Function and Biology Details
Reactions catalysed:
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2)
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2)
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
2-oxoglutarate = succinate semialdehyde + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Thiamin diphosphate-binding fold
- 2-oxoglutarate dehydrogenase E1 component
- Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal
- Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain superfamily
- Transketolase-like, pyrimidine-binding domain
- Dehydrogenase, E1 component
- 2-oxoacid dehydrogenase acyltransferase, catalytic domain
- Chloramphenicol acetyltransferase-like domain superfamily
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Multifunctional 2-oxoglutarate metabolism enzyme (preferred)
PDBe Complex ID:
PDB-CPX-106428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional 2-oxoglutarate metabolism enzyme
Molecule details ›
Chains: A, B
Length: 1113 amino acids
Theoretical weight: 124.1 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 1113 amino acids
Theoretical weight: 124.1 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0R2B1 (Residues: 116-1227; Coverage: 91%)
Sequence domains:
- 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
- Dehydrogenase E1 component
- Transketolase, pyrimidine binding domain
- 2-oxoglutarate dehydrogenase C-terminal
