CYB_YEAST
ID CYB_YEAST Reviewed; 385 AA.
AC P00163; A0A0A7NYK0; Q35802; Q35807; Q36301; Q9ZZW9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Cytochrome b;
DE EC=7.1.1.8 {ECO:0000269|PubMed:2551731, ECO:0000269|PubMed:8031140};
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit CYTB;
DE AltName: Full=Complex III subunit III;
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Cytochrome b-c1 complex subunit CYTB;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase complex cytochrome b subunit;
GN Name=COB; Synonyms=CYTB; OrderedLocusNames=Q0105;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A21;
RX PubMed=6253454; DOI=10.1016/s0021-9258(18)43467-9;
RA Nobrega F.G., Tzagoloff A.;
RT "Assembly of the mitochondrial membrane system. DNA sequence and
RT organization of the cytochrome b gene in Saccharomyces cerevisiae D273-
RT 10B.";
RL J. Biol. Chem. 255:9828-9837(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A21;
RX PubMed=6383504;
RA Bonjardim C.A., Nobrega F.G.;
RT "Revision of the nucleotide sequence at the last intron of the
RT mitochondrial apocytochrome b gene in Saccharomyces cerevisiae.";
RL Braz. J. Med. Biol. Res. 17:17-20(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WR200;
RX PubMed=7737175; DOI=10.1111/j.1432-1033.1995.0762m.x;
RA Claros M.G., Perea J., Shu Y., Samatey F.A., Popot J.-L., Jacq C.;
RT "Limitations to in vivo import of hydrophobic proteins into yeast
RT mitochondria. The case of a cytoplasmically synthesized apocytochrome b.";
RL Eur. J. Biochem. 228:762-771(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-143.
RC STRAIN=ATCC 44821 / 777-3A;
RX PubMed=7004642; DOI=10.1016/0092-8674(80)90344-x;
RA Lazowska J., Jacq C., Slonimski P.P.;
RT "Sequence of introns and flanking exons in wild-type and box3 mutants of
RT cytochrome b reveals an interlaced splicing protein coded by an intron.";
RL Cell 22:333-348(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-169.
RC STRAIN=ATCC 44821 / 777-3A;
RX PubMed=7034963; DOI=10.1016/0092-8674(81)90355-x;
RA Lazowska J., Jacq C., Slonimski P.P.;
RT "Splice points of the third intron in the yeast mitochondrial cytochrome b
RT gene.";
RL Cell 27:12-14(1981).
RN [8]
RP MUTANT W7, AND FUNCTION.
RX PubMed=2551731; DOI=10.1016/0014-5793(89)81050-6;
RA Brivet-Chevillotte P., di Rago J.-P.;
RT "Electron-transfer restoration by vitamin K3 in a complex III-deficient
RT mutant of S. cerevisiae and sequence of the corresponding cytochrome b
RT mutation.";
RL FEBS Lett. 255:5-9(1989).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND PROTEIN SEQUENCE OF 66-76.
RX PubMed=8031140; DOI=10.1006/abbi.1994.1312;
RA Beattie D.S., Jenkins H.C., Howton M.M.;
RT "Biochemical evidence for the orientation of cytochrome b in the yeast
RT mitochondrial membrane in the eight-helix model.";
RL Arch. Biochem. Biophys. 312:292-300(1994).
RN [10]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [11]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER
RP SUBUNITS OF THE BC1 COMPLEX, COFACTOR, TOPOLOGY, AND SUBUNIT.
RX PubMed=10873857; DOI=10.1016/s0969-2126(00)00152-0;
RA Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
RT "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast
RT Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.";
RL Structure 8:669-684(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER
RP SUBUNITS OF THE BC1 COMPLEX, COFACTOR, TOPOLOGY, AND SUBUNIT.
RX PubMed=11880631; DOI=10.1073/pnas.052704699;
RA Lange C., Hunte C.;
RT "Crystal structure of the yeast cytochrome bc1 complex with its bound
RT substrate cytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA Solmaz S.R., Hunte C.;
RT "Structure of complex III with bound cytochrome c in reduced state and
RT definition of a minimal core interface for electron transfer.";
RL J. Biol. Chem. 283:17542-17549(2008).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS) IN COMPLEX WITH HEME AND
RP UBIQUINONE.
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH HEME AND
RP UBIQUINONE.
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (Probable). Cytochrome b is a catalytic core
CC subunit containing 2 b-type hemes BL and BH topographically segregated
CC in the quinone reduction (Qi) and quinol oxidation (Q0) sites on
CC opposite sides of the membrane (PubMed:18390544).
CC {ECO:0000269|PubMed:18390544, ECO:0000305|PubMed:11880631,
CC ECO:0000305|PubMed:2551731, ECO:0000305|PubMed:8031140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:2551731,
CC ECO:0000269|PubMed:8031140};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC Note=Binds 2 heme b groups non-covalently per subunit.
CC {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein
CC (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular
CC weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10
CC (PubMed:10873857, PubMed:11880631, PubMed:8031140, PubMed:30598554).
