A0AA96UJY8 · A0AA96UJY8_9BACI
- ProteinDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- GeneodhB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids417 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO2.
Catalytic activity
- N6-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N6-[(R)-S8-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]
Cofactor
Note: Binds 1 lipoyl cofactor covalently.
Pathway
Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | oxoglutarate dehydrogenase complex | |
Molecular Function | dihydrolipoyllysine-residue succinyltransferase activity | |
Biological Process | L-lysine catabolic process to acetyl-CoA via saccharopine | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0AA96UJY8
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Forms a 24-polypeptide structural core with octahedral symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3).
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-76 | Lipoyl-binding | ||||
Sequence: MAEIKVPELAESISEGTIAQWLKQPGDYVEQGEYLLELETDKVNVELTAEESGVLQEVLKDSGDTVQVGEIIGTIS | ||||||
Region | 75-191 | Disordered | ||||
Sequence: ISEGAGESSAPAPTEKAESKESVKEEKQAEPAAQEVSEEAQSEAKSRTIASPSARKLAREKGIDLSQVPTGDPLGRVRKQDVEAYEKPASKPAPQQKQQPQAPKAQQSFDKPVEVQK | ||||||
Compositional bias | 91-107 | Basic and acidic residues | ||||
Sequence: AESKESVKEEKQAEPAA | ||||||
Domain | 123-160 | Peripheral subunit-binding (PSBD) | ||||
Sequence: IASPSARKLAREKGIDLSQVPTGDPLGRVRKQDVEAYE | ||||||
Compositional bias | 166-180 | Polar residues | ||||
Sequence: PAPQQKQQPQAPKAQ |
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length417
- Mass (Da)45,956
- Last updated2024-03-27 v1
- Checksum0700BC2CB580C816
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 91-107 | Basic and acidic residues | ||||
Sequence: AESKESVKEEKQAEPAA | ||||||
Compositional bias | 166-180 | Polar residues | ||||
Sequence: PAPQQKQQPQAPKAQ |