A0A157ZLT8 · A0A157ZLT8_9BURK

  • Protein
    Pyruvate dehydrogenase E1 component
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Predicted
  • Annotation score
    2/5

Function

function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site242Mg2+ (UniProtKB | ChEBI)
Binding site272Mg2+ (UniProtKB | ChEBI)
Binding site274Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionpyruvate dehydrogenase (acetyl-transferring) activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate dehydrogenase E1 component
  • EC number

Gene names

    • ORF names
      AWB82_00893

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LMG 29325
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia

Accessions

  • Primary accession
    A0A157ZLT8

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-15Polar residues
Region1-23Disordered
Domain116-312Transketolase N-terminal
Domain500-711Pyruvate dehydrogenase E1 component middle
Domain729-858Transketolase-like C-terminal

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    901
  • Mass (Da)
    99,832
  • Last updated
    2016-06-08 v1
  • Checksum
    7B82E04EB97B77A0
MTDLSSGTTQLLSIAKGREDTDPGETAEWLEALDAVVAHVGKDRAQYLFDRLAEHALSVGVESSRARATPYANTIPVSQQQPYPGNLDTEEKLAAVLRWNALAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFKAADENNGGDIVYFQPHSSPGVYARAFLEGFLGEEHLKHYRREIAGPGLCSYPHPWLMPDFWQFPTGSMGIGPINSIYQARFMRYLQNRNLQRTEGRKVWGFFGDGEMDEPESIGALSLAAREQLDNLVFVINCNLQRLDGPVRSNGRIVDELEAQFTGAGWNVIKVLWGSDWDALFARDRTNALLRAFAHTVDGQFQTFSANDGRYNRERFFGQNPELAALVAHMSDEDIDRLRRGGHDVRKLYAAYAKALSHKGQPTVILAKTMKGFGMGTVGQGRMTTHQQKKLDLDDLKQFRDRFRLPLSDEDVEQVKFYKPADNAPEMRYLHERRAALGGYLPRRRAKASLGLTPPALGTWGQFALDASGKEMSTTMAFVRMLGSLLKDKTLGPRVVPVVADEARTFGMANLFRQVGIYSPLGQLYEPEDMGSMLYYREDTRGQILEEGISEAGAVSSWIAAATSYSVHDLPMLPFYIYYSMFGFQRIGDLIFAAADQRSRGFLIGATAGRTTLGGEGLQHQDGTSHLSASTIPNCRAYDPAFAYEVAAIVDEGMQEMMERQNDVFYYVTVTNENYAQPSAPGGSLDAPTREGILRGIYRIGGDANAQVQLLGSGAILNEAAAARAMLKDDWNIDAALWSVTSYTELHRDGASCERAARLTDDANVPFVTRALEGSRGPVIAATDYVRAVPELIRAYVPRRYVTLGTDGFGRSDTRQSLREFFEVDRVSIVIAALKSLVDEGVIDSLTLKTAREKYGKTRESQDAPWLR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FCOJ02000004
EMBL· GenBank· DDBJ
SAK46492.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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