ID   SYFA_SYNAS              Reviewed;         338 AA.
AC   Q2LR28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=SYNAS_06560;
GN   ORFNames=SYN_01721;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC76535.1; -; Genomic_DNA.
DR   RefSeq; WP_011416569.1; NC_007759.1.
DR   AlphaFoldDB; Q2LR28; -.
DR   SMR; Q2LR28; -.
DR   STRING; 56780.SYN_01721; -.
DR   EnsemblBacteria; ABC76535; ABC76535; SYN_01721.
DR   KEGG; sat:SYN_01721; -.
DR   eggNOG; COG0016; Bacteria.
DR   HOGENOM; CLU_025086_0_1_7; -.
DR   OMA; DWHNFTA; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000001933; 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..338
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000006911"
FT   BINDING         253
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   338 AA;  38100 MW;  CE9BF3117505E747 CRC64;
     MIEDLKELQN KAEAEIKAAK TETDLAAVRV RYLGRKGLLT QFLRNLGQLS IEEKQIFGKR
     ANEIKTILSS RFDEAQTVIA ALKKESVLRA EALDVTLPGR SSGYGRAHPV TQVLEEICAI
     FSEIGFSIAE GPEIESDYYN FEALNIPKDH PARDMQDTFY VEEAIVLRTH TSPVQIRTME
     KQSPPVKIIS PGRVYRPDSD VSHTPMFHQV EGLLVDRGIT FGDLKGLLNA FLKQIFGEET
     VLRFRPSYFP FTEPSAEVDI RCVICRGKGC RVCGQSGWLE ILGSGMVDPA VFENVGYDPE
     EYSGFAFGLG VERIAMLKYG ITDIRLFFEN ERRFLQQF