Function and Biology Details
Reaction catalysed:
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- tRNA synthetase, B5-domain
- Ferrodoxin-fold anticodon-binding domain superfamily
- Phenylalanyl tRNA synthetase beta chain, core domain
- tRNA-binding domain
- Nucleic acid-binding, OB-fold
- Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type
- Ferrodoxin-fold anticodon-binding domain
11 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Phenylalanyl-tRNA synthetase complex (preferred)
PDBe Complex ID:
PDB-CPX-139580 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phenylalanine--tRNA ligase alpha subunit
Molecule details ›
Chains: A, C
Length: 327 amino acids
Theoretical weight: 36.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2
Length: 327 amino acids
Theoretical weight: 36.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P08312 (Residues: 1-327; Coverage: 100%)
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2
Phenylalanine--tRNA ligase beta subunit
Molecule details ›
Chains: B, D
Length: 795 amino acids
Theoretical weight: 87.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 795 amino acids
Theoretical weight: 87.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P07395 (Residues: 1-795; Coverage: 100%)
Sequence domains:
- Putative tRNA binding domain
- B3/4 domain
- tRNA synthetase B5 domain
- Phenylalanyl tRNA synthetase beta chain CLM domain
- Ferredoxin-fold anticodon binding domain
