPVEDPFII IGQVASTFYF LILLLLMPAA GMIENKMLNL K //