AC   MF_00282;
DC   Protein; auto
TR   HAMAP; MF_00282; -; 1; level=0
XX
Names: Phe_tRNA_synth_alpha2
XX
ID   SYFA
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE            Short=PheRS;
GN   Name=pheS;
XX
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per tetramer.;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
case not <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily.
XX
DR   Pfam; PF01409; tRNA-synt_2d; 1; trigger=no
DR   NCBIfam; TIGR00468; PheS; 1; trigger=no
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
XX
case not <OG:Chloroplast>
KW   Cytoplasm
end case
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004826; F:phenylalanine-tRNA ligase activity
GO   GO:0006432; P:phenylalanyl-tRNA aminoacylation
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
case not <OG:Chloroplast>
GO   GO:0005737; C:cytoplasm
end case
XX
FT   From: SYFA_THEKO (Q76KA8)
FT   BINDING         426
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with heterodimeric
FT                   partner"
FT   Condition: E
FT   BINDING         344
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT   Condition: T
FT   BINDING         383..385
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT   Optional; Condition: Q-[IVL]-[DE]
FT   BINDING         424
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT   Condition: [FY]
FT   BINDING         449
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT   Condition: F
XX
Size: 465-553;
Related: MF_00281;
Template: P27002; O26837; A5K9S0; Q9Y285;
Scope:
 Bacteria
 Archaea
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Generally found in archaea, but also present in BORBU and TREPA.
 Possible wrong starts various sequences
XX
# Revision 1.38 2023/06/01
//