CYB_TOXGO
ID CYB_TOXGO Reviewed; 368 AA.
AC O20672; O20928;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-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 Toxoplasma gondii.
OG Mitochondrion.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Toursel C., Tomavo S.;
RT "Cytochrome B of Toxoplasma gondii.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-368.
RC STRAIN=RH;
RA McFadden D.C., Boothroyd J.C.;
RT "Cytochrome B gene from Toxoplasma gondii.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AF015627; AAB82741.1; -; mRNA.
DR EMBL; AF023246; AAC34138.1; -; mRNA.
DR AlphaFoldDB; O20672; -.
DR SMR; O20672; -.
DR EnsemblProtists; TGME49_330000-t26_1; TGME49_330000-t26_1-p1-CDS1; TGME49_330000.
DR VEuPathDB; ToxoDB:TGCOUG_364120; -.
DR VEuPathDB; ToxoDB:TGDOM2_322200; -.
DR VEuPathDB; ToxoDB:TGFOU_322210; -.
DR VEuPathDB; ToxoDB:TGGT1_362110; -.
DR VEuPathDB; ToxoDB:TGGT1_409830; -.
DR VEuPathDB; ToxoDB:TGMAS_330000; -.
DR VEuPathDB; ToxoDB:TGME49_330000; -.
DR VEuPathDB; ToxoDB:TGP89_422500; -.
DR VEuPathDB; ToxoDB:TGPRC2_423410; -.
DR VEuPathDB; ToxoDB:TGPRC2_423590; -.
DR VEuPathDB; ToxoDB:TGRH88_085320; -.
DR VEuPathDB; ToxoDB:TGRUB_322210; -.
DR VEuPathDB; ToxoDB:TGRUB_364800; -.
DR VEuPathDB; ToxoDB:TGVAND_237130; -.
DR VEuPathDB; ToxoDB:TGVAND_438480; -.
DR VEuPathDB; ToxoDB:TGVEG_239300B; -.
DR VEuPathDB; ToxoDB:TGVEG_322200; -.
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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..368
FT /note="Cytochrome b"
FT /id="PRO_0000061672"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 82
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 96
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 178
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 192
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 197
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 368 AA; 41595 MW; CC7C6BD3784287CA CRC64;
MVSRTLSLSM SLFRAHLVFY RCALNLNSSY NFGFLVAMTF VLQIITGITL AFRYTSEASC
AFASVQHLVR EVAAGWEFRM LHATTASFVF LCILIHMTRG LYNWSYSYLT TAWMSGLVLY
LLTIATAFLG YVLPWGQMSF WGATVITNLL SPIPYLVPWL LGGYYVSDVT LKRFFVLHFI
LPFIGCIIIV LHIFYLHLNG SSNPAGIDTA LKVAFYPHML MTDAKCLSYL IGLIFLQAAF
GLMELSHPDN SIPVNRFVTP LHIVPEWYFL AYYAVLKVIP SKTGGLLVFM SSLINLGLLS
EIRALNTRML IRQQFMTRNV VSGWVIIWVY SMIFLIIIGS AIPQATYILY GRLATILYLT
TGLVLCLY
