CYOB_ECOLI
ID CYOB_ECOLI Reviewed; 663 AA.
AC P0ABI8; P18401; Q2MBZ5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1;
DE EC=7.1.1.3 {ECO:0000269|PubMed:6365921};
DE AltName: Full=Cytochrome b562-o complex subunit I;
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 1;
DE Short=Cytochrome o subunit 1;
DE AltName: Full=Oxidase bo(3) subunit 1;
DE AltName: Full=Ubiquinol oxidase chain A;
DE AltName: Full=Ubiquinol oxidase polypeptide I;
DE AltName: Full=Ubiquinol oxidase subunit 1;
GN Name=cyoB; OrderedLocusNames=b0431, JW0421;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2162835; DOI=10.1016/s0021-9258(19)38574-6;
RA Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.;
RT "The sequence of the cyo operon indicates substantial structural
RT similarities between the cytochrome o ubiquinol oxidase of Escherichia coli
RT and the aa3-type family of cytochrome c oxidases.";
RL J. Biol. Chem. 265:11185-11192(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN UBIQUINOL OXIDATION, FUNCTION IN PROTON ELECTROCHEMICAL
RP GRADIENT GENERATION, COFACTOR, AND SUBUNIT.
RX PubMed=6308657; DOI=10.1073/pnas.80.16.4889;
RA Matsushita K., Patel L., Gennis R.B., Kaback H.R.;
RT "Reconstitution of active transport in proteoliposomes containing
RT cytochrome o oxidase and lac carrier protein purified from Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4889-4893(1983).
RN [6]
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / KL251/ORF4;
RX PubMed=6365921; DOI=10.1016/s0021-9258(17)43304-7;
RA Kita K., Konishi K., Anraku Y.;
RT "Terminal oxidases of Escherichia coli aerobic respiratory chain. I.
RT Purification and properties of cytochrome b562-o complex from cells in the
RT early exponential phase of aerobic growth.";
RL J. Biol. Chem. 259:3368-3374(1984).
RN [7]
RP TOPOLOGY.
RX PubMed=2165491; DOI=10.1016/s0021-9258(19)38256-0;
RA Chepuri V., Gennis R.B.;
RT "The use of gene fusions to determine the topology of all of the subunits
RT of the cytochrome o terminal oxidase complex of Escherichia coli.";
RL J. Biol. Chem. 265:12978-12986(1990).
RN [8]
RP TOPOLOGY.
RX PubMed=2168206; DOI=10.1016/0005-2728(90)90231-r;
RA Chepuri V., Lemieux L., Hill J., Alben J.O., Gennis R.B.;
RT "Recent studies of the cytochrome o terminal oxidase complex of Escherichia
RT coli.";
RL Biochim. Biophys. Acta 1018:124-127(1990).
RN [9]
RP COPPER-BINDING, HEME-BINDING, COFACTOR, AND MUTAGENESIS OF HIS-54; HIS-106;
RP HIS-284; HIS-333; HIS-334; HIS-411; HIS-419 AND HIS-421.
RX PubMed=1309808; DOI=10.1016/s0021-9258(18)46057-7;
RA Minagawa J., Mogi T., Gennis R.B., Anraku Y.;
RT "Identification of heme and copper ligands in subunit I of the cytochrome
RT bo complex in Escherichia coli.";
RL J. Biol. Chem. 267:2096-2104(1992).
RN [10]
RP MUTAGENESIS OF LYS-55; ARG-80; ASP-135; TYR-173; ASP-188; 256-ASP-ARG-257;
RP GLU-286; TYR-288; LYS-362; ASP-407; 481-ARG-ARG-482 AND GLU-540.
RX PubMed=9378723; DOI=10.1093/oxfordjournals.jbchem.a021770;
RA Kawasaki M., Mogi T., Anraku Y.;
RT "Substitutions of charged amino acid residues conserved in subunit I
RT perturb the redox metal centers of the Escherichia coli bo-type ubiquinol
RT oxidase.";
RL J. Biochem. 122:422-429(1997).
RN [11]
RP PROBABLE HIGH AFFINITY-QUINONE BINDING (QH), COFACTOR, AND MUTAGENESIS OF
RP ARG-71; ASP-75; HIS-98 AND ILE-102.
RX PubMed=12186553; DOI=10.1021/bi012146w;
RA Hellwig P., Yano T., Ohnishi T., Gennis R.B.;
RT "Identification of the residues involved in stabilization of the
RT semiquinone radical in the high-affinity ubiquinone binding site in
RT cytochrome bo(3) from Escherichia coli by site-directed mutagenesis and EPR
RT spectroscopy.";
RL Biochemistry 41:10675-10679(2002).
