CYB_PLAFA
ID CYB_PLAFA Reviewed; 376 AA.
AC Q02768;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 falciparum.
OG Mitochondrion.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3054536; DOI=10.1016/0166-6851(88)90098-9;
RA Suplick K., Akella R., Saul A.J., Vaidya A.;
RT "Molecular cloning and partial sequence of a 5.8 kilobase pair repetitive
RT DNA from Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 30:289-290(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Camp / Malaysia;
RX PubMed=8459834; DOI=10.1016/0166-6851(93)90088-f;
RA Vaidya A.B., Lashgari M.S., Pologe L.G., Morrisey J.;
RT "Structural features of Plasmodium cytochrome b that may underlie
RT susceptibility to 8-aminoquinolines and hydroxynaphthoquinones.";
RL Mol. Biochem. Parasitol. 58:33-42(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-376.
RX PubMed=1542578; DOI=10.1093/nar/20.4.879;
RA Feagin J.E., Werner E., Gardner M.J., Williamson D.H., Wilson R.J.;
RT "Homologies between the contiguous and fragmented rRNAs of the two
RT Plasmodium falciparum extrachromosomal DNAs are limited to core
RT sequences.";
RL Nucleic Acids Res. 20:879-887(1992).
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 EMBL; M99416; AAC06270.1; -; Genomic_DNA.
DR EMBL; M76611; AAC63391.1; -; Genomic_DNA.
DR PIR; S28664; S28664.
DR RefSeq; NP_059668.1; NC_002375.1.
DR AlphaFoldDB; Q02768; -.
DR SMR; Q02768; -.
DR ChEMBL; CHEMBL1777; -.
DR DrugBank; DB01117; Atovaquone.
DR DrugCentral; Q02768; -.
DR GuidetoPHARMACOLOGY; 3087; -.
DR TCDB; 3.D.3.2.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR KEGG; pfa:PlfaoMp3; -.
DR VEuPathDB; PlasmoDB:PF3D7_MIT02300; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000005300; -.
DR VEuPathDB; PlasmoDB:Pf7G8_000015850; -.
DR VEuPathDB; PlasmoDB:PfDd2_000011300; -.
DR VEuPathDB; PlasmoDB:PfGA01_000021300; -.
DR VEuPathDB; PlasmoDB:PfGB4_000031700; -.
DR VEuPathDB; PlasmoDB:PfGN01_000029800; -.
DR VEuPathDB; PlasmoDB:PfHB3_000018900; -.
DR VEuPathDB; PlasmoDB:PfIT_000023800; -.
DR VEuPathDB; PlasmoDB:PfKE01_000017400; -.
DR VEuPathDB; PlasmoDB:PfKH01_000057100; -.
DR VEuPathDB; PlasmoDB:PfKH02_000021100; -.
DR VEuPathDB; PlasmoDB:PfML01_000121600; -.
DR VEuPathDB; PlasmoDB:PfNF135_000041300; -.
DR VEuPathDB; PlasmoDB:PfNF166_000018800; -.
DR VEuPathDB; PlasmoDB:PfNF54_000013000; -.
DR VEuPathDB; PlasmoDB:PfSD01_000015500; -.
DR VEuPathDB; PlasmoDB:PfSN01_000029400; -.
DR VEuPathDB; PlasmoDB:PfTG01_000076600; -.
DR PRO; PR:Q02768; -.
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 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; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 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..376
FT /note="Cytochrome b"
FT /id="PRO_0000061409"
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 169..189
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
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:0000250|UniProtKB:P00163"
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:0000250|UniProtKB:P00163"
FT BINDING 173
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 187
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 192
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 376 AA; 43377 MW; 80B9BD51CC450FAB CRC64;
MNFYSINLVK AHLINYPCPL NINFLWNYGF LLGIIFFIQI ITGVFLASRY TPDVSYAYYS
IQHILRELWS GWCFRYMHAT GASLVFLLTY LHILRGLNYS YMYLPLSWIS GLILFMIFIV
TAFVGYVLPW GQMSYWGATV ITNLLSSIPV AVIWICGGYT VSDPTIKRFF VLHFILPFIG
LCIVFIHIFF LHLHGSTNPL GYDTALKIPF YPNLLSLDVK GFNNVIILFL IQSLFGIIPL
SHPDNAIVVN TYVTPSQIVP EWYFLPFYAM LKTVPSKPAG LVIVLLSLQL LFLLAEQRSL
TTIIQFKMIF GARDYSVPII WFMCAFYALL WIGCQLPQDI FILYGRLFIV LFFCSGLFVL
VHYRRTHYDY SSQANI
