A0A4Y7XBX8 · A0A4Y7XBX8_9GAMM

  • Protein
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

(R)-lipoate (UniProtKB | Rhea| CHEBI:83088 )

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functiondihydrolipoyllysine-residue acetyltransferase activity
Molecular Functionlipoic acid binding
Biological Processacetyl-CoA biosynthetic process from pyruvate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
  • EC number

Gene names

    • ORF names
      E2B99_07495

Organism names

  • Taxonomic identifier
  • Strain
    • NFYY 23406
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Alkanindiges

Accessions

  • Primary accession
    A0A4Y7XBX8

Proteomes

Subcellular Location

Interaction

Subunit

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-73Lipoyl-binding
Region73-118Disordered
Compositional bias79-107Polar residues
Domain113-186Lipoyl-binding
Region192-225Disordered
Domain262-299Peripheral subunit-binding (PSBD)

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    561
  • Mass (Da)
    60,235
  • Last updated
    2019-09-18 v1
  • Checksum
    1F4D7A3D24842A11
MEIKAPDLGVDSADVSEILVKVGDSIEKEQSLLVLESAKASVEVPSPASGVIKAIAIRQGQSVKQGDVLFELEGDTAEQPAPNENSNVDESDQVAPAQQMATEQDESASESGIKDVKVPDLGVDEADVSEILVRVGDSIAKDQSLIVLESAKASVEVPSPVSGTVKEIKLKTGQKVKQGMVILSLEHSEANATANNPEPDAKTQQQTAQPDAPVTQLQNSTQASAYPQESIQLGNPTHTPAQDQVQGQSLNAEQIKANSEVYAGPAVRQLARQLGVVLAQVTPSGANQRILKEDVFAFVKQTLGTDKVATSGQHAVLASNGLPALPDFEKFGGSTLQPMSRLQQVSVPQLSLNNYIPQVTQFDQADITELENWRNTLKADYRKQNISLTILAFIVKAVAYLLKKESYFNSHLADDQKAIVVRNEIHLGIAVATQDGLTVPVLRNPDTLSIQDIAIQLGKLSQKARDKKLKPQELQGASFTITSLGSIGGTAFTPLVNWPQVAILGISPASMQPVWSGQDFKPRLMLPLSLSYDHRVINGADAARFTHALSEILSDIRRVLL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias79-107Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SNTY01000025
EMBL· GenBank· DDBJ
TEU26846.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp