ID   SYFA_THEON              Reviewed;         500 AA.
AC   B6YTJ4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=TON_0396;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00282};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00282}.
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DR   EMBL; CP000855; ACJ15881.1; -; Genomic_DNA.
DR   RefSeq; WP_012571353.1; NC_011529.1.
DR   AlphaFoldDB; B6YTJ4; -.
DR   SMR; B6YTJ4; -.
DR   STRING; 523850.TON_0396; -.
DR   PRIDE; B6YTJ4; -.
DR   EnsemblBacteria; ACJ15881; ACJ15881; TON_0396.
DR   GeneID; 7016691; -.
DR   KEGG; ton:TON_0396; -.
DR   PATRIC; fig|523850.10.peg.400; -.
DR   eggNOG; arCOG00410; Archaea.
DR   HOGENOM; CLU_025086_2_2_2; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 22747at2157; -.
DR   Proteomes; UP000002727; Chromosome.
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   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 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; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..500
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000114936"
FT   BINDING         343
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         382..384
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         423
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         448
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ   SEQUENCE   500 AA;  57700 MW;  105AB98943803406 CRC64;
     MELSYQEKLT LIKLNELKKA KFDELVEKTG LDQVAVMRAV LWLQSKGLAR LHEKSERIAK
     LTETGKKYAQ IGLPEWRALK VLRKKGKVTL DDLKEVLSED ELKPIVGLLR KEGWASIRKE
     DGKLVLEITE NGLKAEERAI DRALKLLAEK EAIPVSEIEE IIKVNDLKRR KIAEEDIVTE
     RTVEITPEGE ELANKGLELK EEVSTLTPEL IKSGKWREVE FKRFNIQAPV RRIYPGKKQP
     YRAFLDKIRR RLIEMGFIEM TVDSLIETQF WNFDALFQPQ NHPAREWTDT YQLKYPKSGY
     LPNKELVERV KTAHERGLAG SRGWGYVWSP ERAMLLMPRA HGTALSGRQL AKGVEIPGKY
     FTIQRVFRPD VLDRTHLIEF NQVDGFVVGE DLNFRHLLGI LKRFAVEIAG AKKVKFLPDY
     YPFTEPSVQM SAYHPELGWV EFGGAGIFRE EMTRALGIDV PVIAWGIGID RLAMFKLGID
     DIRYLFSYDL GWLREARLVW