A0A4Y7XBX8 · A0A4Y7XBX8_9GAMM
- ProteinDihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids561 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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).
Catalytic activity
- N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[protein] + CoA
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | dihydrolipoyllysine-residue acetyltransferase activity | |
Molecular Function | lipoic acid binding | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Alkanindiges
Accessions
- Primary accessionA0A4Y7XBX8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Forms a 24-polypeptide structural core with octahedral symmetry.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-73 | Lipoyl-binding | ||||
Sequence: MEIKAPDLGVDSADVSEILVKVGDSIEKEQSLLVLESAKASVEVPSPASGVIKAIAIRQGQSVKQGDVLFELE | ||||||
Region | 73-118 | Disordered | ||||
Sequence: EGDTAEQPAPNENSNVDESDQVAPAQQMATEQDESASESGIKDVKV | ||||||
Compositional bias | 79-107 | Polar residues | ||||
Sequence: QPAPNENSNVDESDQVAPAQQMATEQDES | ||||||
Domain | 113-186 | Lipoyl-binding | ||||
Sequence: IKDVKVPDLGVDEADVSEILVRVGDSIAKDQSLIVLESAKASVEVPSPVSGTVKEIKLKTGQKVKQGMVILSLE | ||||||
Region | 192-225 | Disordered | ||||
Sequence: ATANNPEPDAKTQQQTAQPDAPVTQLQNSTQASA | ||||||
Domain | 262-299 | Peripheral subunit-binding (PSBD) | ||||
Sequence: YAGPAVRQLARQLGVVLAQVTPSGANQRILKEDVFAFV |
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length561
- Mass (Da)60,235
- Last updated2019-09-18 v1
- Checksum1F4D7A3D24842A11
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 79-107 | Polar residues | ||||
Sequence: QPAPNENSNVDESDQVAPAQQMATEQDES |