ID   SYFA_AQUAE              Reviewed;         338 AA.
AC   O67087;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
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; OrderedLocusNames=aq_953;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07051.1; -; Genomic_DNA.
DR   PIR; D70382; D70382.
DR   RefSeq; NP_213650.1; NC_000918.1.
DR   RefSeq; WP_010880588.1; NC_000918.1.
DR   AlphaFoldDB; O67087; -.
DR   SMR; O67087; -.
DR   STRING; 224324.aq_953; -.
DR   EnsemblBacteria; AAC07051; AAC07051; aq_953.
DR   KEGG; aae:aq_953; -.
DR   PATRIC; fig|224324.8.peg.748; -.
DR   eggNOG; COG0016; Bacteria.
DR   HOGENOM; CLU_025086_0_1_0; -.
DR   InParanoid; O67087; -.
DR   OMA; DWHNFTA; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..338
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000126657"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  39504 MW;  DC36592C22FB2305 CRC64;
     MEKLDKILEE LKLLLSSVSS LKELQEVRSK FLGSKGVIKE LLKKIKEVPS EERKEYGKRV
     NLLKEEAEKL IKEKEEELKE RELEEKLKGE WVDLSIPPAR TVGSLHPITV TLERIVTIFR
     GMGFEVEEGP EVEREEYNFD MLNIPKEHPA RDMQDTFYVN REGYLLRTHT SPVQIRTMLK
     KKPPIQIIAP GKVYRRDDDP THSPMFHQVE GLVVNEYANF RHMKYVIEEF LKKFFETDLP
     VRFRTSYFPF TEPSAEVDIG CVICHQEGCR VCKHTGWLEV MGCGMVHPKV LENCGIDTDF
     YQGFAFGMGV ERLAMLLFGI DNIKLFYEND LRFIKQFF