SYFA_THET8
ID SYFA_THET8 Reviewed; 350 AA.
AC Q5SGX2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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; OrderedLocusNames=TTHA1958;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1451792; DOI=10.1016/0014-5793(92)80215-3;
RA Keller B., Kast P., Hennecke H.;
RT "Cloning and sequence analysis of the phenylalanyl-tRNA synthetase genes
RT (pheST) from Thermus thermophilus.";
RL FEBS Lett. 301:83-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29.
RX PubMed=1508711; DOI=10.1093/nar/20.16.4173;
RA Kreutzer R., Kruft V., Bobkova E.V., Lavrik O.J., Sprinzl M.;
RT "Structure of the phenylalanyl-tRNA synthetase genes from Thermus
RT thermophilus HB8 and their expression in Escherichia coli.";
RL Nucleic Acids Res. 20:4173-4178(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lechler A., Kreutzer R.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=8199244; DOI=10.1016/0300-9084(93)90008-g;
RA Mosyak L., Safro M.;
RT "Phenylalanyl-tRNA synthetase from Thermus thermophilus has four
RT antiparallel folds of which only two are catalytically functional.";
RL Biochimie 75:1091-1098(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7664121; DOI=10.1038/nsb0795-537;
RA Mosyak L., Reshetnikova L., Goldgur Y., Delarue M., Safro M.G.;
RT "Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.";
RL Nat. Struct. Biol. 2:537-547(1995).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000305}.
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DR EMBL; Z12118; CAA78104.1; -; Genomic_DNA.
DR EMBL; X65609; CAA46559.1; -; Genomic_DNA.
DR EMBL; Y15464; CAA75644.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71781.1; -; Genomic_DNA.
DR RefSeq; WP_011229046.1; NC_006461.1.
DR RefSeq; YP_145224.1; NC_006461.1.
DR PDB; 1EIY; X-ray; 3.30 A; A=1-350.
DR PDB; 1JJC; X-ray; 2.60 A; A=1-350.
DR PDB; 1PYS; X-ray; 2.90 A; A=1-350.
DR PDB; 3HFZ; X-ray; 2.90 A; A=1-350.
DR PDBsum; 1EIY; -.
DR PDBsum; 1JJC; -.
DR PDBsum; 1PYS; -.
DR PDBsum; 3HFZ; -.
DR AlphaFoldDB; Q5SGX2; -.
DR SMR; Q5SGX2; -.
DR STRING; 300852.55773340; -.
DR EnsemblBacteria; BAD71781; BAD71781; BAD71781.
DR GeneID; 3169731; -.
DR KEGG; ttj:TTHA1958; -.
DR PATRIC; fig|300852.9.peg.1930; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_025086_0_1_0; -.
DR OMA; DWHNFTA; -.
DR PhylomeDB; Q5SGX2; -.
DR BRENDA; 6.1.1.20; 2305.
DR EvolutionaryTrace; Q5SGX2; -.
DR PRO; PR:Q5SGX2; -.
DR Proteomes; UP000000532; 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_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; IPR004530; Phe-tRNA-synth_IIc_mito.
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 PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..350
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126785"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 17..37
FT /evidence="ECO:0007829|PDB:1EIY"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1EIY"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1EIY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3HFZ"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 192..203
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1EIY"
FT STRAND 214..225
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:1JJC"
SQ SEQUENCE 350 AA; 39259 MW; DEE0237F7CD9A461 CRC64;
MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR GQELNAIKAA
LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL HPITLMEREL VEIFRALGYQ
AVEGPEVESE FFNFDALNIP EHHPARDMWD TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS
PMQVRYMVAH TPPFRIVVPG RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL
AQALFGPDSK VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER
LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL
