Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome bo(3) ubiquinol oxidase subunit 1

Gene

cyoB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytochrome bo3 ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit (PubMed:11017202).4 Publications

Catalytic activityi

2 ubiquinol + O2 + n H+(Side 1) = 2 ubiquinone + 2 H2O + n H+(Side 2).1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Cu2+Note: Binds 1 copper B ion per subunit.
  • heme bNote: Binds 1 low-spin heme b per subunit.
  • heme oNote: Binds 1 high-spin heme o per subunit.
  • a quinoneNote: Binds 1 high-affinity quinone that appears to function as a tightly bound cofactor (QH), forming a semiquinone intermediate in the reaction.

Enzyme regulationi

Competitively inhibited by piericidin A, non-competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide, NaN3 and KCN; 50% inhibition occurs at 2 µM, 2 µM, 15 mM and 10 µM, respectively. Inhibited by Zn2+ and Cd2+.1 Publication

Kineticsi

  1. KM=50 µM for ubiquinol-11 Publication
  2. KM=50 µM for ubiquinol-61 Publication
  1. Vmax=15.5 µmol/min/nmol enzyme with ubiquinol-11 Publication
  2. Vmax=12.6 µmol/min/nmol enzyme with ubiquinol-61 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711Quinone (QH)Curated
Binding sitei75 – 751Quinone (QH)Curated
Binding sitei98 – 981Quinone (QH)Curated
Binding sitei101 – 1011Quinone (QH)Curated
Metal bindingi106 – 1061Iron (heme b axial ligand)
Metal bindingi284 – 2841Copper
Metal bindingi288 – 2881CopperCurated
Metal bindingi333 – 3331Copper
Metal bindingi334 – 3341Copper
Metal bindingi419 – 4191Iron (heme o axial ligand)
Metal bindingi421 – 4211Iron (heme b axial ligand)

GO - Molecular functioni

  • copper ion binding Source: EcoCyc
  • cytochrome bo3 ubiquinol oxidase activity Source: EcoCyc
  • cytochrome-c oxidase activity Source: InterPro
  • electron carrier activity Source: EcoCyc
  • heme binding Source: EcoCyc
  • hydrogen ion transmembrane transporter activity Source: EcoCyc
  • iron ion binding Source: InterPro
  • oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Source: InterPro
  • oxidoreduction-driven active transmembrane transporter activity Source: EcoCyc
  • ubiquinone binding Source: EcoCyc

GO - Biological processi

  • aerobic electron transport chain Source: EcoCyc
  • aerobic respiration Source: EcoCyc
  • electron transport coupled proton transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER.
ECOL316407:JW0421-MONOMER.
MetaCyc:CYOB-MONOMER.
RETL1328306-WGS:GSTH-5877-MONOMER.

Protein family/group databases

TCDBi3.D.4.5.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome bo(3) ubiquinol oxidase subunit 1 (EC:1.10.3.10)
Alternative name(s):
Cytochrome b562-o complex subunit I
Cytochrome o ubiquinol oxidase subunit 1
Short name:
Cytochrome o subunit 1
Oxidase bo(3) subunit 1
Ubiquinol oxidase chain A
Ubiquinol oxidase polypeptide I
Ubiquinol oxidase subunit 1
Gene namesi
Name:cyoB
Ordered Locus Names:b0431, JW0421
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10179. cyoB.

