SYFA_PSEAE
ID SYFA_PSEAE Reviewed; 338 AA.
AC Q9I0A3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PA2740;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06128.1; -; Genomic_DNA.
DR PIR; B83303; B83303.
DR RefSeq; NP_251430.1; NC_002516.2.
DR RefSeq; WP_003114409.1; NZ_QZGE01000011.1.
DR PDB; 4P71; X-ray; 2.79 A; C/D=1-338.
DR PDB; 4P72; X-ray; 2.62 A; C/D=1-338.
DR PDB; 4P73; X-ray; 3.03 A; C/D=1-338.
DR PDB; 4P74; X-ray; 2.70 A; C/D=1-338.
DR PDB; 4P75; X-ray; 2.96 A; C/D=1-338.
DR PDBsum; 4P71; -.
DR PDBsum; 4P72; -.
DR PDBsum; 4P73; -.
DR PDBsum; 4P74; -.
DR PDBsum; 4P75; -.
DR AlphaFoldDB; Q9I0A3; -.
DR SMR; Q9I0A3; -.
DR STRING; 287.DR97_5222; -.
DR PaxDb; Q9I0A3; -.
DR PRIDE; Q9I0A3; -.
DR DNASU; 882970; -.
DR EnsemblBacteria; AAG06128; AAG06128; PA2740.
DR GeneID; 882970; -.
DR KEGG; pae:PA2740; -.
DR PATRIC; fig|208964.12.peg.2865; -.
DR PseudoCAP; PA2740; -.
DR HOGENOM; CLU_025086_0_1_6; -.
DR InParanoid; Q9I0A3; -.
DR OMA; DWHNFTA; -.
DR PhylomeDB; Q9I0A3; -.
DR BioCyc; PAER208964:G1FZ6-2779-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
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; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..338
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126744"
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"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4P74"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4P74"
FT STRAND 204..217
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4P72"
SQ SEQUENCE 338 AA; 38064 MW; 6FEA3219E322F0FC CRC64;
MENLDALVSQ ALEAVRHTED VNALEQIRVH YLGKKGELTQ VMKTLGDLPA EERPKVGALI
NVAKEKVQDV LNARKTELEG AALAARLAAE RIDVTLPGRG QLSGGLHPVT RTLERIEQCF
SRIGYEVAEG PEVEDDYHNF EALNIPGHHP ARAMHDTFYF NANMLLRTHT SPVQVRTMES
QQPPIRIVCP GRVYRCDSDL THSPMFHQVE GLLVDEGVSF ADLKGTIEEF LRAFFEKQLE
VRFRPSFFPF TEPSAEVDIQ CVICSGNGCR VCKQTGWLEV MGCGMVHPNV LRMSNIDPEK
FQGFAFGMGA ERLAMLRYGV NDLRLFFDND LRFLGQFR
