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Protein

Cytochrome bo(3) ubiquinol oxidase subunit 1

Gene

cyoB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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.

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei71Quinone (QH)Curated1
Binding sitei75Quinone (QH)Curated1
Binding sitei98Quinone (QH)Curated1
Binding sitei101Quinone (QH)Curated1
Metal bindingi106Iron (heme b axial ligand)1
Metal bindingi284Copper1
Metal bindingi288CopperCurated1
Metal bindingi333Copper1
Metal bindingi334Copper1
Metal bindingi419Iron (heme o axial ligand)1
Metal bindingi421Iron (heme b axial ligand)1

GO - Molecular functioni

GO - Biological processi

  • aerobic electron transport chain Source: EcoCyc
  • aerobic respiration Source: EcoCyc
  • electron transport coupled proton transport Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport
LigandCopper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER
MetaCyc:CYOB-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Topological domaini1 – 16PeriplasmicAdd BLAST16
Transmembranei17 – 35Helical; Name=IAdd BLAST19
Topological domaini36 – 52CytoplasmicAdd BLAST17
Transmembranei53 – 80Helical; Name=IIAdd BLAST28
Topological domaini81 – 95PeriplasmicAdd BLAST15
Transmembranei96 – 132Helical; Name=IIIAdd BLAST37
Topological domaini133 – 137Cytoplasmic5
Transmembranei138 – 161Helical; Name=IVAdd BLAST24
Topological domaini162 – 184PeriplasmicAdd BLAST23
Transmembranei185 – 215Helical; Name=VAdd BLAST31
Topological domaini216 – 224Cytoplasmic9
Transmembranei225 – 260Helical; Name=VIAdd BLAST36
Topological domaini261 – 270Periplasmic10
Transmembranei271 – 307Helical; Name=VIIAdd BLAST37
Topological domaini308 – 311Cytoplasmic4
Transmembranei312 – 326Helical; Name=VIIIAdd BLAST15
Topological domaini327 – 340PeriplasmicAdd BLAST14
Transmembranei341 – 369Helical; Name=IXAdd BLAST29
Topological domaini370 – 377Cytoplasmic8
Transmembranei378 – 409Helical; Name=XAdd BLAST32
Topological domaini410 – 412Periplasmic3
Transmembranei413 – 445Helical; Name=XIAdd BLAST33
Topological domaini446 – 448Cytoplasmic3
Transmembranei449 – 477Helical; Name=XIIAdd BLAST29
Topological domaini478 – 489PeriplasmicAdd BLAST12
Transmembranei490 – 521Helical; Name=XIIIAdd BLAST32
Topological domaini522 – 587CytoplasmicAdd BLAST66
Transmembranei588 – 606Helical; Name=XIVAdd BLAST19
Topological domaini607 – 613Periplasmic7
Transmembranei614 – 632Helical; Name=XVAdd BLAST19
Topological domaini633 – 663CytoplasmicAdd BLAST31

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi54H → A: 50% quinol oxidase activity. 1 Publication1
Mutagenesisi55K → Q: No effect. 1 Publication1
Mutagenesisi71R → H: No quinol oxidase activity. 2 Publications1
Mutagenesisi71R → Q or L: Abolishes quinol oxidase activity. 2 Publications1
Mutagenesisi75D → E: Very similar to wild-type. 3 Publications1
Mutagenesisi75D → H: No quinol oxidase activity, altered binding of a semiquinone intermediate at the QH site. 3 Publications1
Mutagenesisi75D → N: Abolishes quinol oxidase activity. 3 Publications1
Mutagenesisi80R → Q: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi98H → F: About 1% quinol oxidase activity. 2 Publications1
Mutagenesisi98H → N: Abolishes enzyme activity. 2 Publications1
Mutagenesisi101Q → N: Reduces quinol oxidase activity by 75%, decreased affinity for ubiquinol-1. 1 Publication1
Mutagenesisi102I → W: No quinol oxidase activity. 1 Publication1
Mutagenesisi106H → A: 2% quinol oxidase activity, loss of heme b, loss of heme o, loss of Cu(B). 1 Publication1
Mutagenesisi135D → N: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi173Y → F: No effect. 1 Publication1
Mutagenesisi188D → N: No effect. 1 Publication1
Mutagenesisi256D → N: No effect. 1
Mutagenesisi257R → Q: Abolishes quinol oxidase activity. 1
Mutagenesisi284H → A: 1% quinol oxidase activity, loss of heme o. 1 Publication1
Mutagenesisi286E → Q or D: Great decrease in quinol oxidase activity. 1 Publication1
Mutagenesisi288Y → F: Great decrease in activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication1
Mutagenesisi333H → A: 2% quinol oxidase activity, loss of Cu(B). 1 Publication1
Mutagenesisi334H → A: 1% quinol oxidase activity, loss of Cu(B). 1 Publication1
Mutagenesisi362K → Q: Abolishes quinol oxidase activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication1
Mutagenesisi407D → N: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi411H → A: 50% quinol oxidase activity. 1 Publication1
Mutagenesisi419H → A: 3% quinol oxidase activity, loss of heme o, loss of Cu(B). 1 Publication1
Mutagenesisi421H → A: 1% quinol oxidase activity, loss of heme b, some loss of Cu(B). 1 Publication1
Mutagenesisi481R → Q: No effect. 1
Mutagenesisi482R → Q: No effect. 1
Mutagenesisi540E → Q: Abolishes quinol oxidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001834761 – 663Cytochrome bo(3) ubiquinol oxidase subunit 1Add BLAST663

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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, 271 interactors
ComplexPortaliCPX-2102 Cytochrome o ubiquinol oxidase complex
DIPiDIP-47943N
IntActiP0ABI8, 3 interactors
STRINGi316385.ECDH10B_0387

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00088
ProteinModelPortaliP0ABI8
SMRiP0ABI8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABI8

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZ9 Bacteria
COG0843 LUCA
HOGENOMiHOG000085275
InParanoidiP0ABI8
KOiK02298
OMAiMSFWLLP
PhylomeDBiP0ABI8

Family and domain databases

Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR014207 Cyt_c_ubiqinol_oxidase_su1
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
TIGRFAMsiTIGR02843 CyoB, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

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
PATRICifig|1411691.4.peg.1846

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFTX-ray3.50A/F1-663[»]
DisProtiDP00088
ProteinModelPortaliP0ABI8
SMRiP0ABI8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259710, 271 interactors
ComplexPortaliCPX-2102 Cytochrome o ubiquinol oxidase complex
DIPiDIP-47943N
IntActiP0ABI8, 3 interactors
STRINGi316385.ECDH10B_0387

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
PATRICifig|1411691.4.peg.1846

Organism-specific databases

EchoBASEiEB0176
EcoGeneiEG10179 cyoB

Phylogenomic databases

eggNOGiENOG4105BZ9 Bacteria
COG0843 LUCA
HOGENOMiHOG000085275
InParanoidiP0ABI8
KOiK02298
OMAiMSFWLLP
PhylomeDBiP0ABI8

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER
MetaCyc:CYOB-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ABI8
PROiPR:P0ABI8

Family and domain databases

Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR014207 Cyt_c_ubiqinol_oxidase_su1
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
TIGRFAMsiTIGR02843 CyoB, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCYOB_ECOLI
AccessioniPrimary (citable) accession number: P0ABI8
Secondary accession number(s): P18401, Q2MBZ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: September 12, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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