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616PeriplasmicAdd
BLAST
Transmembranei17 – 3519Helical; Name=IAdd
BLAST
Topological domaini36 – 5217CytoplasmicAdd
BLAST
Transmembranei53 – 8028Helical; Name=IIAdd
BLAST
Topological domaini81 – 9515PeriplasmicAdd
BLAST
Transmembranei96 – 13237Helical; Name=IIIAdd
BLAST
Topological domaini133 – 1375Cytoplasmic
Transmembranei138 – 16124Helical; Name=IVAdd
BLAST
Topological domaini162 – 18423PeriplasmicAdd
BLAST
Transmembranei185 – 21531Helical; Name=VAdd
BLAST
Topological domaini216 – 2249Cytoplasmic
Transmembranei225 – 26036Helical; Name=VIAdd
BLAST
Topological domaini261 – 27010Periplasmic
Transmembranei271 – 30737Helical; Name=VIIAdd
BLAST
Topological domaini308 – 3114Cytoplasmic
Transmembranei312 – 32615Helical; Name=VIIIAdd
BLAST
Topological domaini327 – 34014PeriplasmicAdd
BLAST
Transmembranei341 – 36929Helical; Name=IXAdd
BLAST
Topological domaini370 – 3778Cytoplasmic
Transmembranei378 – 40932Helical; Name=XAdd
BLAST
Topological domaini410 – 4123Periplasmic
Transmembranei413 – 44533Helical; Name=XIAdd
BLAST
Topological domaini446 – 4483Cytoplasmic
Transmembranei449 – 47729Helical; Name=XIIAdd
BLAST
Topological domaini478 – 48912PeriplasmicAdd
BLAST
Transmembranei490 – 52132Helical; Name=XIIIAdd
BLAST
Topological domaini522 – 58766CytoplasmicAdd
BLAST
Transmembranei588 – 60619Helical; Name=XIVAdd
BLAST
Topological domaini607 – 6137Periplasmic
Transmembranei614 – 63219Helical; Name=XVAdd
BLAST
Topological domaini633 – 66331CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cytochrome o ubiquinol oxidase complex Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
  • respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Increased reduction of the ubiquinone pool (in aerobically grown minimal medium with glucose).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541H → A: 50% quinol oxidase activity. 1 Publication
Mutagenesisi55 – 551K → Q: No effect. 1 Publication
Mutagenesisi71 – 711R → H: No quinol oxidase activity. 2 Publications
Mutagenesisi71 – 711R → Q or L: Abolishes quinol oxidase activity. 2 Publications
Mutagenesisi75 – 751D → E: Very similar to wild-type. 3 Publications
Mutagenesisi75 – 751D → H: No quinol oxidase activity, altered binding of a semiquinone intermediate at the QH site. 3 Publications
Mutagenesisi75 – 751D → N: Abolishes quinol oxidase activity. 3 Publications
Mutagenesisi80 – 801R → Q: Abolishes quinol oxidase activity. 1 Publication
Mutagenesisi98 – 981H → F: About 1% quinol oxidase activity. 2 Publications
Mutagenesisi98 – 981H → N: Abolishes enzyme activity. 2 Publications
Mutagenesisi101 – 1011Q → N: Reduces quinol oxidase activity by 75%, decreased affinity for ubiquinol-1. 1 Publication
Mutagenesisi102 – 1021I → W: No quinol oxidase activity. 1 Publication
Mutagenesisi106 – 1061H → A: 2% quinol oxidase activity, loss of heme b, loss of heme o, loss of Cu(B). 1 Publication
Mutagenesisi135 – 1351D → N: Abolishes quinol oxidase activity. 1 Publication
Mutagenesisi173 – 1731Y → F: No effect. 1 Publication
Mutagenesisi188 – 1881D → N: No effect. 1 Publication
Mutagenesisi256 – 2561D → N: No effect.
Mutagenesisi257 – 2571R → Q: Abolishes quinol oxidase activity.
Mutagenesisi284 – 2841H → A: 1% quinol oxidase activity, loss of heme o. 1 Publication
Mutagenesisi286 – 2861E → Q or D: Great decrease in quinol oxidase activity. 1 Publication
Mutagenesisi288 – 2881Y → F: Great decrease in activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication
Mutagenesisi333 – 3331H → A: 2% quinol oxidase activity, loss of Cu(B). 1 Publication
Mutagenesisi334 – 3341H → A: 1% quinol oxidase activity, loss of Cu(B). 1 Publication
Mutagenesisi362 – 3621K → Q: Abolishes quinol oxidase activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication
Mutagenesisi407 – 4071D → N: Abolishes quinol oxidase activity. 1 Publication
Mutagenesisi411 – 4111H → A: 50% quinol oxidase activity. 1 Publication
Mutagenesisi419 – 4191H → A: 3% quinol oxidase activity, loss of heme o, loss of Cu(B). 1 Publication
Mutagenesisi421 – 4211H → A: 1% quinol oxidase activity, loss of heme b, some loss of Cu(B). 1 Publication
Mutagenesisi481 – 4811R → Q: No effect.
Mutagenesisi482 – 4821R → Q: No effect.
Mutagenesisi540 – 5401E → Q: Abolishes quinol oxidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Cytochrome bo(3) ubiquinol oxidase subunit 1PRO_0000183476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki284 ↔ 2881'-histidyl-3'-tyrosine (His-Tyr)By similarity

Proteomic databases

PaxDbiP0ABI8.
PRIDEiP0ABI8.

