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P57543 (CYOB_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome bo(3) ubiquinol oxidase subunit 1

EC=1.10.3.10
Alternative name(s):
Cytochrome o ubiquinol oxidase subunit 1
Short name=Cytochrome o subunit 1
Oxidase bo(3) subunit 1
Ubiquinol oxidase polypeptide I
Ubiquinol oxidase subunit 1
Gene names
Name:cyoB
Ordered Locus Names:BU471
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 copper B ion per subunit By similarity.

Binds 1 low-spin heme b per subunit By similarity.

Binds 1 high-spin heme o per subunit By similarity.

Bind 1 high-affinity quinone that appears to function as a tightly bound cofactor (QH), forming a semiquinone intermediate in the reaction By similarity.

Subunit structure

Heterooctamer of two A chains, two B chains, two C chains and two D chains By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Cytochrome bo(3) ubiquinol oxidase subunit 1
PRO_0000183479

Regions

Topological domain1 – 1414Extracellular Potential
Transmembrane15 – 3521Helical; Potential
Topological domain36 – 5823Cytoplasmic Potential
Transmembrane59 – 7921Helical; Potential
Topological domain80 – 10627Extracellular Potential
Transmembrane107 – 12721Helical; Potential
Topological domain128 – 14518Cytoplasmic Potential
Transmembrane146 – 16621Helical; Potential
Topological domain167 – 18923Extracellular Potential
Transmembrane190 – 21021Helical; Potential
Topological domain211 – 23222Cytoplasmic Potential
Transmembrane233 – 25321Helical; Potential
Topological domain254 – 27724Extracellular Potential
Transmembrane278 – 29821Helical; Potential
Topological domain299 – 30911Cytoplasmic Potential
Transmembrane310 – 33021Helical; Potential
Topological domain331 – 34616Extracellular Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 38013Cytoplasmic Potential
Transmembrane381 – 40121Helical; Potential
Topological domain402 – 41312Extracellular Potential
Transmembrane414 – 43421Helical; Potential
Topological domain435 – 45622Cytoplasmic Potential
Transmembrane457 – 47721Helical; Potential
Topological domain478 – 49316Extracellular Potential
Transmembrane494 – 51421Helical; Potential
Topological domain515 – 58672Cytoplasmic Potential
Transmembrane587 – 60721Helical; Potential
Topological domain6081Extracellular Potential
Transmembrane609 – 62921Helical; Potential
Topological domain630 – 66233Cytoplasmic Potential

Sites

Metal binding1061Iron (heme b axial ligand) By similarity
Metal binding2841Copper By similarity
Metal binding2881Copper By similarity
Metal binding3331Copper By similarity
Metal binding3341Copper By similarity
Metal binding4191Iron (heme o axial ligand) By similarity
Metal binding4211Iron (heme b axial ligand) By similarity
Binding site711Quinone (QH) By similarity
Binding site751Quinone (QH) By similarity
Binding site981Quinone (QH) By similarity
Binding site1011Quinone (QH) By similarity

Amino acid modifications

Cross-link284 ↔ 2881'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P57543 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 3F502A628133EA65

FASTA66275,455
        10         20         30         40         50         60 
MFGKLTFDAI PYHEPIIMIT YIAIILIALC IASTITYYKK WKYLWYEWFT TVDHKKISIM 

        70         80         90        100        110        120 
YGILAFVMLF RGFVDAILMR TQQVVASAGF KGFLPPHHYD QIFTAHGVIM IFFVAMPLVI 

       130        140        150        160        170        180 
GLMNLVIPLQ IGARDVAFPF LNNLSFWLNV SSAVLLTLSL GIGEFAQTGW LAYPPLSGIK 

       190        200        210        220        230        240 
YSSGVGVDYW IWSLQISGVG TTLTGINFLV TILKMRAPGM SFFKMPVFTW TSLCTNILIV 

       250        260        270        280        290        300 
ISFPVLTVTL VLLTLDRYFN FHFFTNDLGG NAMMYVNLIW IWGHPEVYIL VLPVFGVFSE 

       310        320        330        340        350        360 
VVATFSKKRL FGYVSLVWAT LSITILSFIV WLHHFFTMGA GADVNTFFGI TTMIIAIPTG 

       370        380        390        400        410        420 
VKIFNWLFTI YQGRVHMHSS ILWTLGFLVT FSIGGMTGVL LSVPPADFVL HNSLFLVAHF 

       430        440        450        460        470        480 
HNVIIGGVVF GCFAGINYWF PKLFGFVLNE IWGKRAFWFW IIGFFLAFIP LYFLGLMGMT 

       490        500        510        520        530        540 
RRLSQNIDSE FHMLLCIAAI GACFIGIGII CQVIQFFISI KERRHNLDLT GDPWDGRTLE 

       550        560        570        580        590        600 
WSTSSPAPLY NFAIIPKVED RDDFWRNKEG QHYNKLINSI NYHDIHMPKN TGLGFMISIF 

       610        620        630        640        650        660 
SLFFGFSAVW HITWLCILSF LAIIISLFIN SLNEDTEYTI SAEEIKKIEH QYWKNIQKAG 


LK 

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References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB13168.1.
RefSeqNP_240282.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57543.
SMRP57543. Positions 52-552.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13168; BAB13168; BAB13168.
GeneID1109818.
KEGGbuc:BU471.
PATRIC21244484. VBIBucAph127364_0480.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085275.
KOK02298.
OMALFMIGFN.
OrthoDBEOG6B35XR.
ProtClustDBCLSK435874.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-471-MONOMER.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014207. Cyt_c_ubiqinol_oxidase_su1.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02843. CyoB. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYOB_BUCAI
AccessionPrimary (citable) accession number: P57543
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names