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 27-MAR-2024, entry version 177. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7DGQ; EM; 5.00 A; m/y=1-379. DR PDB; 7DGR; EM; 4.60 A; m/y=1-379. DR PDB; 7DGS; EM; 7.80 A; m/y=1-379. DR PDB; 7DKF; EM; 8.30 A; C1/O1=1-379. DR PDB; 7R3V; X-ray; 3.20 A; C=1-379. DR PDB; 7TAY; X-ray; 2.95 A; C=1-379. DR PDB; 7TZ6; EM; 2.88 A; C/P=1-379. 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 PDBsum; 7DGQ; -. DR PDBsum; 7DGR; -. DR PDBsum; 7DGS; -. DR PDBsum; 7DKF; -. DR PDBsum; 7R3V; -. DR PDBsum; 7TAY; -. DR PDBsum; 7TZ6; -. DR AlphaFoldDB; P00157; -. DR EMDB; EMD-26203; -. 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; 9913-ENSBTAP00000053148; -. DR Ensembl; ENSBTAT00000060567.1; ENSBTAP00000053148.1; ENSBTAG00000043550.1. 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; NISAWWN; -. DR OrthoDB; 232320at2759; -. DR TreeFam; TF353088; -. DR Reactome; R-BTA-611105; Respiratory electron transport. DR EvolutionaryTrace; P00157; -. DR PRO; PR:P00157; -. DR Proteomes; UP000009136; Mitochondrion. DR Bgee; ENSBTAG00000043550; Expressed in cardiac ventricle and 102 other cell types or tissues. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0031966; C: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 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; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 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 //