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 22-NOV-2017, entry version 85. 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; Blastocladiomycota; Blastocladiomycetes; OC 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 CC complex (complex III or cytochrome b-c1 complex) that is part of CC the mitochondrial respiratory chain. The b-c1 complex mediates CC electron transfer from ubiquinol to cytochrome c. Contributes to CC the generation of a proton gradient across the mitochondrial CC membrane that is then used for ATP synthesis. CC {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 CC at about 562 nm, and heme 2 (or BH or b566) is high-potential and CC absorbs at about 566 nm. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000255|PROSITE-ProRule:PRU00967, ECO:0000255|PROSITE- CC ProRule:PRU00968}. CC -!- CAUTION: The protein contains only eight transmembrane helices, CC not 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 ProteinModelPortal; Q37395; -. DR SMR; Q37395; -. DR GeneID; 801884; -. 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; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; KW Transmembrane; Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 382 Cytochrome b. FT /FTId=PRO_0000061733. FT TRANSMEM 32 52 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 76 98 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 113 133 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 179 199 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 225 245 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 289 309 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 321 341 Helical. {ECO:0000250|UniProtKB:P00163}. FT TRANSMEM 348 368 Helical. {ECO:0000250|UniProtKB:P00163}. FT METAL 82 82 Iron 1 (heme b562 axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00968}. FT METAL 96 96 Iron 2 (heme b566 axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00968}. FT METAL 183 183 Iron 1 (heme b562 axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00968}. FT METAL 197 197 Iron 2 (heme b566 axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00968}. FT BINDING 202 202 Ubiquinone. FT {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 //