CYB_DROSI
ID CYB_DROSI Reviewed; 378 AA.
AC Q9MDZ9; Q9MD69; Q9ME00; Q9MGK5; Q9MGK9; Q9MI10;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Drosophila simulans (Fruit fly).
OG Mitochondrion {ECO:0000312|EMBL:AAF77458.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000312|EMBL:AAF77458.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C167, DSR, DSW, HW00, HW09, MD106, MD111, MD112, MD199, MD221,
RC MD225, MDW86, NC37, NC48, RU00, RU01, RU07, RU259, RU35, SC00, TT00, and
RC TT01;
RX PubMed=10903373; DOI=10.1007/s002390010067;
RA Ballard J.W.;
RT "Comparative genomics of mitochondrial DNA in Drosophila simulans.";
RL J. Mol. Evol. 51:64-75(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU023 {ECO:0000312|EMBL:AAR91451.1},
RC KY007 {ECO:0000312|EMBL:AAR91392.1}, KY045 {ECO:0000312|EMBL:AAR91412.1},
RC KY201 {ECO:0000312|EMBL:AAR91438.1}, and
RC KY215 {ECO:0000312|EMBL:AAR91425.1};
RX PubMed=14660690; DOI=10.1093/molbev/msh028;
RA Ballard J.W.O.;
RT "Sequential evolution of a symbiont inferred from the host: Wolbachia and
RT Drosophila simulans.";
RL Mol. Biol. Evol. 21:428-442(2004).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-378.
RX PubMed=12927135; DOI=10.1016/s1055-7903(03)00070-8;
RA Kastanis P., Eliopoulos E., Goulielmos G.N., Tsakas S., Loukas M.;
RT "Macroevolutionary relationships of species of Drosophila melanogaster
RT group based on mtDNA sequences.";
RL Mol. Phylogenet. Evol. 28:518-528(2003).
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:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250|UniProtKB:P00157}.
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, ECO:0000305}.
CC -!- CAUTION: The full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; AF200833; AAF77302.1; -; Genomic_DNA.
DR EMBL; AF200834; AAF77305.1; -; Genomic_DNA.
DR EMBL; AF200835; AAF77317.1; -; Genomic_DNA.
DR EMBL; AF200836; AAF77341.1; -; Genomic_DNA.
DR EMBL; AF200837; AAF77354.1; -; Genomic_DNA.
DR EMBL; AF200838; AAF77366.1; -; Genomic_DNA.
DR EMBL; AF200839; AAF77370.1; -; Genomic_DNA.
DR EMBL; AF200840; AAF77392.1; -; Genomic_DNA.
DR EMBL; AF200841; AAF77406.1; -; Genomic_DNA.
DR EMBL; AF200842; AAF77419.1; -; Genomic_DNA.
DR EMBL; AF200843; AAF77432.1; -; Genomic_DNA.
DR EMBL; AF200844; AAF77445.1; -; Genomic_DNA.
DR EMBL; AF200845; AAF77458.1; -; Genomic_DNA.
DR EMBL; AF200846; AAF77471.1; -; Genomic_DNA.
DR EMBL; AF200847; AAF77484.1; -; Genomic_DNA.
DR EMBL; AF200848; AAF77497.1; -; Genomic_DNA.
DR EMBL; AF200849; AAF77500.1; -; Genomic_DNA.
DR EMBL; AF200850; AAF77523.1; -; Genomic_DNA.
DR EMBL; AF200851; AAF77526.1; -; Genomic_DNA.
DR EMBL; AF200852; AAF77549.1; -; Genomic_DNA.
DR EMBL; AF200853; AAF77562.1; -; Genomic_DNA.
DR EMBL; AF200854; AAF77575.1; -; Genomic_DNA.
DR EMBL; AY518670; AAR91392.1; -; Genomic_DNA.
DR EMBL; AY518671; AAR91412.1; -; Genomic_DNA.
DR EMBL; AY518672; AAR91425.1; -; Genomic_DNA.
DR EMBL; AY518673; AAR91438.1; -; Genomic_DNA.
DR EMBL; AY518674; AAR91451.1; -; Genomic_DNA.
DR EMBL; AF164588; AAF81386.1; -; Genomic_DNA.
DR RefSeq; NP_982333.1; NC_005781.1.
DR AlphaFoldDB; Q9MDZ9; -.
DR SMR; Q9MDZ9; -.
DR STRING; 7240.Q9MDZ9; -.
DR GeneID; 2760965; -.
DR KEGG; dsi:CYTB; -.
DR CTD; 4519; -.
DR ChiTaRS; Cyt-b5-r; fly.
DR Proteomes; UP000000304; Mitochondrion.
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; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..378
FT /note="Cytochrome b"
FT /id="PRO_0000060896"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 84
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:P00157"
FT BINDING 98
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:P00157"
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:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
FT BINDING 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT VARIANT 71
FT /note="C -> Y (in strain: RU259)"
FT /evidence="ECO:0000305"
FT VARIANT 235
FT /note="V -> M (in strain: MD111, MD112, MD199, MD221,
FT MDW86, RU00, RU01, RU07 and RU259)"
FT /evidence="ECO:0000305"
FT VARIANT 357
FT /note="V -> I (in strain: NC37, NC48, TT00, TT01, HW00 and
FT HW09)"
FT /evidence="ECO:0000305"
FT VARIANT 370
FT /note="T -> M (in strain: NC37)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 43122 MW; 6DFEAAC86C9302EE CRC64;
MNKPLRNSHP LFKIANNALV DLPAPINISS WWNFGSLLGL CLIIQILTGL FLAMHYTADI
NLAFYSVNHI CRDVNYGWLL RTLHANGASF FFICIYLHVG RGIYYGSYMF TPTWLIGVII
LFLVMGTAFM GYVLPWGQMS FWGATVITNL LSAIPYLGMD LVQWLWGGFA VDNATLTRFF
TFHFILPFIV LAMTMIHLLF LHQTGSNNPI GLNSNIDKIP FHPYFTFKDI VGFIVMIFIL
ISLVLISPNL LGDPDNFIPA NPLVTPAHIQ PEWYFLFAYA ILRSIPNKLG GVIALVLSIA
ILMILPFYNL SKFRGIQFYP INQVMFWSML VTVILLTWIG ARPVEEPYVL IGQILTVVYF
LYYLVNPLIT KWWDNLLN
