CYB_ASPNG
ID CYB_ASPNG Reviewed; 385 AA.
AC Q33798; Q3HM86;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=cobA, cytB;
OS Aspergillus niger.
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WU-2223L;
RA Narusawa T., Kanayama S., Kirimura K., Usami S.;
RT "Nucleotide sequence of the apocytochrome b gene of Aspergillus niger WU-
RT 2223L.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N909;
RA Juhasz A., Hamari Z., Kevei F., Pfeiffer I.;
RT "Aspergillus niger strain N909 complete mitochondrial genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 142-286.
RC STRAIN=IFM 40606, IFM 41398, IFM 41399, IFM 46897, IFM 5367, and IFM 5368;
RX PubMed=9776828; DOI=10.1080/02681219880000231;
RA Wang L., Yokoyama K., Miyaji M., Nishimura K.;
RT "The identification and phylogenetic relationship of pathogenic species of
RT Aspergillus based on the mitochondrial cytochrome b gene.";
RL Med. Mycol. 36:153-164(1998).
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; D63375; BAA09690.1; -; Genomic_DNA.
DR EMBL; DQ207726; ABA33721.1; -; Genomic_DNA.
DR EMBL; AB000575; BAA34142.1; -; Genomic_DNA.
DR EMBL; AB000576; BAA34143.1; -; Genomic_DNA.
DR EMBL; AB000577; BAA34144.1; -; Genomic_DNA.
DR EMBL; AB000578; BAA34145.1; -; Genomic_DNA.
DR EMBL; AB000583; BAA34150.2; -; Genomic_DNA.
DR EMBL; AB000597; BAA34162.1; -; Genomic_DNA.
DR RefSeq; YP_337876.1; NC_007445.1.
DR AlphaFoldDB; Q33798; -.
DR SMR; Q33798; -.
DR GeneID; 3703570; -.
DR KEGG; ang:Asnifp01; -.
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; 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..385
FT /note="Cytochrome b"
FT /id="PRO_0000061737"
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 226..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 349..369
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 CONFLICT 99
FT /note="R -> G (in Ref. 2; ABA33721)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> F (in Ref. 2; ABA33721)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> F (in Ref. 2; ABA33721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43078 MW; 73980B1D34386EF3 CRC64;
MRILKSHPLL KIVNSYMIDS PQPANISYLW NFGSLLALCL GIQIVTGVTL AMHYTPSVLE
AFNSVEHIMR DVNNGWLVRY LHANTASAFF FLVYLHIGRG LYYGSYKSPR TLTWAIGTVI
LIVMMATAFL GYVLPYGQMS LWGATVITNL MSAIPWIGQD IVEFIWGGFS VNNATLNRFF
ALHFLLPFVL AALALMHLIA MHDTVGSGNP LGISGNYDRL PFAPYFIFKD LVTIFIFFIV
LSIFVFFMPN ALGDSENYVM ANPMQTPPAI VPEWYLLPFY AILRSIPNKL LGVIAMFSAI
LALMVMPITD LSKLRGVQFR PLSKVAFYIF VANFLVLMQI GAKHVETPFI ELGQISTVLY
LAHFLVIVPV VSLIENSLVE LATKK
