SYFA_ARCFU
ID SYFA_ARCFU Reviewed; 474 AA.
AC O28324;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=AF_1955;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89300.1; -; Genomic_DNA.
DR PIR; B69494; B69494.
DR RefSeq; WP_010879447.1; NC_000917.1.
DR AlphaFoldDB; O28324; -.
DR SMR; O28324; -.
DR STRING; 224325.AF_1955; -.
DR EnsemblBacteria; AAB89300; AAB89300; AF_1955.
DR GeneID; 1485176; -.
DR KEGG; afu:AF_1955; -.
DR eggNOG; arCOG00410; Archaea.
DR HOGENOM; CLU_025086_2_2_2; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 22747at2157; -.
DR PhylomeDB; O28324; -.
DR Proteomes; UP000002199; 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 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..474
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126807"
FT BINDING 317
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 356..358
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 396
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT BINDING 398
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 421
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ SEQUENCE 474 AA; 54582 MW; 9937737D67BF8BE5 CRC64;
MLSKIELMLL RSLETGKTYT PEEAAELSGL SKDAVLKAAY MLQERGYVRV IENVRTHYSL
TEEGERYLKE GLPEEKLYSL VKSGVNSMDE LRKRMGREFQ IALGWLRRKG AVEVEGDKVV
PKREPSFDER AALQAIKEGR GVDEGTLKTL MKRKLVTKSE TKQVYIEVMK KPEIELEDII
TDLTPEMLLE GTWRGKQFLK YDITIPAKEI YGGKIHPYER IIEECRKVFL EMGFTEIKGH
YVQPAFWNFD ALFQPQDHPA RDMQDTFYLD RYIDLEGEIV ERVKATHENG WITGSTGWGG
EWSLEKARQL VLRTHTTAIT IHYLAENPEP PQKAFCIDRV YRRETIDATH LPEFDQLEGV
VLDRDVGFKH LLGLLKEFFT KMGFEDVRFR PGYFPYTEPS VEPEVYVEGL GWVELGGAGV
FRKEVTEPLG IRGKVLAWGL GIGRLAMLKI GLKDLRRLYL PDLGWLRSMP VARK
