CYB_BRAPC
ID CYB_BRAPC Reviewed; 379 AA.
AC B1GYJ5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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:Cyt-b; Synonyms=Cob, cytb;
OS Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX NCBI_TaxID=10195;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NH1L;
RX PubMed=18326862; DOI=10.1093/molbev/msn058;
RA Suga K., Welch D.B.M., Tanaka Y., Sakakura Y., Hagiwara A.;
RT "Two circular chromosomes of unequal copy number make up the mitochondrial
RT genome of the rotifer Brachionus plicatilis.";
RL Mol. Biol. Evol. 25:1129-1137(2008).
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:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00163}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- CAUTION: The full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; AP009407; BAG12874.1; -; Genomic_DNA.
DR RefSeq; YP_001728980.1; NC_010472.1.
DR AlphaFoldDB; B1GYJ5; -.
DR SMR; B1GYJ5; -.
DR GeneID; 6054831; -.
DR CTD; 4519; -.
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; 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..379
FT /note="Cytochrome b"
FT /id="PRO_0000357458"
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 111..131
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 287..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 348..367
FT /note="Helical"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
FT BINDING 181
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:P00157"
FT BINDING 195
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:P00157"
FT BINDING 200
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 379 AA; 42970 MW; ECA19FF15FA34FF5 CRC64;
MSFRKTHPLI KIVNSTLVDL PSPANLSVNW NYGSLLGLVL VIQLITGIVL ATRFSGHSDM
SFDSVISIYQ DSNYGWLLRL VHSTGASFFF LFIYLHIGRG LYYGSYVYPE VWNIGVLIYL
ILMGTAFLGY VLPWGQMSYW AATVITNLLS AIPWLGPTMV EWVWGGFAVG NPTLTRFFAL
HYLLPFVVTA LVILHIFYLH IYGSSNPLGI SSNTNKVSFH YYYSVKDLYV YFVFFFVFMV
FTLKYGYVFM DAENFIPANP LVTPTHIQPE WYFLFAYAIL RSIPNKLGGV VGLLLAVLVL
FLFSVSTSKL LFSGTIYSPL ARLLYWSLVS NFFLLTWLGS CPAESPYNEV ALVATVTYFT
FMLTMCALPH ISTYLYLKS
