ID   CYB_PLAGA               Reviewed;         300 AA.
AC   P81376;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Plasmodium gallinaceum.
OG   Mitochondrion.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX   NCBI_TaxID=5849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2779560; DOI=10.1128/mcb.9.9.3614-3620.1989;
RA   Aldritt S.M., Joseph J.T., Wirth D.F.;
RT   "Sequence identification of cytochrome b in Plasmodium gallinaceum.";
RL   Mol. Cell. Biol. 9:3614-3620(1989).
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   -!- 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 an even number of transmembrane helices,
CC       fewer than predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00163}.
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DR   PIR; A32566; A32566.
DR   AlphaFoldDB; P81376; -.
DR   SMR; P81376; -.
DR   VEuPathDB; PlasmoDB:PGAL8A_MIT00300; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   Gene3D; 1.20.810.10; -; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   InterPro; IPR027387; Cytb/b6-like_sf.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   SUPFAM; SSF81342; SSF81342; 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.
FT   CHAIN           1..300
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061410"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        72..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        168..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         78
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         92
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"
SQ   SEQUENCE   300 AA;  35019 MW;  7B5763BDA6794AE5 CRC64;
     MNYYSINLAK AHLLHYPCPL NINFLWNYGF LLGIVFFIQI LKGVLLALVI LQKLSYAYYS
     VQHILRAIMD GWCFRYMHAT GASFVFILTY LHILRGLNYS YSYLPLSWIS GLMIFLISIV
     TAFYGYVLPW GQMSFWNTTV ITNLLYLFRT CFMDCGGYLV SDPTLKRFFV FIYFPFIALC
     QSLFGILPLS HPDNAITVDR YATPLHIVPE WYFLPFYAML KTIPNKTAGL LVMLASLQIL
     FLLAEQRNLT TLIHFKFAFG AREYSVPTIC YMSSMLIWIG CQLPQILHFI WSFIYYIILF