SYFA_THEKO
ID SYFA_THEKO Reviewed; 501 AA.
AC Q76KA8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
DE AltName: Full=Tk-pheRSA;
GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=TK0921;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=14607984; DOI=10.1093/jb/mvg175;
RA Shiraki K., Tsuji M., Hashimoto Y., Fujimoto K., Fujiwara S., Takagi M.,
RA Imanaka T.;
RT "Genetic, enzymatic, and structural analyses of phenylalanyl-tRNA
RT synthetase from Thermococcus kodakaraensis KOD1.";
RL J. Biochem. 134:567-574(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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:0000250|UniProtKB:A5K9S0,
CC ECO:0000255|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00282};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.;
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, ECO:0000305}.
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DR EMBL; AB093556; BAC99020.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85110.1; -; Genomic_DNA.
DR RefSeq; WP_011249872.1; NC_006624.1.
DR AlphaFoldDB; Q76KA8; -.
DR SMR; Q76KA8; -.
DR STRING; 69014.TK0921; -.
DR EnsemblBacteria; BAD85110; BAD85110; TK0921.
DR GeneID; 3235101; -.
DR KEGG; tko:TK0921; -.
DR PATRIC; fig|69014.16.peg.899; -.
DR eggNOG; arCOG00410; Archaea.
DR HOGENOM; CLU_025086_2_2_2; -.
DR InParanoid; Q76KA8; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 22747at2157; -.
DR PhylomeDB; Q76KA8; -.
DR BRENDA; 6.1.1.20; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..501
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126818"
FT BINDING 344
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285, ECO:0000255|HAMAP-
FT Rule:MF_00282"
FT BINDING 383..385
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285, ECO:0000255|HAMAP-
FT Rule:MF_00282"
FT BINDING 424
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285, ECO:0000255|HAMAP-
FT Rule:MF_00282"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000250|UniProtKB:A5K9S0, ECO:0000255|HAMAP-
FT Rule:MF_00282"
FT BINDING 449
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285, ECO:0000255|HAMAP-
FT Rule:MF_00282"
SQ SEQUENCE 501 AA; 57603 MW; 908B3D3BAEC27E45 CRC64;
MELSYPEKLT LIKLAELKRA KVEELVKESG LEQVAVMRAL LGLQAKGLAK LHERSERVVK
LTETGMKYAQ IGLPEWRALK VLREKGKATL DDLKDVLSED ELKPIVGLLR REGWANVRKE
DGKLVLEITE KGREASERPI DKALKLLAER GEVPVKEIEK LVPVNELKRR KIGEEDVITE
RVAEITEKGE ELVKKGLELK KEVSVLTPEL IKSGKWREVE FRKFDIKAPV RRIYPGKKQP
YRAFLDKIRR RLIEMGFIEM TVDSLIETQF WNFDALFQPQ NHPAREWTDT YQLKYPKVGS
LPDEELVARV KAAHEHGGDT GSRGWGYVWS PERAMLLMPR AHGTALDARQ LAKGVEIPGK
YFTIQRVFRP DVLDRTHLIE FNQIDGFVVG EDLNFRHLLG ILKRFAVEIA GAKKVKFLPD
YYPFTEPSVQ MSAYHPELGW VEFGGAGIFR EEMTKALGID VPVIAWGIGI DRLAMFKLGI
DDIRYLFSYD LRWLREARLV W
