ID A0A166B062_9EURY Unreviewed; 513 AA.
AC A0A166B062;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00282};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00282};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00282,
GN ECO:0000313|EMBL:KZX12696.1};
GN ORFNames=MBCUR_09490 {ECO:0000313|EMBL:KZX12696.1};
OS Methanobrevibacter curvatus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX12696.1, ECO:0000313|Proteomes:UP000077245};
RN [1] {ECO:0000313|EMBL:KZX12696.1, ECO:0000313|Proteomes:UP000077245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX12696.1,
RC ECO:0000313|Proteomes:UP000077245};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00282};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703, ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX12696.1}.
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DR EMBL; LWMV01000163; KZX12696.1; -; Genomic_DNA.
DR RefSeq; WP_067090874.1; NZ_LWMV01000163.1.
DR AlphaFoldDB; A0A166B062; -.
DR STRING; 49547.MBCUR_09490; -.
DR PATRIC; fig|49547.3.peg.1018; -.
DR OrthoDB; 372178at2157; -.
DR Proteomes; UP000077245; Unassembled WGS sequence.
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_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 NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00282};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00282};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00282, ECO:0000313|EMBL:KZX12696.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00282};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00282}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00282};
KW Reference proteome {ECO:0000313|Proteomes:UP000077245}.
FT DOMAIN 254..505
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 353
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 391..393
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 430
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 456
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
SQ SEQUENCE 513 AA; 58948 MW; 9C7AC67D2DBBFC7D CRC64;
MSQTVENIIN ELPIYEKKLL KTLKKDEIKV PEEIVKETGM DIKSVMSATG SLVSKDIISV
NTIENDFVSL TDVGLKYAND GLPERIILSV LIDKKEIAIG DLSNYLEKKD IKIAIGWLAR
KKWAKINKGV LYILDEGEKK GSLKDNDEKL LYELLKSDTI NISVLNENLL NGFKLLNSRK
NILNIKKTKN HEILINKLGL DILKKGFEIK EDATQLSHEQ LKDGSWKDLN YRPYDINTEF
PKIYPGKAHP LRAIIEEIRE VFLNFGFTES IGPILDSAFW NFDSLFQPQD HAAREMQDTF
YMKNPSKAEL PNENLVNKVK NSHEFGGNTG SIGWNYKWDE EIAKQTVLRT HTTGISTRFL
SQNLPPLKMF SIGKVFRRET ITYKHLPEFY QVEGIVAGEN INYQNLLGVL KEFYKKLGFE
VRFRPAYFPY TYLSTECEVY LEEKESWIEL GGSGMFRPEV LEPLGVNVPV LAFGLGIERL
AMIRYDISDI RMLYKSDIKW LRELPLTNGI NLD
//
