A0A4R5L8Q3 · A0A4R5L8Q3_9BURK

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 site50thiamine diphosphate (UniProtKB | ChEBI)
Binding site251-254FAD (UniProtKB | ChEBI)
Binding site274-278FAD (UniProtKB | ChEBI)
Binding site292FAD (UniProtKB | ChEBI)
Binding site408-410thiamine diphosphate (UniProtKB | ChEBI)
Binding site435Mg2+ (UniProtKB | ChEBI)
Binding site435-437thiamine diphosphate (UniProtKB | ChEBI)
Binding site462Mg2+ (UniProtKB | ChEBI)
Binding site462-468thiamine diphosphate (UniProtKB | ChEBI)
Site467Moves 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
      E1N52_29115

Organism names

  • Taxonomic identifier
  • Strain
    • CNPSo 3008
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A4R5L8Q3

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain6-113Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region183-334FAD-binding domain
Domain191-319Thiamine pyrophosphate enzyme central
Domain381-527Thiamine pyrophosphate enzyme TPP-binding
Region533-574Membrane-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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    574
  • Mass (Da)
    61,416
  • Last updated
    2019-07-31 v1
  • Checksum
    439653899E060A3E
MTRIASDYMVDALVKAGVKRVYGVVGDSLNGFTDSLRRDGSIEWVHMRHEESAAFAAGAEAHLTGELAVCCGSCGPGNLHLINGLFDCHRSGVPVLAIAAHIPSTEIGIDYFQATHPEVLFKECSHYVELVSSPEQLPQILNRAMRAAIGRKGVAVVVVPGNVALAPLAAPAPNWIAPAAPSLVRPPLAEVDKLAEMLNESSRVALLCGAGCKDSHTEVIELARKLKAPIVHALRGKEYIEYDNPFDVGMTGLIGFTSGYAAMTSCDMLLMLGTDFPYRQFYPEGAAIAQIDIRPETLGNRCPIDLGVLGTVKDTLGALLPMIEEKTDAAFLNSALEDYQKARRSLDGLAAPEAGSDTIHPQYVTRLVSELADDDAIFACDVGTPVAWAARYLKMNGKRRLIGSFNHGSMANSLLHTIGAQAAFPDRQVISLSGDGGFTMMMGEFLTLVQAGLPVKVVVLNNGTLGFVEMEMKASGFVDTGCDLKNPNFAAMANAMGVKGVRVEHPGELEDALRSAFAHPGPALVDVVSARQELVMPPTTTADQAYKFGLFMLRAVMDGRGHELVDLAKVNLFR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SMOD01000027
EMBL· GenBank· DDBJ
TDG04517.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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