SYFA_PYRAB
ID SYFA_PYRAB Reviewed; 500 AA.
AC Q9UYX3; G8ZHJ0;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=PYRAB13840;
GN ORFNames=PAB2426;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ248287; CAB50289.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70827.1; -; Genomic_DNA.
DR PIR; D75049; D75049.
DR RefSeq; WP_010868499.1; NC_000868.1.
DR AlphaFoldDB; Q9UYX3; -.
DR SMR; Q9UYX3; -.
DR STRING; 272844.PAB2426; -.
DR EnsemblBacteria; CAB50289; CAB50289; PAB2426.
DR GeneID; 1496773; -.
DR KEGG; pab:PAB2426; -.
DR PATRIC; fig|272844.11.peg.1471; -.
DR eggNOG; arCOG00410; Archaea.
DR HOGENOM; CLU_025086_2_2_2; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 22747at2157; -.
DR PhylomeDB; Q9UYX3; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..500
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126814"
FT BINDING 343
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 382..384
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 423
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 425
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 448
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ SEQUENCE 500 AA; 57847 MW; C16133E4D94BF487 CRC64;
MTLGYNEKLV LLTIAKLEKA SVEEIVKETR LDQVAVMRAI LTLEKEGLIK LHERKEKIIV
LTDIGKEYSK IGLPEIRALR VLREKKKAYL DELKDVLRED ELKAIVGILR REGLANVRKD
EKGLVLEITE KGEKLGERPI DIALKLLSEK GEVSVDEISR IIDVKDLKRR KIAREDERVE
RTVEITEKGK KLVSKGIELK REVTRLTPEL IASGKWREVE LKPFNIKAPV KRIYPGKKQP
YRVFLDKIRR RLIEMGFIEM TVDSLIETQF WNFDALFQPQ NHPAREWTDT YQLKYPEKGY
LPDESLVSRV KEAHERGLAG SRGWGYVWSP ERAMLLMPRA HATALSARQL AKGIEIPGKY
FTIQRVFRPD VLDRTHLIEF NQIDGFVAGE DLTFRHLLGI LKRFAIEIAG AKKVKFFPDY
YPFTEPSVQL SAYHPELGWV EFGGAGVFRE EMTEALGIKV PVIAWGIGID RLAMFKLGID
DIRYLFSYDL RWLREAKLIW
