ID   SYFA_PYRFU              Reviewed;         499 AA.
AC   Q8U261;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=PF0989;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81113.1; -; Genomic_DNA.
DR   RefSeq; WP_011012126.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U261; -.
DR   SMR; Q8U261; -.
DR   IntAct; Q8U261; 1.
DR   STRING; 186497.PF0989; -.
DR   EnsemblBacteria; AAL81113; AAL81113; PF0989.
DR   GeneID; 41712802; -.
DR   KEGG; pfu:PF0989; -.
DR   PATRIC; fig|186497.12.peg.1048; -.
DR   eggNOG; arCOG00410; Archaea.
DR   HOGENOM; CLU_025086_2_2_2; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 22747at2157; -.
DR   PhylomeDB; Q8U261; -.
DR   Proteomes; UP000001013; 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; 1.10.10.10; -; 1.
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   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46785; SSF46785; 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..499
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000126816"
FT   BINDING         342
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         381..383
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         422
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         424
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         447
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ   SEQUENCE   499 AA;  57751 MW;  8D6E02185A571B2A CRC64;
     MLGYNEKLVL LKLNEVKKAR IEELVKLTGL EQVAIMRALL TLEKEGLAKI SERKERIIRL
     TDLGRKYIQM GLPEIRALNV LKSKKKVKLD ELRGVLTEDE LKPIVGILRK EGWVKVEKTP
     EGLVLEITER GENPEERPID KALKILSEKE YATSEEISKI VPINELKRRK VAQEEEVVER
     IAEITEKGVE LVKKGIELKR EVTSLTPELI ASGKWREVEF KPFNIKAPVK KIYPGKKQPY
     RVFLDKIRRK LIEMGFIEIT VDSLIETQFW NFDALFQPQN HPAREWTDTY QLKYPEKGYL
     PNRELVERVK EAHERGLAGS RGWGYVWSPE RAMFLMPRAH ATALSARQLA KGIEIPGKYF
     TIQRVFRPDV LDRTHLIEFN QIDGFVAAED LTFRHLLGIL KKFAIEIAGA KKVKFFPDYY
     PFTEPSVQLS AYHPELGWVE FGGAGVFREE MTKALGIDVP VIAWGIGIDR LAMFRLGIDD
     IRYLFSYDLK WLREAKLIW