SYFA_METMP
ID SYFA_METMP Reviewed; 500 AA.
AC Q6LX56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MMP1496;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF31052.1; -; Genomic_DNA.
DR RefSeq; WP_011171440.1; NC_005791.1.
DR AlphaFoldDB; Q6LX56; -.
DR SMR; Q6LX56; -.
DR STRING; 267377.MMP1496; -.
DR EnsemblBacteria; CAF31052; CAF31052; MMP1496.
DR GeneID; 2762496; -.
DR KEGG; mmp:MMP1496; -.
DR PATRIC; fig|267377.15.peg.1533; -.
DR eggNOG; arCOG00410; Archaea.
DR HOGENOM; CLU_025086_2_2_2; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 22747at2157; -.
DR BioCyc; MMAR267377:MMP_RS07690-MON; -.
DR Proteomes; UP000000590; 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;
KW Reference proteome.
FT CHAIN 1..500
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_1000007665"
FT BINDING 340
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; 58087 MW; 01A841DD88334F72 CRC64;
MELHNDEKRL LKAFQESNEK TMNLEELSKY IEKEKVMRAA FWLSGRDFLE IIENKTKLCE
LNELGNKSLD FGIPERKVAN YIKENNLESI PIKELSKILE KDETGAALGN LKKKGLVEID
KGNIVFKNLN YEDIEEEILK KVSINPDLST YSKDEVKIVE NLKKRGFLNL KEVVDRSFEI
KDAGTEFIKN PIEIKEEITQ LTREMIVSGK WKDYFIRPYD AKIPTEDIYP AKAHPMSKII
QEVNEVLISM GFKEVKSQIV QTEFWNFDTL FEPQDHPARD MQDTFFVKYP NTGKVPKELL
EKVKGIHECG TIDGEKISKG WCYKFDENVS KRTVLRTHTT VSSIKYLASL SESERENPHK
VFCIDRVFRN ETIDYKHLPE FYQCEGIVMA EDVNFDNLVG ILKEFLRKLG FEKVRIRPAY
FPFTEPSLEA EVYMEGKGWL ELLGAGVFRP EVLEPFGIKK PVLAWGIGLS RLAMLRFGLT
DIRELHKNDM EWLKKTAVNE
