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CYB_VICFA
ID   CYB_VICFA               Reviewed;         392 AA.
AC   P05718;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3405753; DOI=10.1093/nar/16.14.6897;
RA   Wahleithner J.A., Wolstenholme D.R.;
RT   "Ribosomal protein S14 genes in broad bean mitochondrial DNA.";
RL   Nucleic Acids Res. 16:6897-6913(1988).
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: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein. {ECO:0000250}.
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; X07237; CAA30226.1; -; Genomic_DNA.
DR   PIR; S01221; CBVF.
DR   AlphaFoldDB; P05718; -.
DR   SMR; P05718; -.
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..392
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061716"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        354..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   BINDING         88
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:0000250|UniProtKB:P00163"
FT   BINDING         102
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:0000250|UniProtKB:P00163"
FT   BINDING         189
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:0000250|UniProtKB:P00163"
FT   BINDING         203
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:0000250|UniProtKB:P00163"
FT   BINDING         208
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
SQ   SEQUENCE   392 AA;  44014 MW;  023D3396B2FA2BD3 CRC64;
     MTIRNQRLSL LKQPISSTLN QHLIDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY
     TPHVDLAFNS VEHVMRDVEG GWLLRYMHAN GASMFLIVVH LHIFRGLYHA SYSSPREFVR
     CLGVVIFLLM IVTAFTGYVP PWGQMSFWGA TVITSLASAI PVVGDTIVTW LWGGFSVDNA
     TLNRFFSLHH LLPFILVGAS LLHLAALHQY GSNNPLGVHS EMDQISFYPY FYVKDLVGWV
     AFAIFFSIWI FYAPNVLGHP DNYIPANPMP TPPHIVPEWY FLPIHAILRS IPDKSGGVAA
     IAPVFICLLA LPFFKSMYVR SSSFRPIHQG IFWLLLADRL LLGWIGCQPV EAPFVTIGQI
     PPFVFFLFFA ITPIPGRVGR GIPNSYTDET DQ
 
 
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