CYB_MYZSE
ID CYB_MYZSE Reviewed; 377 AA.
AC A6MVL7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
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 Myzostoma seymourcollegiorum (Polychaete worm).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Myzostomida;
OC Myzostomatidae; Myzostoma.
OX NCBI_TaxID=447489;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17483114; DOI=10.1093/molbev/msm086;
RA Bleidorn C., Eeckhaut I., Podsiadlowski L., Schult N., McHugh D.,
RA Halanych K.M., Milinkovitch M.C., Tiedemann R.;
RT "Mitochondrial genome and nuclear sequence data support myzostomida as part
RT of the annelid radiation.";
RL Mol. Biol. Evol. 24:1690-1701(2007).
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: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
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 protein contains an even number of transmembrane helices,
CC fewer than predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00163}.
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DR EMBL; EF506562; ABR12404.1; -; Genomic_DNA.
DR AlphaFoldDB; A6MVL7; -.
DR SMR; A6MVL7; -.
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..377
FT /note="Cytochrome b"
FT /id="PRO_0000357463"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 86
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:P00163"
FT BINDING 100
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:P00163"
FT BINDING 185
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:P00163"
FT BINDING 199
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:P00163"
FT BINDING 204
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 377 AA; 43947 MW; 61A3DED0B5DD607B CRC64;
MNLKHPTRKD HILIKVVNNL LIDLPTPSNL SIMWNWGSLL GIFLIIPIIT GLFLAMHYTP
HMNLAFESIY HIMYDVNMGW LIRFIHVNGA SFFFIFLYLH MARGMYYYSF HYKEVWLIGC
TIYVVSMATA FMGYILPWGQ MSLWGATVIT NMLTTIPYLG QYLVQWIWGG FAVGNPTLNR
FFVLHFILPF IILALSIIHL IFLHSKGSTN PLGMNSNAYK IPFHPYYSSK DLMFLLLLMM
IMMVIIFWNP FLFMDAENSL EANFMKTPVH IKPEWYFLWV YTLLRSIPNK LGGVLTMVFS
ILILFLLPFI SNFNYITSMS MINKLLFWSF VVNMLILTWI GGMPVVPLFE TMGLTSTFLY
FIIILIYSNS FLMINKS
