P0ABJ9 · CYDA_ECOLI

Function

function

A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H2O, transferring 1 proton/electron.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 protoheme IX center (heme b558) per subunit.
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 protoheme IX center (heme b595, originally called cytochrome a1) per heterodimer, in conjunction with CydB.
heme d cis-diol (UniProtKB | Rhea| CHEBI:62814 )

Note: Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydB.

Activity regulation

90% inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide, at 1 mM and 40 uM respectively.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.1 mMubiquinol-1
0.28 mM2,3,5,6-tetramethyl-p-phenylenediamine
0.68 mMN,N,N',N'-tetramethyl-p-phenylenediamine
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
383 μmol/min/mgfor ubiquinol-1
270 μmol/min/mgfor 2,3,5,6-tetramethyl-p-phenylenediamine
126 μmol/min/mgfor N,N,N',N'-tetramethyl-p-phenylenediamine
pH 7.0, 37 degrees Celsius.

Pathway

Energy metabolism; oxidative phosphorylation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site19Fe (UniProtKB | ChEBI) of heme b b595 (UniProtKB | ChEBI); axial binding residue
Binding site186Fe (UniProtKB | ChEBI) of heme b b558 (UniProtKB | ChEBI); axial binding residue
Binding site393Fe (UniProtKB | ChEBI) of heme b b558 (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentcytochrome complex
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functionelectron transfer activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on diphenols and related substances as donors
Molecular Functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
Biological Processaerobic electron transport chain
Biological Processoxidative phosphorylation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 3.D.4.3.2the proton-translocating cytochrome oxidase (cox) superfamily

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome bd-I ubiquinol oxidase subunit 1
  • EC number
  • Alternative names
    • Cytochrome bd-I oxidase subunit I
    • Cytochrome d ubiquinol oxidase subunit I

Gene names

    • Name
      cydA
    • Synonyms
      cyd-1
    • Ordered locus names
      b0733, JW0722

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
    • MR43L/F152
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0ABJ9
  • Secondary accessions
    • P11026
    • P75754
    • P76823

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-15Periplasmic
Transmembrane16-35Helical
Topological domain36-54Cytoplasmic
Transmembrane55-69Helical
Topological domain70-96Periplasmic
Transmembrane97-114Helical
Topological domain115-128Cytoplasmic
Transmembrane129-146Helical
Topological domain147-186Periplasmic
Transmembrane187-203Helical
Topological domain204-219Cytoplasmic
Transmembrane220-235Helical
Topological domain236-390Periplasmic
Transmembrane391-407Helical
Topological domain408-423Cytoplasmic
Transmembrane424-441Helical
Topological domain442-472Periplasmic
Transmembrane473-487Helical
Topological domain488-522Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

A double cydA/cydB deletion shows increased sensitivity to reductant (beta-mercapoethanol).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis19Loss of cytochrome b595 and heme d, no aerobic growth, complex assembles.
Mutagenesis86No effect.
Mutagenesis126Loss of all cofactors, no aerobic growth, complex assembles.
Mutagenesis126No effect.
Mutagenesis186Loss of cytochrome b558, no aerobic growth, complex assembles, this subunit is more susceptible to proteolysis.
Mutagenesis314Grows aerobically, has altered cytochrome b/d ratio, complex assembles.
Mutagenesis314Loss of cytochrome b595 and heme d, no aerobic growth, loss of complex.
Mutagenesis393Cytochrome b558 shifts to a high spin configuration, complex assembles. Retains about 1% quinol oxidoreductase activity after purification.
Mutagenesis510No effect.

Expression

Induction

Under conditions of low aeration, in stationary phase (at protein level).

Interaction

Subunit

Heterodimer of subunits I and II. Probably interacts with CydX, and overexpressed AppX.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P0ABJ9cydB P0ABK25EBI-906928, EBI-1213195

Complex viewer

View interactors in UniProtKB
View CPX-268 in Complex Portal

Protein-protein interaction databases

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    522
  • Mass (Da)
    58,205
  • Last updated
    2005-10-25 v1
  • MD5 Checksum
    24E689B003B14408A49A151692CF629C
MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLSALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAWYMLKGRDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQEEETNKFAIQIPYALGIIATRSVDTPVIGLKELMVQHEERIRNGMKAYSLLEQLRSGSTDQAVRDQFNSMKKDLGYGLLLKRYTPNVADATEAQIQQATKDSIPRVAPLYFAFRIMVACGFLLLAIIALSFWSVIRNRIGEKKWLLRAALYGIPLPWIAVEAGWFVAEYGRQPWAIGEVLPTAVANSSLTAGDLIFSMVLICGLYTLFLVAELFLMFKFARLGPSSLKTGRYHFEQSSTTTQPAR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict213in Ref. 1; AAA18804

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J03939
EMBL· GenBank· DDBJ
AAA18804.1
EMBL· GenBank· DDBJ
Unassigned DNA
U00096
EMBL· GenBank· DDBJ
AAC73827.2
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA35399.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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