RN [12]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [13]
RP MUTAGENESIS OF ASP-75.
RX PubMed=17267395; DOI=10.1074/jbc.m611595200;
RA Yap L.L., Samoilova R.I., Gennis R.B., Dikanov S.A.;
RT "Characterization of mutants that change the hydrogen bonding of the
RT semiquinone radical at the QH site of the cytochrome bo3 from Escherichia
RT coli.";
RL J. Biol. Chem. 282:8777-8785(2007).
RN [14]
RP FUNCTION AS AN OXIDASE, FUNCTION AS A PROTON PUMP, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=19542282; DOI=10.1128/jb.00562-09;
RA Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
RT "Respiration of Escherichia coli can be fully uncoupled via the
RT nonelectrogenic terminal cytochrome bd-II oxidase.";
RL J. Bacteriol. 191:5510-5517(2009).
RN [15]
RP FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=22843529; DOI=10.1128/aem.01507-12;
RA Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.;
RT "Uncoupling of substrate-level phosphorylation in Escherichia coli during
RT glucose-limited growth.";
RL Appl. Environ. Microbiol. 78:6908-6913(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), HEME-BINDING, COPPER-BINDING,
RP PROBABLE UBIQUINONE-BINDING, PROBABLE PROTON CHANNELS, COFACTOR, SUBUNIT,
RP AND MUTAGENESIS OF ARG-71; ASP-75; HIS-98 AND GLN-101.
RX PubMed=11017202; DOI=10.1038/82824;
RA Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M.,
RA Puustinen A., Iwata S., Wikstrom M.;
RT "The structure of the ubiquinol oxidase from Escherichia coli and its
RT ubiquinone binding site.";
RL Nat. Struct. Biol. 7:910-917(2000).
CC -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component
CC of the aerobic respiratory chain of E.coli that predominates when cells
CC are grown at high aeration. Has proton pump activity across the
CC membrane in addition to electron transfer, pumping 2 protons/electron.
CC Protons are probably pumped via D- and K- channels found in this
CC subunit (PubMed:11017202). {ECO:0000269|PubMed:11017202,
CC ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529,
CC ECO:0000269|PubMed:6308657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out)
CC + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3;
CC Evidence={ECO:0000269|PubMed:6365921};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 low-spin heme b per subunit.;
CC -!- COFACTOR:
CC Name=heme o; Xref=ChEBI:CHEBI:24480;
CC Note=Binds 1 high-spin heme o per subunit.;
CC -!- COFACTOR:
CC Name=a quinone; Xref=ChEBI:CHEBI:132124;
CC Note=Binds 1 high-affinity quinone that appears to function as a
CC tightly bound cofactor (QH), forming a semiquinone intermediate in the
CC reaction.;
CC -!- ACTIVITY REGULATION: Competitively inhibited by piericidin A, non-
CC competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide,
CC NaN(3) and KCN; 50% inhibition occurs at 2 uM, 2 uM, 15 mM and 10 uM,
CC respectively. Inhibited by Zn(2+) and Cd(2+).
CC {ECO:0000269|PubMed:6365921}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for ubiquinol-1 {ECO:0000269|PubMed:6365921};
CC KM=50 uM for ubiquinol-6 {ECO:0000269|PubMed:6365921};
CC Vmax=15.5 umol/min/nmol enzyme with ubiquinol-1
CC {ECO:0000269|PubMed:6365921};
CC Vmax=12.6 umol/min/nmol enzyme with ubiquinol-6
CC {ECO:0000269|PubMed:6365921};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:6365921};
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC two D chains. {ECO:0000269|PubMed:11017202,
CC ECO:0000269|PubMed:6308657}.
CC -!- INTERACTION:
CC P0ABI8; P77806: ybdL; NbExp=3; IntAct=EBI-2932021, EBI-543661;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:6365921};
CC Multi-pass membrane protein {ECO:0000269|PubMed:6365921}.
CC -!- DISRUPTION PHENOTYPE: Increased reduction of the ubiquinone pool (in
CC aerobically grown minimal medium with glucose).
CC {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529}.
CC -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in the
CC electron transport chain.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; J05492; AAA23632.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40187.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73534.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76211.1; -; Genomic_DNA.
DR PIR; B42226; B42226.
DR RefSeq; NP_414965.1; NC_000913.3.
