A0A6C7HPJ2 · A0A6C7HPJ2_SALEP

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.

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 site50thiamine diphosphate (UniProtKB | ChEBI)
Binding site251-254FAD (UniProtKB | ChEBI)
Binding site274-278FAD (UniProtKB | ChEBI)
Binding site292FAD (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
      G2359_13110
      , G2427_10710
      , G2691_10530
      , G2720_08615
      , G2816_14055
      , G2853_16365
      , G2854_09870
    • Ordered locus names
      SEN0843

Organism names

Accessions

  • Primary accession
    A0A6C7HPJ2

Proteomes

Subcellular Location

Cell inner membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain4-116Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region183-334FAD-binding domain
Domain191-319Thiamine pyrophosphate enzyme central
Region335-530PP-binding domain
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
    572
  • Mass (Da)
    61,707
  • Last updated
    2020-06-17 v1
  • Checksum
    188DEA35ADC23192
MKQTVAAFIAKTLEQAGVKQIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAQAQLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPENAVTHWYHAPHPVVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHEELVALAAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPSDAKIIQIDINPGSIGAHSKVDMALVGDIKATLRALLPLVEEKSNRKFLDKALEHYRDARKGLDDLAKLSDKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATAPGRQVIAMCGDGGFSMLMGDFLSVVQMKLPIKIVVFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKAADVDGALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGRGDEVIELAKTNWLR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM933172
EMBL· GenBank· DDBJ
CAR32426.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQLS010000007
EMBL· GenBank· DDBJ
HAD9860617.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQPD010000006
EMBL· GenBank· DDBJ
HAE0280187.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQPM010000005
EMBL· GenBank· DDBJ
HAE0330270.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQRD010000005
EMBL· GenBank· DDBJ
HAE0517951.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQSA010000006
EMBL· GenBank· DDBJ
HAE0637859.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQTA010000024
EMBL· GenBank· DDBJ
HAE0744802.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQVY010000024
EMBL· GenBank· DDBJ
HAE1095557.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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