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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)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

  • 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.

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

  • 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)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. 224 interactors.
DIPiDIP-47943N.
IntActiP0ABI8. 3 interactors.
STRINGi511145.b0431.

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 79Combined sources26
Turni80 – 84Combined sources5
Beta strandi85 – 88Combined sources4
Helixi97 – 112Combined sources16
Helixi117 – 131Combined sources15
Helixi139 – 160Combined sources22
Turni161 – 163Combined sources3
Turni169 – 172Combined sources4
Turni174 – 176Combined sources3
Helixi186 – 214Combined sources29
Helixi222 – 224Combined sources3
Helixi227 – 241Combined sources15
Helixi244 – 259Combined sources16
Turni266 – 269Combined sources4
Helixi272 – 289Combined sources18
Helixi292 – 306Combined sources15
Helixi313 – 325Combined sources13
Helixi331 – 334Combined sources4
Turni335 – 339Combined sources5
Helixi342 – 354Combined sources13
Helixi357 – 368Combined sources12
Turni369 – 372Combined sources4
Helixi379 – 401Combined sources23
Helixi404 – 408Combined sources5
Turni409 – 412Combined sources4
Helixi414 – 425Combined sources12
Turni426 – 428Combined sources3
Helixi429 – 444Combined sources16
Helixi450 – 476Combined sources27
Helixi491 – 520Combined sources30
Turni539 – 542Combined sources4

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...

Miscellaneous databases

EvolutionaryTraceiP0ABI8.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFTX-ray3.50A/F1-663[»]
DisProtiDP00088.
ProteinModelPortaliP0ABI8.
SMRiP0ABI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259710. 224 interactors.
DIPiDIP-47943N.
IntActiP0ABI8. 3 interactors.
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.
PhylomeDBiP0ABI8.

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER.
ECOL316407:JW0421-MONOMER.
MetaCyc:CYOB-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABI8.
PROiP0ABI8.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
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...

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: November 30, 2016
This is version 100 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.