CYB_BOVIN
ID CYB_BOVIN Reviewed; 379 AA.
AC P00157; Q8SE06;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 169.
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 Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1901092; DOI=10.1007/bf02515385;
RA Irwin D.M., Kocher T.D., Wilson A.C.;
RT "Evolution of the cytochrome b gene of mammals.";
RL J. Mol. Evol. 32:128-144(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1225597; DOI=10.1016/0014-5793(75)80219-5;
RA Vail W.J., Riley R.K., Rieske J.S.;
RT "Fine structure of beef heart mitochondrial complex III.";
RL FEBS Lett. 58:33-38(1975).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=189810; DOI=10.1016/0005-2728(77)90026-3;
RA Riccio P., Schaegger H., Engel W.D., Von Jagow G.;
RT "bc1-complex from beef heart. One-step purification by hydroxyapatite
RT chromatography in Triton X-100, polypeptide pattern and respiratory chain
RT characteristics.";
RL Biochim. Biophys. Acta 459:250-262(1977).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1327781; DOI=10.1111/j.1432-1033.1992.tb17312.x;
RA Cocco T., Lorusso M., Di Paola M., Minuto M., Papa S.;
RT "Characteristics of energy-linked proton translocation in liposome
RT reconstituted bovine cytochrome bc1 complex. Influence of the protonmotive
RT force on the H+/e- stoichiometry.";
RL Eur. J. Biochem. 209:475-481(1992).
RN [7]
RP FUNCTION.
RX PubMed=9485330; DOI=10.1021/bi9724164;
RA Cocco T., Di Paola M., Papa S., Lorusso M.;
RT "Chemical modification of the bovine mitochondrial bc1 complex reveals
RT critical acidic residues involved in the proton pumping activity.";
RL Biochemistry 37:2037-2043(1998).
RN [8]
RP FUNCTION.
RX PubMed=20025846; DOI=10.1016/j.bbabio.2009.12.003;
RA Berry E.A., Huang L.S., Lee D.W., Daldal F., Nagai K., Minagawa N.;
RT "Ascochlorin is a novel, specific inhibitor of the mitochondrial cytochrome
RT bc1 complex.";
RL Biochim. Biophys. Acta 1797:360-370(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH THE CYTOCHROME BC1
RP COMPLEX AND HEME, SUBUNIT, TOPOLOGY, AND COFACTOR.
RX PubMed=9204897; DOI=10.1126/science.277.5322.60;
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RT "Crystal structure of the cytochrome bc1 complex from bovine heart
RT mitochondria.";
RL Science 277:60-66(1997).
RN [10] {ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH THE CYTOCHROME BC1
RP COMPLEX AND HEME, SUBUNIT, TOPOLOGY, AND COFACTOR.
RX PubMed=9651245; DOI=10.1126/science.281.5373.64;
RA Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A.,
RA Ramaswamy S., Jap B.K.;
RT "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1
RT complex.";
RL Science 281:64-71(1998).
RN [11] {ECO:0007744|PDB:1L0L, ECO:0007744|PDB:1L0N}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE CYTOCHROME BC1
RP COMPLEX AND HEME, SUBUNIT, TOPOLOGY, AND COFACTOR.
RX PubMed=12269811; DOI=10.1021/bi026252p;
RA Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L.,
RA Xia D.;
RT "The crystal structure of mitochondrial cytochrome bc1 in complex with
RT famoxadone: the role of aromatic-aromatic interaction in inhibition.";
RL Biochemistry 41:11692-11702(2002).
RN [12] {ECO:0007744|PDB:1SQB, ECO:0007744|PDB:1SQP, ECO:0007744|PDB:1SQQ, ECO:0007744|PDB:1SQV, ECO:0007744|PDB:1SQX}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP SUBUNIT, TOPOLOGY, AND COFACTOR.
RX PubMed=15312779; DOI=10.1016/j.jmb.2004.05.065;
RA Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.;
RT "Crystallographic studies of quinol oxidation site inhibitors: a modified
RT classification of inhibitors for the cytochrome bc(1) complex.";
RL J. Mol. Biol. 341:281-302(2004).
RN [13] {ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1PPJ, ECO:0007744|PDB:2A06}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP SUBUNIT, TOPOLOGY, AND COFACTOR.
RX PubMed=16024040; DOI=10.1016/j.jmb.2005.05.053;
RA Huang L.S., Cobessi D., Tung E.Y., Berry E.A.;
RT "Binding of the respiratory chain inhibitor antimycin to the mitochondrial
RT bc1 complex: a new crystal structure reveals an altered intramolecular
RT hydrogen-bonding pattern.";
RL J. Mol. Biol. 351:573-597(2005).
RN [14] {ECO:0007744|PDB:2FYU}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT,
RP TOPOLOGY, AND COFACTOR.
RX PubMed=16924113; DOI=10.1073/pnas.0601149103;
RA Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.;
RT "Surface-modulated motion switch: capture and release of iron-sulfur
RT protein in the cytochrome bc1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006).
