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CYB_ANOQU
ID   CYB_ANOQU               Reviewed;         378 AA.
AC   P33501;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 99.
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-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Anopheles quadrimaculatus (Common malaria mosquito).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Orlando;
RX   PubMed=2134168; DOI=10.1002/arch.940140104;
RA   Cockburn A.F., Mitchell S.E., Seawright J.A.;
RT   "Cloning of the mitochondrial genome of Anopheles quadrimaculatus.";
RL   Arch. Insect Biochem. Physiol. 14:31-36(1990).
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}.
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; L04272; AAA93551.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33501; -.
DR   SMR; P33501; -.
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..378
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060588"
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"
SQ   SEQUENCE   378 AA;  43536 MW;  6D0561FCB990EB9F CRC64;
     MFKPIRKTHP LISIANNALV DLPAPSNISA WWNFGSLLGL CLMLQILTGL FLAMHYAADI
     ETAFNSVNHI CRDVNNGWFL RICHANGASF FFACLFMHVG RGVYYESYLY HMTWNTGVII
     LFLTMATGFL GYVLPWGQMS FWGATVITNL LSAVPYLGMD LVQWIWGGFA VDNTTLTRFF
     TFHFIFPFII LALMMIHLLF LHQTGSNNPL GLNSNVDKIP FHPYFIYKDI FGFIVFYWIL
     IRFIWKFNYL LMDPENFIPA NPLVTPVHIQ PEWYFLFAYA ILRSIPNKLG GVIALVLSIA
     ILLILPFTHS SKFRGLQFYP LNQILFWNMV VVASLLTWIG ARPVEDPYVL TGQILTVLYF
     SYFIINPLLA KYWDKLLN
 
 
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