DR RefSeq; WP_000467180.1; NZ_STEB01000007.1.
DR PDB; 1FFT; X-ray; 3.50 A; A/F=1-663.
DR PDB; 6WTI; EM; 2.38 A; A=1-663.
DR PDB; 7CUB; EM; 2.55 A; A=1-663.
DR PDB; 7CUQ; EM; 2.64 A; A=1-663.
DR PDB; 7CUW; EM; 2.63 A; A=1-663.
DR PDB; 7N9Z; EM; 2.19 A; F=1-663.
DR PDBsum; 1FFT; -.
DR PDBsum; 6WTI; -.
DR PDBsum; 7CUB; -.
DR PDBsum; 7CUQ; -.
DR PDBsum; 7CUW; -.
DR PDBsum; 7N9Z; -.
DR AlphaFoldDB; P0ABI8; -.
DR SMR; P0ABI8; -.
DR BioGRID; 4259710; 271.
DR BioGRID; 849987; 1.
DR ComplexPortal; CPX-2102; Cytochrome bo3 ubiquinol oxidase complex.
DR DIP; DIP-47943N; -.
DR IntAct; P0ABI8; 3.
DR STRING; 511145.b0431; -.
DR TCDB; 3.D.4.5.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR jPOST; P0ABI8; -.
DR PaxDb; P0ABI8; -.
DR PRIDE; P0ABI8; -.
DR EnsemblBacteria; AAC73534; AAC73534; b0431.
DR EnsemblBacteria; BAE76211; BAE76211; BAE76211.
DR GeneID; 66671267; -.
DR GeneID; 945615; -.
DR KEGG; ecj:JW0421; -.
DR KEGG; eco:b0431; -.
DR PATRIC; fig|1411691.4.peg.1846; -.
DR EchoBASE; EB0176; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_6; -.
DR InParanoid; P0ABI8; -.
DR OMA; WAMMSIG; -.
DR PhylomeDB; P0ABI8; -.
DR BioCyc; EcoCyc:CYOB-MON; -.
DR BioCyc; MetaCyc:CYOB-MON; -.
DR BRENDA; 7.1.1.3; 2026.
DR EvolutionaryTrace; P0ABI8; -.
DR PRO; PR:P0ABI8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IDA:EcoCyc.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0048039; F:ubiquinone binding; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0015990; P:electron transport coupled proton transport; IDA:ComplexPortal.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR DisProt; DP00088; -.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014207; Cyt_c_ubiqinol_oxidase_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02843; CyoB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Copper;
KW Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
KW Membrane; Metal-binding; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..663
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 1"
FT /id="PRO_0000183476"
FT TOPO_DOM 1..16
FT /note="Periplasmic"
FT TRANSMEM 17..35
FT /note="Helical; Name=I"
FT TOPO_DOM 36..52
FT /note="Cytoplasmic"
FT TRANSMEM 53..80
FT /note="Helical; Name=II"
FT TOPO_DOM 81..95
FT /note="Periplasmic"
FT TRANSMEM 96..132
FT /note="Helical; Name=III"
FT TOPO_DOM 133..137
FT /note="Cytoplasmic"
FT TRANSMEM 138..161
FT /note="Helical; Name=IV"
FT TOPO_DOM 162..184
FT /note="Periplasmic"
FT TRANSMEM 185..215
FT /note="Helical; Name=V"
FT TOPO_DOM 216..224
FT /note="Cytoplasmic"
FT TRANSMEM 225..260
FT /note="Helical; Name=VI"
FT TOPO_DOM 261..270
FT /note="Periplasmic"
FT TRANSMEM 271..307
FT /note="Helical; Name=VII"
FT TOPO_DOM 308..311
FT /note="Cytoplasmic"
FT TRANSMEM 312..326
FT /note="Helical; Name=VIII"
FT TOPO_DOM 327..340
FT /note="Periplasmic"
FT TRANSMEM 341..369
FT /note="Helical; Name=IX"
FT TOPO_DOM 370..377
FT /note="Cytoplasmic"
FT TRANSMEM 378..409
FT /note="Helical; Name=X"
FT TOPO_DOM 410..412
FT /note="Periplasmic"
FT TRANSMEM 413..445
FT /note="Helical; Name=XI"
FT TOPO_DOM 446..448
FT /note="Cytoplasmic"
FT TRANSMEM 449..477
FT /note="Helical; Name=XII"
FT TOPO_DOM 478..489
FT /note="Periplasmic"
FT TRANSMEM 490..521
FT /note="Helical; Name=XIII"
FT TOPO_DOM 522..587
FT /note="Cytoplasmic"
FT TRANSMEM 588..606
FT /note="Helical; Name=XIV"
FT TOPO_DOM 607..613
FT /note="Periplasmic"
FT TRANSMEM 614..632
FT /note="Helical; Name=XV"
FT TOPO_DOM 633..663
FT /note="Cytoplasmic"
FT BINDING 71
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000305"
FT BINDING 101
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000305"
FT BINDING 106
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305"
FT BINDING 333
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 419
FT /ligand="Fe(II)-heme o"
FT /ligand_id="ChEBI:CHEBI:60530"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 421
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CROSSLNK 284..288
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT MUTAGEN 54
FT /note="H->A: 50% quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 55
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 71
FT /note="R->H: No quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553"
FT MUTAGEN 71
FT /note="R->Q,L: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553"
FT MUTAGEN 75
FT /note="D->E: Very similar to wild-type."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553, ECO:0000269|PubMed:17267395"
FT MUTAGEN 75
FT /note="D->H: No quinol oxidase activity, altered binding of
