CYB_CANAL
ID CYB_CANAL Reviewed; 387 AA.
AC P0C8L0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, 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;
GN OrderedLocusNames=CM_00330W {ECO:0000312|CGD:CAL0000196083};
GN ORFNames=CaalfMp11;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=11208783; DOI=10.1128/jb.183.3.865-872.2001;
RA Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T.,
RA Kohn L.M.;
RT "Infrequent genetic exchange and recombination in the mitochondrial genome
RT of Candida albicans.";
RL J. Bacteriol. 183:865-872(2001).
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; AF285261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 7RJA; EM; 3.00 A; K/T=1-387.
DR PDB; 7RJB; EM; 3.20 A; K=1-387.
DR PDB; 7RJC; EM; 3.30 A; K=1-387.
DR PDB; 7RJD; EM; 3.20 A; K=1-387.
DR PDB; 7RJE; EM; 3.30 A; K/T=1-387.
DR PDBsum; 7RJA; -.
DR PDBsum; 7RJB; -.
DR PDBsum; 7RJC; -.
DR PDBsum; 7RJD; -.
DR PDBsum; 7RJE; -.
DR AlphaFoldDB; P0C8L0; -.
DR SMR; P0C8L0; -.
DR STRING; 237561.P0C8L0; -.
DR ChEMBL; CHEMBL4296307; -.
DR CGD; CAL0000196083; COB.
DR VEuPathDB; FungiDB:CM_00330W; -.
DR InParanoid; P0C8L0; -.
DR Proteomes; UP000000559; Mitochondrion.
DR GO; GO:0000792; C:heterochromatin; ISS:CGD.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISS:CGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; ISS:CGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISS:CGD.
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; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..387
FT /note="Cytochrome b"
FT /id="PRO_0000356872"
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"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7RJE"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 75..102
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 111..135
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 173..204
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7RJE"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 226..244
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:7RJE"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 366..382
FT /evidence="ECO:0007829|PDB:7RJA"
SQ SEQUENCE 387 AA; 43708 MW; 4F345A9AD99624F1 CRC64;
MPTRKSNTYL SLVNSYLIDS PQPSSINYWW NLGSLLGLCL VIQIASGVFL AMHYSSNIEL
AFDSVEHIMR DVNAGWLIRY IHANGASFFF ICMYLHIGKA LYYGSYKQPR VMLWVIGVVI
FILTMAIAFM GYCLVYGQMS HWGATVITNL LSAIPFIGND IVPFIWGGFS VSNPTIQRFF
ALHFLLPFIL AALVCMHLMA LHVHGSSNPV GITGNIDRLP MHPYFIFKDL ITVFVFLLIF
SLFVFYSPNT LGHPDNYIPG NPMVTPPSIV PEWYLLPFYA ILRSIPDKLG GVIAMFGAIL
ILLSLPYTDR SIIRGNSFKV LSKLAFYLFV FNFILLGNLG QLHVEVPYIQ LGQFATAYYF
AHYIIVVPVI STLENILYYI GTQTRVK