Interactioni

Subunit structurei

Heterooctamer of two A chains, two B chains, two C chains and two D chains.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ybdLP778063EBI-2932021,EBI-543661

Protein-protein interaction databases

BioGridi4259710. 224 interactions.
DIPiDIP-47943N.
IntActiP0ABI8. 3 interactions.
STRINGi511145.b0431.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 7926Combined sources
Turni80 – 845Combined sources
Beta strandi85 – 884Combined sources
Helixi97 – 11216Combined sources
Helixi117 – 13115Combined sources
Helixi139 – 16022Combined sources
Turni161 – 1633Combined sources
Turni169 – 1724Combined sources
Turni174 – 1763Combined sources
Helixi186 – 21429Combined sources
Helixi222 – 2243Combined sources
Helixi227 – 24115Combined sources
Helixi244 – 25916Combined sources
Turni266 – 2694Combined sources
Helixi272 – 28918Combined sources
Helixi292 – 30615Combined sources
Helixi313 – 32513Combined sources
Helixi331 – 3344Combined sources
Turni335 – 3395Combined sources
Helixi342 – 35413Combined sources
Helixi357 – 36812Combined sources
Turni369 – 3724Combined sources
Helixi379 – 40123Combined sources
Helixi404 – 4085Combined sources
Turni409 – 4124Combined sources
Helixi414 – 42512Combined sources
Turni426 – 4283Combined sources
Helixi429 – 44416Combined sources
Helixi450 – 47627Combined sources
Helixi491 – 52030Combined sources
Turni539 – 5424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFTX-ray3.50A/F1-663[»]
DisProtiDP00088.
ProteinModelPortaliP0ABI8.
SMRiP0ABI8. Positions 41-628.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABI8.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZ9. Bacteria.
COG0843. LUCA.
HOGENOMiHOG000085275.
InParanoidiP0ABI8.
KOiK02298.
OMAiFCGKRLF.
OrthoDBiEOG6B35XR.
PhylomeDBiP0ABI8.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014207. Cyt_c_ubiqinol_oxidase_su1.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
TIGRFAMsiTIGR02843. CyoB. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT
60 70 80 90 100
SVDHKRLGIM YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD
110 120 130 140 150
QIFTAHGVIM IFFVAMPFVI GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV
160 170 180 190 200
VGVILVNVSL GVGEFAQTGW LAYPPLSGIE YSPGVGVDYW IWSLQLSGIG
210 220 230 240 250
TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII ASFPILTVTV
260 270 280 290 300
ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
310 320 330 340 350
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI
360 370 380 390 400
TTMIIAIPTG VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL
410 420 430 440 450
LAVPGADFVL HNSLFLIAHF HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE
460 470 480 490 500
TWGKRAFWFW IIGFFVAFMP LYALGFMGMT RRLSQQIDPQ FHTMLMIAAS
510 520 530 540 550
GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE WATSSPPPFY
560 570 580 590 600
NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST
610 620 630 640 650
IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH
660
FDEITKAGLK NGN
Length:663
Mass (Da):74,368
Last modified:October 25, 2005 - v1
Checksum:i17357B8D44C7CF84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05492 Genomic DNA. Translation: AAA23632.1.
U82664 Genomic DNA. Translation: AAB40187.1.
U00096 Genomic DNA. Translation: AAC73534.1.
AP009048 Genomic DNA. Translation: BAE76211.1.
PIRiB42226.
RefSeqiNP_414965.1. NC_000913.3.
WP_000467180.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73534; AAC73534; b0431.
BAE76211; BAE76211; BAE76211.
GeneIDi945615.
KEGGiecj:JW0421.
eco:b0431.
PATRICi32116013. VBIEscCol129921_0448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05492 Genomic DNA. Translation: AAA23632.1.
U82664 Genomic DNA. Translation: AAB40187.1.
U00096 Genomic DNA. Translation: AAC73534.1.
AP009048 Genomic DNA. Translation: BAE76211.1.
PIRiB42226.
RefSeqiNP_414965.1. NC_000913.3.
WP_000467180.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFTX-ray3.50A/F1-663[»]
DisProtiDP00088.
ProteinModelPortaliP0ABI8.
SMRiP0ABI8. Positions 41-628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259710. 224 interactions.
DIPiDIP-47943N.
IntActiP0ABI8. 3 interactions.
STRINGi511145.b0431.