CC The complex exists as an obligatory dimer and forms supercomplexes
CC (SCs) in the inner mitochondrial membrane with a monomer or a dimer of
CC cytochrome c oxidase (complex IV, CIV), resulting in 2 different
CC assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262,
CC PubMed:10764779, PubMed:30598556, PubMed:30598554).
CC {ECO:0000269|PubMed:10764779, ECO:0000269|PubMed:10775262,
CC ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556,
CC ECO:0000269|PubMed:8031140}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:8031140}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:8031140}.
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}.
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DR EMBL; V00696; CAA24073.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X84042; CAA58861.1; -; mRNA.
DR EMBL; KP263414; AIZ98890.1; -; Genomic_DNA.
DR EMBL; J01473; AAA32151.2; -; Genomic_DNA.
DR EMBL; J01472; AAA32151.2; JOINED; Genomic_DNA.
DR EMBL; J01475; AAA32152.2; -; Genomic_DNA.
DR EMBL; J01474; AAA32152.2; JOINED; Genomic_DNA.
DR PIR; A00159; CBBY.
DR PIR; S78660; S78660.
DR RefSeq; NP_009315.1; NC_001224.1.
DR PDB; 1EZV; X-ray; 2.30 A; C=1-385.
DR PDB; 1KB9; X-ray; 2.30 A; C=1-385.
DR PDB; 1KYO; X-ray; 2.97 A; C/N=1-385.
DR PDB; 1P84; X-ray; 2.50 A; C=1-385.
DR PDB; 2IBZ; X-ray; 2.30 A; C=1-385.
DR PDB; 3CX5; X-ray; 1.90 A; C/N=1-385.
DR PDB; 3CXH; X-ray; 2.50 A; C/N=1-385.
DR PDB; 4PD4; X-ray; 3.04 A; C=1-385.
DR PDB; 6GIQ; EM; 3.23 A; C/N=1-385.
DR PDB; 6HU9; EM; 3.35 A; C/N=1-385.
DR PDB; 6T0B; EM; 2.80 A; C/N=1-385.
DR PDB; 6T15; EM; 3.29 A; C/N=1-385.
DR PDB; 6YMX; EM; 3.17 A; C/N=1-385.
DR PDBsum; 1EZV; -.
DR PDBsum; 1KB9; -.
DR PDBsum; 1KYO; -.
DR PDBsum; 1P84; -.
DR PDBsum; 2IBZ; -.
DR PDBsum; 3CX5; -.
DR PDBsum; 3CXH; -.
DR PDBsum; 4PD4; -.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR AlphaFoldDB; P00163; -.
DR SMR; P00163; -.
DR BioGRID; 34779; 38.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR IntAct; P00163; 4.
DR STRING; 4932.Q0105; -.
DR ChEMBL; CHEMBL4296317; -.
DR TCDB; 3.D.3.3.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P00163; -.
DR TopDownProteomics; P00163; -.
DR EnsemblFungi; Q0105_mRNA; Q0105; Q0105.
DR GeneID; 854583; -.
DR KEGG; sce:Q0105; -.
DR SGD; S000007270; COB.
DR VEuPathDB; FungiDB:Q0105; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P00163; -.
DR OMA; RFFAFHF; -.
DR BioCyc; MetaCyc:Q0105-MON; -.
DR BioCyc; YEAST:Q0105-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P00163; -.
DR PRO; PR:P00163; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P00163; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IDA:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..385
FT /note="Cytochrome b"
FT /id="PRO_0000061769"
FT TOPO_DOM 1..27
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 52..74
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 75..102
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 103..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 111..135
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 136..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 173..204
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 205..223
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 247..287
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 309..319
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 341..347
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT TRANSMEM 348..364
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:3CX5"
FT TOPO_DOM 365..385
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000305|PubMed:8031140"
FT BINDING 16
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:30598554"
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:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
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:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
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:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
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:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT BINDING 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT VARIANT 131
FT /note="G -> S (in mutant W7 which is respiratory
FT deficient)"
FT CONFLICT 122
FT /note="I -> T (in Ref. 3; CAA58861 and 6; AAA32151)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> ID (in Ref. 1; CAA24073 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 75..102
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1KYO"
FT HELIX 111..135
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 173..204
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6YMX"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 320..340
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 366..380
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 385 AA; 43656 MW; 1B1B1616BBC2A798 CRC64;
MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM AMHYSSNIEL
AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG LYYGSYRSPR VTLWNVGVII
FILTIATAFL GYCCVYGQMS HWGATVITNL FSAIPFVGND IVSWLWGGFS VSNPTIQRFF
ALHYLVPFII AAMVIMHLMA LHIHGSSNPL GITGNLDRIP MHSYFIFKDL VTVFLFMLIL
ALFVFYSPNT LGHPDNYIPG NPLVTPASIV PEWYLLPFYA ILRSIPDKLL GVITMFAAIL
VLLVLPFTDR SVVRGNTFKV LSKFFFFIFV FNFVLLGQIG ACHVEVPYVL MGQIATFIYF
AYFLIIVPVI STIENVLFYI GRVNK
