ID   SYFA_PYRCJ              Reviewed;         488 AA.
AC   A3MUA4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=Pcal_0795;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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_00282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00282};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00282}.
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DR   EMBL; CP000561; ABO08221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MUA4; -.
DR   SMR; A3MUA4; -.
DR   STRING; 410359.Pcal_0795; -.
DR   EnsemblBacteria; ABO08221; ABO08221; Pcal_0795.
DR   KEGG; pcl:Pcal_0795; -.
DR   eggNOG; arCOG00410; Archaea.
DR   HOGENOM; CLU_025086_2_2_2; -.
DR   OMA; QIEGWVM; -.
DR   Proteomes; UP000001431; 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_00282; Phe_tRNA_synth_alpha2; 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; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   Pfam; PF01409; tRNA-synt_2d; 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.
FT   CHAIN           1..488
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000007668"
FT   BINDING         315
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         354..356
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         394
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         419
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ   SEQUENCE   488 AA;  55926 MW;  E0FDB6E135840CD4 CRC64;
     MLVLPPPLYE IVKRAQEWRP LDEIARELGV TQESLMRYVE EGRAKGVLQV DKRYAVAYEL
     TEEGALRVRE GLPEYKLLKA AVCDEARCVI ELKHPEAPLA LANLAKLGVK PRGGVIELSR
     DVYERVLASI EEKQRALAQL DSAPPDLLQE FLRRKLVKKV EKTLIYVKAA APLDSVKPAE
     VKTALTSEDI ATGRWREYYL KPFDLSIEPP QYPAPVPHFF NEFLNYVREV MVGLGFEEVR
     GPILEVEFWN FDALFQAQDH PAREVHDTFY VHWDGPREEP PRHLMEAVGR VHEEKWRYKW
     SPQKALNLVL RTQTTATTIR ALAERGEGAY KVFTIGRVFR PEKLDPKHSM EFHQLDGIVV
     GPGLTFKHLL GQLEQIAKAL GMGRVKFRPA YFPFTSPSVE VYAEHPTLGW VEFGGAGIFR
     PEVTEPLGVK NSRVLAWGWG LDRVAMILLG IDDIRDLFTK DLDKLREYYA RWEKYRRGVG
     TRGIKYTL