ID SYFA_HAHCH Reviewed; 331 AA.
AC Q2SDJ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00281};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00281};
GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00281}; OrderedLocusNames=HCH_04575;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(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_00281};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00281};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00281}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00281}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00281}.
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DR EMBL; CP000155; ABC31278.1; -; Genomic_DNA.
DR RefSeq; WP_011398343.1; NC_007645.1.
DR AlphaFoldDB; Q2SDJ6; -.
DR SMR; Q2SDJ6; -.
DR STRING; 349521.HCH_04575; -.
DR KEGG; hch:HCH_04575; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_025086_0_1_6; -.
DR OrthoDB; 9800719at2; -.
DR Proteomes; UP000000238; 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 CDD; cd00496; PheRS_alpha_core; 1.
DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 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; IPR004188; Phe-tRNA_ligase_II_N.
DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 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..331
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_1000006840"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00281"
SQ SEQUENCE 331 AA; 37712 MW; 5C39F1F3DF85C122 CRC64;
MENLEGIVDR AKDAVAKAES EQSLEQLRVD YLGKKGRITQ LLKELGRLDA AERPAAGAKI
NEAKLLVQDL INEAKSELSS KNEAAKLAAE SIDVTLPGRK ESLGTLHPVT RTMLRIEDFF
ARSGYTVEEG PEIQDDYHNF EALNIPSHHP ARAMHDTFYF DPKTLLRTHT SPVQIRVMES
SKPPFRMICP GRVYRCDSDM THTPMFHQVE GLMVDKHVSF ADLKSTIVEF LREFFEKDLE
VRFRPSYFPF TEPSAEVDIE WGRNEDGSIK WLEVMGCGMV HPKVFEAAGV DSETYSGFAF
GMGVERLAML RYGVNDLRMF FENDMRFLDQ F
//
