ID   SYFA_PHYAS              Reviewed;         343 AA.
AC   B1VA93;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=PA0532;
OS   Phytoplasma australiense.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/jb.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(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_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; AM422018; CAM11866.1; -; Genomic_DNA.
DR   RefSeq; WP_012359004.1; NC_010544.1.
DR   AlphaFoldDB; B1VA93; -.
DR   SMR; B1VA93; -.
DR   STRING; 59748.PA0532; -.
DR   PRIDE; B1VA93; -.
DR   EnsemblBacteria; CAM11866; CAM11866; PA0532.
DR   KEGG; pal:PA0532; -.
DR   eggNOG; COG0016; Bacteria.
DR   OMA; DWHNFTA; -.
DR   Proteomes; UP000008323; 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..343
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000119400"
FT   BINDING         256
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   343 AA;  39999 MW;  039F2F7B155463E5 CRC64;
     MHNKINLLKE KFEHDLAKNK NSLENLIYLE QKFLGKKSFL QELNQTLKNI PSEKKPAIGK
     LINEFKKTII LSLQKEKQYL KTQKMNLELM QESVDVNLPG FNFSTGSIHP LYQIIEQLED
     LFLSLGYEIK DGNEIESDFY NFEMLNIGKN HPARAMQDSF YINPQKLLRT HTSNIQVKEM
     LANEGKPLKI ISSGKVFRKD NDDATHSHQF MQLEGLVIDQ KINFLNLKET ILTIIKELFG
     DSQEINIRPS YFPFTEPSIE VDLVIRKKDN SKEYLEILGA GLVHPQVLLN ANYNPEKYQG
     FAFGIGIERI AMIKYQIENI RHFYQNDIRF LKQFSKKVKH ENS