A0A3N2C5V8 · A0A3N2C5V8_9MICO

  • Protein
    Pyruvate dehydrogenase [ubiquinone]
  • Gene
    poxB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO2. It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Activity regulation

The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site49thiamine diphosphate (UniProtKB | ChEBI)
Binding site249-252FAD (UniProtKB | ChEBI)
Binding site272-276FAD (UniProtKB | ChEBI)
Binding site290FAD (UniProtKB | ChEBI)
Binding site406-408thiamine diphosphate (UniProtKB | ChEBI)
Binding site433Mg2+ (UniProtKB | ChEBI)
Binding site433-435thiamine diphosphate (UniProtKB | ChEBI)
Binding site460Mg2+ (UniProtKB | ChEBI)
Binding site460-466thiamine diphosphate (UniProtKB | ChEBI)
Site465Moves into active site upon enzyme activation, plays a role in electron transfer

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionlipid binding
Molecular Functionmagnesium ion binding
Molecular Functionpyruvate dehydrogenase (quinone) activity
Molecular Functionthiamine pyrophosphate binding
Molecular Functionubiquinone binding
Biological Processpyruvate catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate dehydrogenase [ubiquinone]
  • EC number
  • Alternative names
    • Pyruvate oxidase
      (POX
      )
    • Pyruvate:ubiquinone-8 oxidoreductase

Gene names

    • Name
      poxB
    • ORF names
      EDD42_3001

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 14012
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Plantibacter

Accessions

  • Primary accession
    A0A3N2C5V8

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain3-114Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region181-332FAD-binding domain
Domain189-317Thiamine pyrophosphate enzyme central
Domain379-525Thiamine pyrophosphate enzyme TPP-binding
Region531-572Membrane-binding domain

Domain

Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.

Sequence similarities

Belongs to the TPP enzyme family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    578
  • Mass (Da)
    62,229
  • Last updated
    2019-04-10 v1
  • Checksum
    A3693D0D2A0B3463
MSTVAETVVATLQASGVQRVYGLPGDSLNGFTDALRSSGGIDWVHVRHEEAAAFAAAAEAELTGELAVVAASCGPGNLHLINGLFDANRSRVPVLAIAAHIPSSEIGSTYFQETHPQELFRECSVYVELVSVPEQLPRVLEIAMRTAVERRGVAVVVVPGDVMLQRAVSEHVSAIRATQPRILPSEHELDEAARILNAGKRVTILAGAGVAGAHAQLIDTADTLAAPIVHALRGKEHVEYDNPFDVGMTGLLGFASGYHAMLSCDVLLMLGTDFPYPQFFPEDATVIQVDIRGEQIGRRHPVDLPLVGTVRDTLDALLPKLERKTHRKHLEESLKHYRSSRKGLDDLATADHDGQAIHPQYLAKVVDELATDDAVFIPDVGSPVVWASRYLTMNGRRRLIGSFSHGSMANAVSHGLGAQASHPGRQVVALAGDGGLTMLLGELISLTQNKLPVKIIVINNSSLNFVELEMKAAGFVTYGTDLENPDFARVAEGMGIHGERVERASELEGAIRRAFDHDGPALVDVVTARQELSIPPTITAEQMKGFTLYALRTVMSGRGDELLDLANTNLLRRILPGH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RKHL01000001
EMBL· GenBank· DDBJ
ROR82901.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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