Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Biotin/lipoyl attachment
- Biotin--acetyl-CoA-carboxylase ligase
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
- Biotin-binding site
- Single hybrid motif
- Transcriptional repressor, C-terminal
- Biotin protein ligase, C-terminal
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129626 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BPL/LPL catalytic domain-containing protein
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 26.02 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 235 amino acids
Theoretical weight: 26.02 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
- Canonical:
O57883 (Residues: 1-235; Coverage: 100%)
Sequence domains:
Structure domains:
Lipoyl-binding domain-containing protein
Molecule details ›
Chains: C, D
Length: 74 amino acids
Theoretical weight: 7.99 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 74 amino acids
Theoretical weight: 7.99 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
- Canonical: O59021 (Residues: 77-149; Coverage: 49%)
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
