ID SYFA_THETH Reviewed; 350 AA. AC P27001; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 24-JAN-2024, entry version 149. 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; OS Thermus thermophilus. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=10092459; DOI=10.1006/jmbi.1999.2617; RA Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.; RT "Crystal structures of phenylalanyl-tRNA synthetase complexed with RT phenylalanine and a phenylalanyl-adenylate analogue."; RL J. Mol. Biol. 287:555-568(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + CC L-phenylalanyl-tRNA(Phe); 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. {ECO:0000305}. CC -!- CAUTION: The sequence shown here has been extracted from PDB entry CC 1B70. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; WP_011229046.1; NZ_DFSU01000029.1. DR PDB; 1B70; X-ray; 2.70 A; A=1-350. DR PDB; 1B7Y; X-ray; 2.50 A; A=1-350. DR PDB; 2AKW; X-ray; 2.80 A; A=85-350. DR PDB; 2ALY; X-ray; 2.60 A; A=85-350. DR PDB; 2AMC; X-ray; 2.70 A; A=85-350. DR PDB; 2IY5; X-ray; 3.10 A; A=1-350. DR PDB; 3TEH; X-ray; 2.85 A; A=1-350. DR PDB; 4TVA; X-ray; 2.60 A; A=1-350. DR PDBsum; 1B70; -. DR PDBsum; 1B7Y; -. DR PDBsum; 2AKW; -. DR PDBsum; 2ALY; -. DR PDBsum; 2AMC; -. DR PDBsum; 2IY5; -. DR PDBsum; 3TEH; -. DR PDBsum; 4TVA; -. DR AlphaFoldDB; P27001; -. DR SMR; P27001; -. DR DIP; DIP-6104N; -. DR MINT; P27001; -. DR GeneID; 3169731; -. DR EvolutionaryTrace; P27001; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; EXP:DisProt. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00496; PheRS_alpha_core; 1. DR DisProt; DP00053; -. DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR004188; Phe-tRNA_ligase_II_N. DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR010978; tRNA-bd_arm. DR NCBIfam; TIGR00468; pheS; 1. DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1. DR Pfam; PF02912; Phe_tRNA-synt_N; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46589; tRNA-binding arm; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..350 FT /note="Phenylalanine--tRNA ligase alpha subunit" FT /id="PRO_0000126786" FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with beta subunit" FT HELIX 102..115 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 134..138 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 144..147 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 192..203 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 214..225 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 230..244 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 251..255 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 261..271 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 272..275 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 276..286 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 319..326 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:2AMC" FT HELIX 340..343 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:1B7Y" SQ SEQUENCE 350 AA; 39259 MW; DEE0237F7CD9A461 CRC64; MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR GQELNAIKAA LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL HPITLMEREL VEIFRALGYQ AVEGPEVESE FFNFDALNIP EHHPARDMWD TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS PMQVRYMVAH TPPFRIVVPG RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL AQALFGPDSK VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL //