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A0A1H1M1H7 · A0A1H1M1H7_9BRAD

  • 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.

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.

Type
IDPosition(s)Description
Binding site51thiamine diphosphate (UniProtKB | ChEBI)
Binding site277-281FAD (UniProtKB | ChEBI)
Binding site295FAD (UniProtKB | ChEBI)
Binding site411-413thiamine diphosphate (UniProtKB | ChEBI)
Binding site438Mg2+ (UniProtKB | ChEBI)
Binding site438-440thiamine diphosphate (UniProtKB | ChEBI)
Binding site465Mg2+ (UniProtKB | ChEBI)
Binding site465-471thiamine diphosphate (UniProtKB | ChEBI)
Site470Moves 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
      SAMN05444158_0029

Organism names

  • Taxonomic identifier
  • Strain
    • GAS369
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0A1H1M1H7

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain5-117Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region186-337FAD-binding domain
Domain195-322Thiamine pyrophosphate enzyme central
Domain384-530Thiamine pyrophosphate enzyme TPP-binding
Region536-577Membrane-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)
    61,786
  • Last updated
    2017-01-18 v1
  • MD5 Checksum
    093D8CAD7E5EBC847F890379EF81B630
MRIENVADLIAETLIQAGVKRIFGVVGDSLNGLTEALRKRKTIDWIHVRHEEVAAFAAAGEAQITGELAVCAGSCGPGNLHLINGLFDAHRSRTPVLAIAAQIPSGEIGGGYFQETHPQELFRECSHYCELVSDTAQLPYVLENAIRAAVGRRGVAVLVIPGDVALRSSPKRGISPNAGLLPAAPIVRPAEPELTALAELLNNAKRVTLFCGRGCAGAHDSLMQLAEMLKSPMVHALGGKEHVEFDNPYDVGMTGFIGFSSGYAAMHACDVLLMLGTDFPYKQFLPDDAKIAQVDIRPENLGRRCKLDLGIVGDVGATITALLPKLKAKTDSKHLDASRAHYKKARAGLDELARGTPGHKPIHPQYLARLLSEQASEDAVFTADVGTPTIWAARYLAMNGRRRLIGSWVHGSMANAMAHAIGVQASQPARQVISMSGDGGFAMLMGDLITLTQMKLPVKVVIFNNGILGFVALEMKASGFVETGVDLQNPDFATMARAMGIHAVRVEDPGELPNAIRDVLAHDGPAVLDVVTATQELSMPPTITAEQVKGFSLWVLRAVMSGRGDEVVDLAKTNLLPR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LT629750
EMBL· GenBank· DDBJ
SDR79859.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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