Function and Biology Details
Reaction catalysed:
(1a) ATP + (R)-lipoate = lipoyl-AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glycine cleavage system H-protein/Simiate
- Glycine cleavage system H-protein
- Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
- Lipoyltransferase/lipoate-protein ligase
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- 2-oxo acid dehydrogenase, lipoyl-binding site
- Biotin/lipoyl attachment
- Single hybrid motif
3 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141428 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lipoate-protein ligase A
Molecule details ›
Glycine cleavage system H protein
Molecule details ›
Chains: B, D
Length: 128 amino acids
Theoretical weight: 13.69 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Glycine cleavage H-protein
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 128 amino acids
Theoretical weight: 13.69 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A6T9 (Residues: 2-129; Coverage: 99%)
Sequence domains: Glycine cleavage H-protein
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
