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CYB_RHIOR
ID   CYB_RHIOR               Reviewed;         386 AA.
AC   Q3T4F1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 148428;
RX   PubMed=15689432; DOI=10.1093/nar/gki199;
RA   Seif E., Leigh J., Liu Y., Roewer I., Forget L., Lang B.F.;
RT   "Comparative mitochondrial genomics in zygomycetes: bacteria-like RNase P
RT   RNAs, mobile elements, and a close source of the group I intron invasion in
RT   angiosperms.";
RL   Nucleic Acids Res. 33:734-744(2005).
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 b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00163};
CC       Note=Binds 2 heme b 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}.
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DR   EMBL; AY863212; AAW49472.1; -; Genomic_DNA.
DR   RefSeq; YP_203305.1; NC_006836.1.
DR   AlphaFoldDB; Q3T4F1; -.
DR   SMR; Q3T4F1; -.
DR   GeneID; 3260154; -.
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:0022904; P:respiratory electron transport chain; 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..386
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061755"
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   BINDING         82
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         96
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         183
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         197
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         202
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
SQ   SEQUENCE   386 AA;  43731 MW;  77D9BD6F5B63B3B1 CRC64;
     MKLLKSHPFL SLANSYVIDS PQPSNLNYAW NFGSLLALCL GIQIVTGVTL AMHYTPNIDL
     AFISVEHIMR DVNYGWMIRY LHANTASFFF LFVYLHIGRG LYYGSYKSPR ALPWSIGVII
     LILMMATAFL GYVLPWGQMS LWGATVITNL LSAIPWIGKD LVEFIWGGFS VDNATLNRFF
     SLHYLLPFIL AALAVMHLLA LHEHGSSNPL GITANADRLY MHPYYTFKDL VTIFLFFLVL
     ALFLFYAPNK LGHPDNYIPA NPMQTPASIV PEWYLLPFYA ILRSIPDKLG GVIAMFGSLL
     ILLAMPLLDL SRVRGSAFRP LMKFFFWLLV VDFLILLWCG SQHVEEPFIT LGQFATTFYF
     SWFLIIVPVV SVIENTLIDL ATENKS
 
 
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