CYB_CANPA
ID CYB_CANPA Reviewed; 384 AA.
AC Q7GEV4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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;
OS Candida parapsilosis (Yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR23 / CBS 7157;
RX PubMed=15449175; DOI=10.1007/s00438-004-1046-0;
RA Nosek J., Novotna M., Hlavatovicova Z., Ussery D.W., Fajkus J., Tomaska L.;
RT "Complete DNA sequence of the linear mitochondrial genome of the pathogenic
RT yeast Candida parapsilosis.";
RL Mol. Genet. Genomics 272:173-180(2004).
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; X74411; CAE54595.1; -; Genomic_DNA.
DR RefSeq; NP_943632.1; NC_005253.2.
DR AlphaFoldDB; Q7GEV4; -.
DR SMR; Q7GEV4; -.
DR GeneID; 2657775; -.
DR CGD; CAL0000145068; CapafMp03.
DR VEuPathDB; FungiDB:CapafMp03; -.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:EnsemblFungi.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
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..384
FT /note="Cytochrome b"
FT /id="PRO_0000061741"
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 384 AA; 43337 MW; 0617949489D2FA8A CRC64;
MPIRKSNTYL SLVNSYLIDS PQPSSINYWW NVGSLLGLCL VIQIASGIFL AMHYSSNIEL
AFNSVEHIMR DVNAGWLIRY IHANGASFFF ICMYLHIGKA LYYGSYKSPR VMLWVIGVII
FVVTMATAFM GYCLVYGQMS HWGATVITNL LSAIPFIGKD IVPFIWGGFS VSNPTIQRFF
ALHFLLPFIL AALVCMHLMA LHVNGSSNPL GITGNVDRLP MHPYFIFKDL VTVFVFLLVF
SLFVFYSPNT LGHPDNYIPG NPLVTPPSIV PEWYLLPFYA ILRSIPDKLG GVIAMFGAIL
ILLTLPYTDR SFIRGNSFKV LSKFMFFLFL FNFILLGNLG QLHVEVPYIE LGQYATAFYF
AYYLLIVPAI SSAENILYYI GTKK
