SYFA_THETH
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 03-AUG-2022, entry version 142.
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; Deinococcus-Thermus; 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}.
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DR RefSeq; WP_011229046.1; NC_006461.1.
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; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR DisProt; DP00053; -.
DR Gene3D; 3.30.930.10; -; 1.
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; IPR004530; Phe-tRNA-synth_IIc_mito.
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 PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 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
