CYB_CERSP
ID CYB_CERSP Reviewed; 445 AA.
AC Q02761;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytochrome b;
GN Name=petB; Synonyms=fbcB;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2176595; DOI=10.1111/j.1432-1033.1990.tb15633.x;
RA Yun C.-H., Beci R., Crofts A.R., Kaplan S., Gennis R.B.;
RT "Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1
RT complex from Rhodobacter sphaeroides. Characterization of fbc deletion
RT mutants and complementation by a site-specific mutational variant.";
RL Eur. J. Biochem. 194:399-411(1990).
RN [2]
RP TOPOLOGY.
RX PubMed=1645718; DOI=10.1016/s0021-9258(18)99114-3;
RA Yun C.H., Van Doren S.R., Crofts A.R., Gennis R.B.;
RT "The use of gene fusions to examine the membrane topology of the L-subunit
RT of the photosynthetic reaction center and of the cytochrome b subunit of
RT the bc1 complex from Rhodobacter sphaeroides.";
RL J. Biol. Chem. 266:10967-10973(1991).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 2 heme b groups non-covalently. {ECO:0000250};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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}.
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DR EMBL; X56157; CAA39624.1; -; Genomic_DNA.
DR PIR; S13869; S13869.
DR RefSeq; WP_002722007.1; NZ_WTFI01000004.1.
DR PDB; 2FYN; X-ray; 3.20 A; A/D/G/J/M/P=1-445.
DR PDB; 2QJK; X-ray; 3.10 A; A/D/G/J/M/P=3-430.
DR PDB; 2QJP; X-ray; 2.60 A; A/D/G/J=3-430.
DR PDB; 2QJY; X-ray; 2.40 A; A/D/G/J/M/P=1-445.
DR PDB; 5KKZ; X-ray; 2.97 A; A/E/K/O=1-445.
DR PDB; 5KLI; X-ray; 3.00 A; A/E/K/O=1-445.
DR PDBsum; 2FYN; -.
DR PDBsum; 2QJK; -.
DR PDBsum; 2QJP; -.
DR PDBsum; 2QJY; -.
DR PDBsum; 5KKZ; -.
DR PDBsum; 5KLI; -.
DR AlphaFoldDB; Q02761; -.
DR SMR; Q02761; -.
DR DIP; DIP-61256N; -.
DR IntAct; Q02761; 1.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB08690; Ubiquinone Q2.
DR TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family.
DR OrthoDB; 262439at2; -.
DR EvolutionaryTrace; Q02761; -.
DR GO; GO:0005886; C:plasma 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..445
FT /note="Cytochrome b"
FT /id="PRO_0000061774"
FT TOPO_DOM 2..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 68..94
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 114..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 150..193
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 217..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 253..270
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 271..329
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 330..346
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 347..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 383..388
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 409..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1645718"
FT BINDING 97
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 BINDING 111
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 BINDING 198
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 BINDING 212
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 HELIX 14..20
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 90..118
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2QJK"
FT HELIX 126..148
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 188..219
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 244..269
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 361..381
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:2QJY"
SQ SEQUENCE 445 AA; 50050 MW; 3DE9FB13523CDBD2 CRC64;
MSGIPHDHYE PRTGIEKWLH SRLPIVALAY DTIMIPTPRN LNWMWIWGVV LAFCLVLQIV
TGIVLAMHYT PHVDLAFASV EHIMRNVNGG FMLRYLHANG ASLFFIAVYL HIFRGLYYGS
YKAPREVTWI VGMLIYLAMM ATAFMGYVLP WGQMSFWGAT VITGLFGAIP GIGHSIQTWL
LGGPAVDNAT LNRFFSLHYL LPFVIAALVA IHIWAFHSTG NNNPTGVEVR RTSKAEAQKD
TVPFWPYFII KDVFALAVVL LVFFAIVGFM PNYLGHPDNY IEANPLSTPA HIVPEWYFLP
FYAILRAFTA DVWVVQIANF ISFGIIDAKF FGVLAMFGAI LVMALVPWLD TSPVRSGRYR
PMFKIYFWLL AADFVILTWV GAQQTTFPYD WISLIASAYW FAYFLVILPI LGAIEKPVAP
PATIEEDFNA HYSPATGGTK TVVAE
