CYB_SCHPO
ID CYB_SCHPO Reviewed; 387 AA.
AC P05501;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 4.
DT 03-AUG-2022, entry version 145.
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; ORFNames=SPMIT.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD7-50;
RX PubMed=4046021; DOI=10.1016/0022-2836(85)90286-4;
RA Lang B.F., Ahne F., Bonen L.;
RT "The mitochondrial genome of the fission yeast Schizosaccharomyces pombe.
RT The cytochrome b gene has an intron closely related to the first two
RT introns in the Saccharomyces cerevisiae cox1 gene.";
RL J. Mol. Biol. 184:353-366(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD7-50;
RA Lang B.F.;
RT "The mitochondrial genome of Schizosaccharomyces pombe.";
RL (In) O'Brien S.J. (eds.);
RL Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL Press, New York (1993).
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; X02819; CAA26588.1; -; Genomic_DNA.
DR EMBL; X54421; CAA38287.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_039502.1; NC_001326.1.
DR AlphaFoldDB; P05501; -.
DR SMR; P05501; -.
DR STRING; 4896.SPMIT.05.1; -.
DR PaxDb; P05501; -.
DR EnsemblFungi; SPMIT.05.1; SPMIT.05.1:pep; SPMIT.05.
DR GeneID; 1669523; -.
DR KEGG; spo:ScpofMp04; -.
DR PomBase; SPMIT.05; -.
DR VEuPathDB; FungiDB:SPMIT.05; -.
DR eggNOG; KOG4663; Eukaryota.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P05501; -.
DR OMA; RFFAFHF; -.
DR PhylomeDB; P05501; -.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:P05501; -.
DR Proteomes; UP000002485; Mitochondrion.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; TAS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:PomBase.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; TAS:PomBase.
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; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..387
FT /note="Cytochrome b"
FT /id="PRO_0000061762"
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 387 AA; 43737 MW; 3C6EB9E3E4FC4494 CRC64;
MKILKSNPFL ALANNYMIDA PEPSNISYFW NFGSLLACVL VIQIVIGILL ACFYIPNMDL
AFLSVERIVR DVNYGFLLRA FHANGASFFF IFLYLHIGRG LYYGSYKYPR TMTWNIGVII
FLLTIITAFL GYCLPANQMS FWGATVITNL LSAVPFIGDD LVHLLWGGFS VSNPTLNRFF
SLHYLMPFVI AALSVMHLIA LHTNGSSNPL GVTANMDRIP MNPYYLIKDL ITIFIFLIGI
NYMAFYNPYG FMEPDCALPA DPLKTPMSIV PEWYLLPFYA ILRAIPNFQL GVIAMLLSIL
VLLLLPLLDF SAIRGNSFNP FGKFFFWTFV ADFVILAWIG GSHPENVFIT IGAIATIFYF
SYFFILIPVY TILGNTLIDL NLSSIKR
