Function and Biology Details
Reaction catalysed:
ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Alanine-tRNA ligase, class IIc
- Threonyl/alanyl tRNA synthetase, SAD
- Alanine-tRNA ligase, archaea
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily
- Translation protein, beta-barrel domain superfamily
- Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily
- Alanyl-tRNA synthetase, class IIc, N-terminal
1 more domain
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Alanine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-129660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 752 amino acids
Theoretical weight: 86.86 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 752 amino acids
Theoretical weight: 86.86 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
- Canonical:
O58035 (Residues: 1-752; Coverage: 82%)
Sequence domains:
Structure domains:
