P11961 · ODP2_GEOSE
- ProteinDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- GenepdhC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids428 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- acetyl-CoA + N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[protein]
Cofactor
Note: Binds 1 lipoyl cofactor covalently.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 399 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | dihydrolipoyllysine-residue acetyltransferase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Geobacillus
Accessions
- Primary accessionP11961
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000162273 | 2-428 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex | |||
Sequence: AFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGYENMTFKGQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEAGPNRRVIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGAKPAPAAAEEKAAPAAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAHRKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTSIDDETEEIIQKHYYNIGIAADTDRGLLVPVIKHADRKPIFALAQEINELAEKARDGKLTPGEMKGASCTITNIGSAGGQWFTPVINHPEVAILGIGRIAEKPIVRDGEIVAAPMLALSLSFDHRMIDGATAQKALNHIKRLLSDPELLLMEA | ||||||
Modified residue | 43 | N6-lipoyllysine | ||||
Sequence: K |
Interaction
Subunit
Forms a 60-polypeptide structural core with icosahedral symmetry.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P11961 | pdhD P11959 | 3 | EBI-1040691, EBI-9021392 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-77 | Lipoyl-binding | ||||
Sequence: AFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLD | ||||||
Compositional bias | 88-108 | Basic and acidic residues | ||||
Sequence: GQEQEEAKKEEKTETVSKEEK | ||||||
Region | 88-123 | Disordered | ||||
Sequence: GQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEA | ||||||
Domain | 130-167 | Peripheral subunit-binding (PSBD) | ||||
Sequence: IAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFL | ||||||
Region | 177-201 | Disordered | ||||
Sequence: AAEEKAAPAAAKPATTEGEFPETRE |
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)46,326
- Last updated2007-01-23 v3
- Checksum2600CD150261ACB0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 88-108 | Basic and acidic residues | ||||
Sequence: GQEQEEAKKEEKTETVSKEEK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X53560 EMBL· GenBank· DDBJ | CAA37630.1 EMBL· GenBank· DDBJ | Genomic DNA |