ID SYFA_CLOBK Reviewed; 339 AA.
AC B1IML3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=CLD_1410;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA44286.1; -; Genomic_DNA.
DR RefSeq; WP_003403382.1; NC_010516.1.
DR AlphaFoldDB; B1IML3; -.
DR SMR; B1IML3; -.
DR GeneID; 5185223; -.
DR KEGG; cbb:CLD_1410; -.
DR HOGENOM; CLU_025086_0_1_9; -.
DR Proteomes; UP000008541; 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:0016740; F:transferase activity; IEA:UniProt.
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.
FT CHAIN 1..339
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_1000114860"
FT BINDING 254
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 339 AA; 38585 MW; 84B7D3FB8A5AFBD0 CRC64;
MRQKLEEIKN SAINELKTTL SKDQLEAIRV KYLGKKGELT QILRGMGALS QEERPIVGKV
ANEVRSYIEE TIKEAFSDIK NKEKSIRLEN ETIDITMPGK KQAVGKRHPL DLTLESMKDI
FISMGFTIEE GPEVELDKYN FEALNIPKNH PARGEQDTFY INDNLVLRTQ TSPIQIRTME
NQKPPIKMIA PGKVYRSDSV DATHSPIFYQ MEGLVVDKGI TFSDLKGTLE LFAKRMFGDK
VKTKFRPHHF PFTEPSAEMD ATCFVCNGEG CKVCKGSGWI ELLGCGMVHP QVLRNCNIDP
EVYSGFAFGF GVDRMVMMKY GIDDIRLLYE SDMRFLNQF
//
