Q8BMF4 · ODP2_MOUSE
- ProteinDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- GeneDlat
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids642 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[protein] + CoAThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 lipoyl cofactors covalently.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 456 | CoA (UniProtKB | ChEBI) | |||
Binding site | 470 | CoA (UniProtKB | ChEBI) | |||
Binding site | 561 | CoA (UniProtKB | ChEBI) | |||
Binding site | 562 | CoA (UniProtKB | ChEBI) | |||
Binding site | 586 | CoA (UniProtKB | ChEBI) | |||
Active site | 615 | ||||
Active site | 619 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | acetyltransferase complex | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | myelin sheath | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | acetyltransferase activity | |
Molecular Function | dihydrolipoyllysine-residue acetyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | pyruvate dehydrogenase (NAD+) activity | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate | |
Biological Process | glucose metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BMF4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-85 | Mitochondrion | |||
Chain | PRO_0000285717 | 86-642 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | ||
Modified residue | 99 | Phosphoserine | |||
Modified residue | 131 | N6-lipoyllysine | |||
Modified residue | 258 | N6-lipoyllysine | |||
Modified residue | 461 | N6-acetyllysine | |||
Modified residue | 468 | N6-succinyllysine | |||
Modified residue | 542 | N6-succinyllysine | |||
Post-translational modification
Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity.
Keywords
- PTM
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).
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 80-99 | Disordered | |||
Domain | 90-166 | Lipoyl-binding 1 | |||
Domain | 217-293 | Lipoyl-binding 2 | |||
Region | 313-346 | Disordered | |||
Compositional bias | 316-341 | Pro residues | |||
Domain | 351-388 | Peripheral subunit-binding (PSBD) | |||
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length642
- Mass (Da)67,942
- Last updated2007-05-01 v2
- MD5 ChecksumDF72A82BEE12A3865838C54BD3FD2D41
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 84 | in Ref. 3; AAL02400 | |||
Sequence conflict | 198 | in Ref. 1; BAC27715 | |||
Sequence conflict | 225 | in Ref. 3; AAL02400 | |||
Compositional bias | 316-341 | Pro residues | |||
Sequence conflict | 393 | in Ref. 2; AAH31495 | |||
Sequence conflict | 604 | in Ref. 2; AAH31495 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |