ID   SYFA_PHOLL              Reviewed;         327 AA.
AC   Q7N3Q0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00281}; OrderedLocusNames=plu2665;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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_00281};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00281}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00281}.
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DR   EMBL; BX571867; CAE15039.1; -; Genomic_DNA.
DR   RefSeq; WP_011146887.1; NC_005126.1.
DR   AlphaFoldDB; Q7N3Q0; -.
DR   SMR; Q7N3Q0; -.
DR   STRING; 243265.plu2665; -.
DR   EnsemblBacteria; CAE15039; CAE15039; plu2665.
DR   GeneID; 24170526; -.
DR   KEGG; plu:plu2665; -.
DR   eggNOG; COG0016; Bacteria.
DR   HOGENOM; CLU_025086_0_1_6; -.
DR   OMA; DWHNFTA; -.
DR   OrthoDB; 469058at2; -.
DR   BioCyc; PLUM243265:PLU_RS13210-MON; -.
DR   Proteomes; UP000002514; 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_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..327
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000126739"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00281"
SQ   SEQUENCE   327 AA;  37256 MW;  48CBB21B690EED71 CRC64;
     MPHLAELVAN ARAAIEDAQD VAALDLVRVE YLGKKGHLTL QMSSLRDLPV EERPAAGAVI
     NQVKQEVQEA LNIRKEKLET DLLNFRLAAE KIDVSLPGRR MENGGLHPVN RTIERIETFF
     GELGFSIESG PEIEDDYHNF DALNIPAHHP ARADHDTFWF DAKRLLRTQT SGVQVRTMHS
     QQPPIRVIAP GRVYRNDYDQ THTPMFHQVE GLIIDRDISF TSLKGTLHDF LTNFFEEDLQ
     VRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL HNVGLDPEIY SGFAFGMGVE
     RLTMLRYGVT DLRAFFENDL RFLKQFK