AC MF_00281; DC Protein; auto TR HAMAP; MF_00281; -; 1; level=0 XX Names: Phe_tRNA_synth_alpha1 XX ID SYFA DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit; DE Short=PheRS; GN Name=pheS; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Phe) + L-phenylalanine + ATP = L-phenylalanyl-tRNA(Phe) + CC AMP + diphosphate + H(+); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 magnesium ions per tetramer.; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Phe-tRNA synthetase alpha subunit type 1 subfamily. XX DR Pfam; PF01409; tRNA-synt_2d; 1; trigger=no DR NCBIfam; TIGR00468; PheS; 1; trigger=no DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no XX KW Cytoplasm KW Aminoacyl-tRNA synthetase KW Protein biosynthesis KW Ligase KW ATP-binding KW Nucleotide-binding KW Magnesium KW Metal-binding XX GO GO:0005524; F:ATP binding GO GO:0000287; F:magnesium ion binding GO GO:0004826; F:phenylalanine-tRNA ligase activity GO GO:0006432; P:phenylalanyl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT From: SYFA_THETH (P27001) FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with beta subunit" FT Condition: E XX Size: 325-373; Related: MF_00282; Template: P08312; P27001; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: BUCAI and BUCAP lack the conserved Glu that bind magnesium XX # Version: 24 # Last updated date: 2024-09-02 # Created date: 2005-02-28 //