A0A7J7EZM7 · A0A7J7EZM7_DICBM

Function

function

As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety. The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Caution

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

Catalytic activity

Cofactor

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

Note: Binds 2 lipoyl cofactors covalently.

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Cellular Componentpyruvate dehydrogenase complex
Molecular Functiondihydrolipoyllysine-residue acetyltransferase activity
Biological Processacetyl-CoA biosynthetic process from pyruvate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetyltransferase component of pyruvate dehydrogenase complex
  • EC number

Gene names

    • ORF names
      HPG69_018561

Organism names

Accessions

  • Primary accession
    A0A7J7EZM7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_502984416920-576Acetyltransferase component of pyruvate dehydrogenase complex

Interaction

Subunit

Part of the pyruvate dehydrogenase complex (PDHc) that is a multi-enzyme complex composed of multiple copies of three enzymes, pyruvate dehydrogenase (subunits PDH1A and PDHB, E1 component), dihydrolipoamide acetyltransferase (DLAT, E2 component), and dihydrolipoamide dehydrogenase (DLD, E3 component) to which is added an additional protein the E3-binding protein (PDHX, E3BP). In terms of structural architecture, the E2 and E3BP components assemble into a 60meric central core with icosahedral symmetry. The central core is decorated with E1 and E3 proteins. Currently, two alternative models for the E2:E3BP stoichiometry are considered as being either 48:12 (E248-E3BP12) or 40:20 (E240-E3BP20).
Interacts with PDK2 and PDK3. Interacts with SIRT4. Interacts with PDHB

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain5-81Lipoyl-binding
Region98-128Disordered
Compositional bias102-124Pro residues
Domain132-208Lipoyl-binding
Region261-282Disordered
Domain285-322Peripheral subunit-binding (PSBD)

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    576
  • Mass (Da)
    61,506
  • Last updated
    2021-04-07 v1
  • Checksum
    EA30FA98AE94AE14
FLLFLLQVPLPSLSPTMQAGTIARWEKKEGEKINEGELIAEIETDKATVGFESLEECYMAKILVAEGTRDVPVGSVICITVEKPEDVEAFKNYTLDSSAAPTPPAAPAPTPAAPASPPAPSAQAPGSSYPTHMQVVLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILIAEGTRDVPLGTPLCIIVEKEADIPAFADYRPTEVTDLKPQAPPTPAPVSLCSGELTICNFFQKVVPVPPSPQPVAPTPSATRPATPAGPKGRLFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTKAAPAPAAAVPPPAPGLAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKMLEGRSKISVNDFIIKASALACLKVPEANSSWLDTVIRQNHVVDISVAVNTPAGLITPIVFNAHIKGLEVIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEERLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL

Features

Showing features for non-terminal residue, compositional bias.

Type
IDPosition(s)Description
Non-terminal residue1
Compositional bias102-124Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDTQ010001719
EMBL· GenBank· DDBJ
KAF5921161.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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