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 05-OCT-2016, entry version 80. 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), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. {ECO:0000250}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC Note=Binds 2 heme groups non-covalently. {ECO:0000250}; 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 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. 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 --------------------------------------------------------------------------- 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 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:0009055; F:electron carrier activity; 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; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like. 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. FT CHAIN 1 382 Cytochrome b. FT /FTId=PRO_0000061733. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TRANSMEM 262 282 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. 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}. 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 //