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   31-OCT-2006, entry version 35.
DE   Cytochrome b.
GN   Name=cob; Synonyms=cytB;
OS   Allomyces macrogynus.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Chytridiomycota; Blastocladiales; Blastocladiaceae;
OC   Allomyces.
OX   NCBI_TaxID=28583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=96226032; 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 (By similarity).
CC   -!- COFACTOR: Binds 2 heme groups non-covalently (By similarity).
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
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DR   EMBL; U41288; AAC49221.1; -; Genomic_DNA.
DR   PIR; S63638; S63638.
DR   HSSP; P00163; 1EZV.
DR   InterPro; IPR005798; Cytb_b6_C.
DR   InterPro; IPR005797; Cytb_b6_N.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrom_B_N; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
KW   Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Respiratory chain; Transmembrane; Transport.
FT   CHAIN         1    382       Cytochrome b.
FT                                /FTId=PRO_0000061733.
FT   METAL        82     82       Iron 1 (heme b562 axial ligand) (By
FT                                similarity).
FT   METAL        96     96       Iron 2 (heme b566 axial ligand) (By
FT                                similarity).
FT   METAL       183    183       Iron 1 (heme b562 axial ligand) (By
FT                                similarity).
FT   METAL       197    197       Iron 2 (heme b566 axial ligand) (By
FT                                similarity).
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
//