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:0000269|PubMed:1327781,
CC ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:9485330,
CC ECO:0000305|PubMed:189810}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
CC ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
CC ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
CC ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
CC ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245};
CC -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory
CC subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC UQCRFS1). This cytochrome bc1 complex then forms a dimer.
CC {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
CC ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
CC ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245,
CC ECO:0000305|PubMed:189810}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:1225597, ECO:0000305|PubMed:1327781,
CC ECO:0000305|PubMed:189810}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
CC ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
CC ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}.
CC -!- TISSUE SPECIFICITY: Detected in heart (at protein level).
CC {ECO:0000269|PubMed:1225597, ECO:0000269|PubMed:1327781,
CC ECO:0000269|PubMed:189810}.
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.
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:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
CC ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
CC ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}.
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DR EMBL; V00654; CAA24007.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08329.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08342.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12801.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12814.1; -; Genomic_DNA.
DR PIR; A00152; CBBO.
DR RefSeq; YP_209217.1; NC_006853.1.
DR PDB; 1BE3; X-ray; 3.00 A; C=1-379.
DR PDB; 1BGY; X-ray; 3.00 A; C/O=1-379.
DR PDB; 1L0L; X-ray; 2.35 A; C=1-379.
DR PDB; 1L0N; X-ray; 2.60 A; C=1-379.
DR PDB; 1NTK; X-ray; 2.60 A; C=1-379.
DR PDB; 1NTM; X-ray; 2.40 A; C=1-379.
DR PDB; 1NTZ; X-ray; 2.60 A; C=1-379.
DR PDB; 1NU1; X-ray; 3.20 A; C=1-379.
DR PDB; 1PP9; X-ray; 2.10 A; C/P=1-379.
DR PDB; 1PPJ; X-ray; 2.10 A; C/P=1-379.
DR PDB; 1QCR; X-ray; 2.70 A; C=2-379.
DR PDB; 1SQB; X-ray; 2.69 A; C=1-379.
DR PDB; 1SQP; X-ray; 2.70 A; C=1-379.
DR PDB; 1SQQ; X-ray; 3.00 A; C=1-379.
DR PDB; 1SQV; X-ray; 2.85 A; C=1-379.
DR PDB; 1SQX; X-ray; 2.60 A; C=1-379.
DR PDB; 2A06; X-ray; 2.10 A; C/P=1-379.
DR PDB; 2FYU; X-ray; 2.26 A; C=1-379.
DR PDB; 2YBB; EM; 19.00 A; C/c=1-379.
DR PDB; 4D6T; X-ray; 3.57 A; C/P=1-379.
DR PDB; 4D6U; X-ray; 4.09 A; C/P=1-379.
DR PDB; 5GPN; EM; 5.40 A; C/O=1-379.
DR PDB; 5KLV; X-ray; 2.65 A; C=1-379.
DR PDB; 5LUF; EM; 9.10 A; b/o=1-379.
DR PDB; 5NMI; X-ray; 3.50 A; C/P=8-379.
DR PDB; 5OKD; X-ray; 3.10 A; C=1-379.
DR PDB; 6FO0; EM; 4.10 A; C/P=1-379.
DR PDB; 6FO2; EM; 4.40 A; C/P=1-379.
DR PDB; 6FO6; EM; 4.10 A; C/P=1-379.
DR PDB; 6HAW; X-ray; 3.45 A; C=2-379.
DR PDB; 6NHG; X-ray; 2.80 A; C=1-379.
DR PDB; 6XVF; X-ray; 3.50 A; C=2-379.
DR PDB; 6ZFS; X-ray; 3.50 A; C=2-379.
DR PDB; 6ZFT; X-ray; 3.30 A; C=2-379.
DR PDB; 6ZFU; X-ray; 3.50 A; C=2-379.
DR PDBsum; 1BE3; -.
DR PDBsum; 1BGY; -.
DR PDBsum; 1L0L; -.
DR PDBsum; 1L0N; -.
DR PDBsum; 1NTK; -.
DR PDBsum; 1NTM; -.
DR PDBsum; 1NTZ; -.
DR PDBsum; 1NU1; -.
DR PDBsum; 1PP9; -.
DR PDBsum; 1PPJ; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2A06; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 4D6T; -.
DR PDBsum; 4D6U; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 5OKD; -.
DR PDBsum; 6FO0; -.
DR PDBsum; 6FO2; -.
DR PDBsum; 6FO6; -.
DR PDBsum; 6HAW; -.
DR PDBsum; 6NHG; -.
DR PDBsum; 6XVF; -.
DR PDBsum; 6ZFS; -.
DR PDBsum; 6ZFT; -.
DR PDBsum; 6ZFU; -.
DR AlphaFoldDB; P00157; -.
DR SMR; P00157; -.
DR CORUM; P00157; -.
DR DIP; DIP-350N; -.
DR IntAct; P00157; 2.
DR STRING; 9913.ENSBTAP00000053148; -.
DR TCDB; 3.D.3.2.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P00157; -.
