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)
- Threonyl/alanyl tRNA synthetase, SAD
- TGS
- Anticodon-binding
- Threonine-tRNA ligase, class IIa, anticodon-binding domain
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
6 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Threonine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-141712 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Threonine--tRNA ligase
Molecule details ›
Chain: A
Length: 642 amino acids
Theoretical weight: 74.12 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains:
Length: 642 amino acids
Theoretical weight: 74.12 KDa
Source organism: Escherichia coli
UniProt:
- Canonical:
P0A8M3 (Residues: 1-642; 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
