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}.
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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
//