Protein family/group databases

TCDBi3.D.4.5.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Proteomic databases

PaxDbiP0ABI8.
PRIDEiP0ABI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73534; AAC73534; b0431.
BAE76211; BAE76211; BAE76211.
GeneIDi945615.
KEGGiecj:JW0421.
eco:b0431.
PATRICi32116013. VBIEscCol129921_0448.

Organism-specific databases

EchoBASEiEB0176.
EcoGeneiEG10179. cyoB.

Phylogenomic databases

eggNOGiENOG4105BZ9. Bacteria.
COG0843. LUCA.
HOGENOMiHOG000085275.
InParanoidiP0ABI8.
KOiK02298.
OMAiFCGKRLF.
OrthoDBiEOG6B35XR.
PhylomeDBiP0ABI8.

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER.
ECOL316407:JW0421-MONOMER.
MetaCyc:CYOB-MONOMER.
RETL1328306-WGS:GSTH-5877-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABI8.
PROiP0ABI8.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014207. Cyt_c_ubiqinol_oxidase_su1.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
TIGRFAMsiTIGR02843. CyoB. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases."
    Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.
    J. Biol. Chem. 265:11185-11192(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli."
    Matsushita K., Patel L., Gennis R.B., Kaback H.R.
    Proc. Natl. Acad. Sci. U.S.A. 80:4889-4893(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUINOL OXIDATION, FUNCTION IN PROTON ELECTROCHEMICAL GRADIENT GENERATION, COFACTOR, SUBUNIT.
  6. "Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth."
    Kita K., Konishi K., Anraku Y.
    J. Biol. Chem. 259:3368-3374(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    Strain: K12 / KL251/ORF4.
  7. "The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli."
    Chepuri V., Gennis R.B.
    J. Biol. Chem. 265:12978-12986(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  8. "Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli."
    Chepuri V., Lemieux L., Hill J., Alben J.O., Gennis R.B.
    Biochim. Biophys. Acta 1018:124-127(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  9. "Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli."
    Minagawa J., Mogi T., Gennis R.B., Anraku Y.
    J. Biol. Chem. 267:2096-2104(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: COPPER-BINDING, HEME-BINDING, COFACTOR, MUTAGENESIS OF HIS-54; HIS-106; HIS-284; HIS-333; HIS-334; HIS-411; HIS-419 AND HIS-421.
  10. "Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase."
    Kawasaki M., Mogi T., Anraku Y.
    J. Biochem. 122:422-429(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-55; ARG-80; ASP-135; TYR-173; ASP-188; 256-ASP-ARG-257; GLU-286; TYR-288; LYS-362; ASP-407; 481-ARG-ARG-482 AND GLU-540.
  11. "Identification of the residues involved in stabilization of the semiquinone radical in the high-affinity ubiquinone binding site in cytochrome bo(3) from Escherichia coli by site-directed mutagenesis and EPR spectroscopy."
    Hellwig P., Yano T., Ohnishi T., Gennis R.B.
    Biochemistry 41:10675-10679(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE HIGH AFFINITY-QUINONE BINDING (QH), COFACTOR, MUTAGENESIS OF ARG-71; ASP-75; HIS-98 AND ILE-102.
  12. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  13. "Characterization of mutants that change the hydrogen bonding of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli."
    Yap L.L., Samoilova R.I., Gennis R.B., Dikanov S.A.
    J. Biol. Chem. 282:8777-8785(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-75.
  14. "Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase."
    Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.
    J. Bacteriol. 191:5510-5517(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, FUNCTION AS A PROTON PUMP, DISRUPTION PHENOTYPE.
    Strain: K12.
  15. "Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth."
    Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.
    Appl. Environ. Microbiol. 78:6908-6913(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.
  16. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site."
    Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Puustinen A., Iwata S., Wikstrom M.
    Nat. Struct. Biol. 7:910-917(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), HEME-BINDING, COPPER-BINDING, PROBABLE UBIQUINE-BINDING, PROBABLE PROTON CHANNELS, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-71; ASP-75; HIS-98 AND GLN-101.

Entry informationi

Entry nameiCYOB_ECOLI
AccessioniPrimary (citable) accession number: P0ABI8
Secondary accession number(s): P18401, Q2MBZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: January 20, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Ubiquinol oxidase catalyzes the terminal step in the electron transport chain.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.