ID CYB_ALLMA Reviewed; 382 AA. AC Q37395; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-DEC-2019, entry version 89. 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=cob; Synonyms=cytB; OS Allomyces macrogynus. OG Mitochondrion. OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota; OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces. OX NCBI_TaxID=28583; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8636971; DOI=10.1006/jmbi.1996.0056; RA Paquin B., Lang B.F.; RT "The mitochondrial DNA of Allomyces macrogynus: the complete genomic RT sequence from an ancestral fungus."; RL J. Mol. Biol. 255:688-701(1996). 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:P00163}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00163}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000250|UniProtKB:P00163}; CC -!- SUBUNIT: Fungal cytochrome b-c1 complex contains 10 subunits; 3 CC respiratory subunits, 2 core proteins and 5 low-molecular weight CC proteins. Cytochrome b-c1 complex is a homodimer. CC {ECO:0000250|UniProtKB:P00163}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00163}. 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 protein contains only eight transmembrane helices, not CC nine as predicted by bioinformatics tools. CC {ECO:0000250|UniProtKB:P00163}. 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; U41288; AAC49221.1; -; Genomic_DNA. DR PIR; S63638; S63638. DR RefSeq; NP_043720.1; NC_001715.1. DR SMR; Q37395; -. DR GeneID; 801884; -. 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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; 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..382 FT /note="Cytochrome b" FT /id="PRO_0000061733" FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 76..98 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 289..309 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 321..341 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT TRANSMEM 348..368 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P00163" FT METAL 82 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968" FT METAL 96 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968" FT METAL 183 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968" FT METAL 197 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968" FT BINDING 202 FT /note="Ubiquinone" FT /evidence="ECO:0000250|UniProtKB:P00157" SQ SEQUENCE 382 AA; 43468 MW; A892A1A46A6915FA CRC64; MRFLKSHPVL SLANSFLIDS PLPSNITYLW NFGSLLGLCL VIQIVTGVTL AMHYAPSTSL AFVSVEHIMR DVFYGWLIRY AHANGASFFF ICVYIHMARG LYFNSYTKPR VLLWSVGVVI YILMMATAFL GYVLPWGQMS FWGATVITNL LSAIPYIGTA LVEFVWGGFS VDNATLNRFF SLHYLLPFIL AALVVVHLIA LHEHGSNNPL GISSKVDRLP FHPYFTYKDL VGFFVFFLIF FGFVFYQPNL MGHPDNYIPA NPLVTPVSIV PEWYFLPFYA ILRAIPSKLG GVIGMFGALL ILLALPWLET SKVRGAGFRP VMKFFFWLFV VNFFLLMYCG GQHAEEPFIT LSRICTAYYF MYFLVIIPVI GHLENLLHRC RD //