Function and Biology Details
Reaction catalysed:
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Threonine-tRNA ligase, class IIa
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- TGS
- Anticodon-binding
- Threonine-tRNA ligase, class IIa, anticodon-binding domain
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Threonine-tRNA ligase catalytic core domain
5 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Threonine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-185681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 645 amino acids
Theoretical weight: 74.56 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 645 amino acids
Theoretical weight: 74.56 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q8NW68 (Residues: 1-645; Coverage: 100%)
Sequence domains:
- TGS domain
- Threonyl and Alanyl tRNA synthetase second additional domain
- tRNA synthetase class II core domain (G, H, P, S and T)
- Anticodon binding domain
