A0A7J7EZM7 · A0A7J7EZM7_DICBM
- ProteinAcetyltransferase component of pyruvate dehydrogenase complex
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids576 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | dihydrolipoyllysine-residue acetyltransferase activity | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyltransferase component of pyruvate dehydrogenase complex
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7EZM7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-19 | ||||
Chain | PRO_5029844169 | 20-576 | Acetyltransferase 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
Interacts with PDK2 and PDK3. Interacts with SIRT4. Interacts with PDHB
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-81 | Lipoyl-binding | |||
Region | 98-128 | Disordered | |||
Compositional bias | 102-124 | Pro residues | |||
Domain | 132-208 | Lipoyl-binding | |||
Region | 261-282 | Disordered | |||
Domain | 285-322 | Peripheral subunit-binding (PSBD) | |||
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length576
- Mass (Da)61,506
- Last updated2021-04-07 v1
- ChecksumEA30FA98AE94AE14
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Compositional bias | 102-124 | Pro residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACDTQ010001719 EMBL· GenBank· DDBJ | KAF5921161.1 EMBL· GenBank· DDBJ | Genomic DNA |