Q8BMF4 · ODP2_MOUSE

  • Protein
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
  • Gene
    Dlat
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Catalytic activity

Cofactor

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

Note: Binds 2 lipoyl cofactors covalently.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site456CoA (UniProtKB | ChEBI)
Binding site470CoA (UniProtKB | ChEBI)
Binding site561CoA (UniProtKB | ChEBI)
Binding site562CoA (UniProtKB | ChEBI)
Binding site586CoA (UniProtKB | ChEBI)
Active site615
Active site619

GO annotations

AspectTerm
Cellular Componentacetyltransferase complex
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Cellular Componentmyelin sheath
Cellular Componentpyruvate dehydrogenase complex
Molecular Functionacetyltransferase activity
Molecular Functiondihydrolipoyllysine-residue acetyltransferase activity
Molecular Functionidentical protein binding
Molecular Functionpyruvate dehydrogenase (NAD+) activity
Biological Processacetyl-CoA biosynthetic process from pyruvate
Biological Processglucose metabolic process
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
  • EC number
  • Alternative names
    • Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    • Pyruvate dehydrogenase complex component E2 (PDC-E2
      ; PDCE2)

Gene names

    • Name
      Dlat

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
    • FVB/N-3
    • NMRI
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8BMF4
  • Secondary accessions
    • Q8K2G8
    • Q8R339
    • Q91ZB1

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

Type
IDPosition(s)Description
Transit peptide1-85Mitochondrion
ChainPRO_000028571786-642Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Modified residue99Phosphoserine
Modified residue131N6-lipoyllysine
Modified residue258N6-lipoyllysine
Modified residue461N6-acetyllysine
Modified residue468N6-succinyllysine
Modified residue542N6-succinyllysine

Post-translational modification

Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity.

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

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) (By similarity).
In terms of structural architecture, the E2 and E3BP components assemble into a 60meric central core with icosahedral symmetry (By similarity).
The central core is decorated with E1 and E3 proteins (By similarity).
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 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region80-99Disordered
Domain90-166Lipoyl-binding 1
Domain217-293Lipoyl-binding 2
Region313-346Disordered
Compositional bias316-341Pro residues
Domain351-388Peripheral subunit-binding (PSBD)

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    642
  • Mass (Da)
    67,942
  • Last updated
    2007-05-01 v2
  • MD5 Checksum
    DF72A82BEE12A3865838C54BD3FD2D41
MWRVCARRARSAVPRDGFRARWAALKEGPGAPCGSPRIGPAAVRCGSGIPRYGVRSLCGWSSGSGTVPRNRLLRQLLGSPSRRSYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEAFKNYTLDLAAAAAPQAAPAAAPAPAAAPAAPSASAPGSSYPTHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGAPLCIIVEKQEDIAAFADYRPTEVTSLKPQAAPPAPPPVAAVPPTPQPVAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPSKAAPAAAAAMAPPGPRVAPAPAGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPITMLL

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict84in Ref. 3; AAL02400
Sequence conflict198in Ref. 1; BAC27715
Sequence conflict225in Ref. 3; AAL02400
Compositional bias316-341Pro residues
Sequence conflict393in Ref. 2; AAH31495
Sequence conflict604in Ref. 2; AAH31495

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK032124
EMBL· GenBank· DDBJ
BAC27715.1
EMBL· GenBank· DDBJ
mRNA
BC026680
EMBL· GenBank· DDBJ
AAH26680.1
EMBL· GenBank· DDBJ
mRNA
BC031495
EMBL· GenBank· DDBJ
AAH31495.1
EMBL· GenBank· DDBJ
mRNA
BC069862
EMBL· GenBank· DDBJ
AAH69862.1
EMBL· GenBank· DDBJ
mRNA
AY044265
EMBL· GenBank· DDBJ
AAL02400.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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