ID   SYFA_FLAPJ              Reviewed;         339 AA.
AC   A6GVW9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=FP0124;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL42242.1; -; Genomic_DNA.
DR   RefSeq; WP_011962303.1; NC_009613.3.
DR   RefSeq; YP_001295062.1; NC_009613.3.
DR   AlphaFoldDB; A6GVW9; -.
DR   SMR; A6GVW9; -.
DR   STRING; 402612.FP0124; -.
DR   EnsemblBacteria; CAL42242; CAL42242; FP0124.
DR   GeneID; 66553751; -.
DR   KEGG; fps:FP0124; -.
DR   PATRIC; fig|402612.5.peg.126; -.
DR   eggNOG; COG0016; Bacteria.
DR   HOGENOM; CLU_025086_0_1_10; -.
DR   OMA; DWHNFTA; -.
DR   Proteomes; UP000006394; 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..339
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000006829"
FT   BINDING         250
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   339 AA;  39218 MW;  C2782AB8A9DE5852 CRC64;
     MTDKIKEYIA EAKAFSTQNK EKLEEFRIKF LGSKGLVKDI FAEFKNVPND QKKEFGQVIN
     LLKTIAEEKV KTITEELESK EEIKSLYGDL SRPSEHIKIG SRHPISLIKN QIIDIFSNIG
     FNVSEGPEIE DDWHNFTALN LPEYHPARDM QDTFFIQTNP DILLRTHTSS VQVRYMENNK
     PPIRTISPGR VFRNEAVSSR SHCIFHQVEG LYIDKDVSFA DMKQTLLYFT KEMFGKSKIR
     LRPSYFPFTE PSAEIDIYWG LKTETDYRIT KGTGWLEIGG CGMVDPNVLK NCGIEPDQFN
     GFAFGMGIER IAMLIYQIGD IRMFYENDIR FLEQFKSTI