A0A6L8DJM3 · A0A6L8DJM3_UNCGE
- ProteinPyruvate dehydrogenase E1 component
- GeneaceE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids893 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Catalytic activity
- H+ + N6-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | pyruvate dehydrogenase (acetyl-transferring) activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase E1 component
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Gemmatimonadota
Accessions
- Primary accessionA0A6L8DJM3
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 205-299 | Transketolase N-terminal | ||||
Sequence: IMSIYQARFNRYLEDRGLKQGNGCKVWAFLGDGETDEPEALGAITLAAREKLDNLIFVVNCNLQRLDGPVRGNGKIIQELEAAFHGAGWNVIKVI | ||||||
Domain | 484-705 | Pyruvate dehydrogenase E1 component middle | ||||
Sequence: DEVFEEFKAGTDGREVSTTMVFTRMLSRLLREPEIGKLIVPIVPDEARTFGMEALFRQCGIYSHAGQLYEPVDIDTLLYYKEAQDGQILEEGITEAGSLSSFVAAGTAYSTHGVNTIPFFIFYSMFGLQRVGDLIWAAAEMRTRGFLLGGTAGRTTLNGEGLQHQDGQSHLLADPVPNLLTYDPAYAYELATIIKDGIRRMYVDQEDLFYYITVQNENYAMP |
Family and domain databases
Sequence
- Sequence statusComplete
- Length893
- Mass (Da)99,968
- Last updated2020-10-07 v1
- ChecksumBABD8FC5AE43EB64