FT a semiquinone intermediate at the QH site."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553, ECO:0000269|PubMed:17267395"
FT MUTAGEN 75
FT /note="D->N: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553, ECO:0000269|PubMed:17267395"
FT MUTAGEN 80
FT /note="R->Q: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 98
FT /note="H->F: About 1% quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553"
FT MUTAGEN 98
FT /note="H->N: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11017202,
FT ECO:0000269|PubMed:12186553"
FT MUTAGEN 101
FT /note="Q->N: Reduces quinol oxidase activity by 75%,
FT decreased affinity for ubiquinol-1."
FT /evidence="ECO:0000269|PubMed:11017202"
FT MUTAGEN 102
FT /note="I->W: No quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:12186553"
FT MUTAGEN 106
FT /note="H->A: 2% quinol oxidase activity, loss of heme b,
FT loss of heme o, loss of Cu(B)."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 135
FT /note="D->N: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 173
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 188
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 256
FT /note="D->N: No effect."
FT MUTAGEN 257
FT /note="R->Q: Abolishes quinol oxidase activity."
FT MUTAGEN 284
FT /note="H->A: 1% quinol oxidase activity, loss of heme o."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 286
FT /note="E->Q,D: Great decrease in quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 288
FT /note="Y->F: Great decrease in activity, 100-fold decrease
FT in heme b-to-heme o electron transfer."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 333
FT /note="H->A: 2% quinol oxidase activity, loss of Cu(B)."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 334
FT /note="H->A: 1% quinol oxidase activity, loss of Cu(B)."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 362
FT /note="K->Q: Abolishes quinol oxidase activity, 100-fold
FT decrease in heme b-to-heme o electron transfer."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 407
FT /note="D->N: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:9378723"
FT MUTAGEN 411
FT /note="H->A: 50% quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 419
FT /note="H->A: 3% quinol oxidase activity, loss of heme o,
FT loss of Cu(B)."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 421
FT /note="H->A: 1% quinol oxidase activity, loss of heme b,
FT some loss of Cu(B)."
FT /evidence="ECO:0000269|PubMed:1309808"
FT MUTAGEN 481
FT /note="R->Q: No effect."
FT MUTAGEN 482
FT /note="R->Q: No effect."
FT MUTAGEN 540
FT /note="E->Q: Abolishes quinol oxidase activity."
FT /evidence="ECO:0000269|PubMed:9378723"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 15..38
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 54..86
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 139..161
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 186..214
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 227..258
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:7CUB"
FT HELIX 272..305
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 335..339
FT /evidence="ECO:0007829|PDB:1FFT"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:7CUW"
FT HELIX 379..401
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 429..439
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 450..476
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:7CUB"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 492..520
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 521..525
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 583..586
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 591..607
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 611..627
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 635..638
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 640..657
FT /evidence="ECO:0007829|PDB:6WTI"
SQ SEQUENCE 663 AA; 74368 MW; 17357B8D44C7CF84 CRC64;
MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT SVDHKRLGIM
YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI
GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNVSL GVGEFAQTGW LAYPPLSGIE
YSPGVGVDYW IWSLQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII
ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG
VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF
HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYALGFMGMT
RRLSQQIDPQ FHTMLMIAAS GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE
WATSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST
IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH FDEITKAGLK
NGN