DR Ensembl; ENSBTAT00000060567; ENSBTAP00000053148; ENSBTAG00000043550.
DR GeneID; 3283889; -.
DR KEGG; bta:3283889; -.
DR CTD; 4519; -.
DR VEuPathDB; HostDB:ENSBTAG00000043550; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P00157; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR TreeFam; TF353088; -.
DR EvolutionaryTrace; P00157; -.
DR PRO; PR:P00157; -.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043550; Expressed in cardiac ventricle and 102 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0098573; C:intrinsic component of mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
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:0048039; F:ubiquinone binding; IDA:UniProtKB.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; 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; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..379
FT /note="Cytochrome b"
FT /id="PRO_0000060686"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:1L0L"
FT BINDING 83
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 ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779,
FT ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113,
FT ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1L0L, ECO:0007744|PDB:1L0N,
FT ECO:0007744|PDB:1NTK, ECO:0007744|PDB:1NTM,
FT ECO:0007744|PDB:1NTZ, ECO:0007744|PDB:1NU1,
FT ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1PPJ,
FT ECO:0007744|PDB:1SQB, ECO:0007744|PDB:1SQP,
FT ECO:0007744|PDB:1SQQ, ECO:0007744|PDB:1SQV,
FT ECO:0007744|PDB:1SQX, ECO:0007744|PDB:2A06,
FT ECO:0007744|PDB:2FYU, ECO:0007744|PDB:2YBB,
FT ECO:0007744|PDB:4D6T, ECO:0007744|PDB:4D6U"
FT BINDING 97
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:12269811,
FT ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040,
FT ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897,
FT ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3,
FT ECO:0007744|PDB:1BGY, ECO:0007744|PDB:1L0L,
FT ECO:0007744|PDB:1L0N, ECO:0007744|PDB:1NTK,
FT ECO:0007744|PDB:1NTM, ECO:0007744|PDB:1NTZ,
FT ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1PPJ,
FT ECO:0007744|PDB:1SQB, ECO:0007744|PDB:1SQP,
FT ECO:0007744|PDB:1SQQ, ECO:0007744|PDB:1SQV,
FT ECO:0007744|PDB:1SQX, ECO:0007744|PDB:2A06,
FT ECO:0007744|PDB:2FYU, ECO:0007744|PDB:2YBB,
FT ECO:0007744|PDB:4D6T, ECO:0007744|PDB:4D6U"
FT BINDING 182
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:12269811,
FT ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040,
FT ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897,
FT ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1L0N,
FT ECO:0007744|PDB:1NTK, ECO:0007744|PDB:1NTM,
FT ECO:0007744|PDB:1NTZ, ECO:0007744|PDB:1NU1,
FT ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1PPJ,
FT ECO:0007744|PDB:1SQB, ECO:0007744|PDB:1SQP,
FT ECO:0007744|PDB:1SQQ, ECO:0007744|PDB:1SQV,
FT ECO:0007744|PDB:1SQX, ECO:0007744|PDB:2A06,
FT ECO:0007744|PDB:2FYU, ECO:0007744|PDB:2YBB,
FT ECO:0007744|PDB:4D6T, ECO:0007744|PDB:4D6U"
FT BINDING 196
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:12269811,
FT ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040,
FT ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897,
FT ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3,
FT ECO:0007744|PDB:1BGY, ECO:0007744|PDB:1L0L,
FT ECO:0007744|PDB:1L0N, ECO:0007744|PDB:1NTK,
FT ECO:0007744|PDB:1NTM, ECO:0007744|PDB:1NTZ,
FT ECO:0007744|PDB:1PP9, ECO:0007744|PDB:1PPJ,
FT ECO:0007744|PDB:1SQB, ECO:0007744|PDB:1SQP,
FT ECO:0007744|PDB:1SQQ, ECO:0007744|PDB:1SQV,
FT ECO:0007744|PDB:1SQX, ECO:0007744|PDB:2A06,
FT ECO:0007744|PDB:2FYU, ECO:0007744|PDB:2YBB,
FT ECO:0007744|PDB:4D6T, ECO:0007744|PDB:4D6U"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:15312779,
FT ECO:0000269|PubMed:16024040, ECO:0007744|PDB:1PP9,
FT ECO:0007744|PDB:1SQV, ECO:0007744|PDB:2A06,
FT ECO:0007744|PDB:2YBB"
FT VARIANT 90
FT /note="F -> V (in strain: 65, 66 and D)"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 33..52
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1BE3"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 172..203
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 220..245
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1NTM"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 319..339
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 347..363
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 379 AA; 42591 MW; 90160B99E031E016 CRC64;
MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT
TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTFL ETWNIGVILL
LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA
FHFILPFIIM AIAMVHLLFL HETGSNNPTG ISSDVDKIPF HPYYTIKDIL GALLLILALM
LLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALAFSILI
LALIPLLHTS KQRSMMFRPL SQCLFWALVA DLLTLTWIGG QPVEHPYITI GQLASVLYFL
LILVLMPTAG TIENKLLKW
