ID E7RJX5_9BACL Unreviewed; 345 AA.
AC E7RJX5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281};
GN ORFNames=GPDM_13976 {ECO:0000313|EMBL:EGA88717.1};
OS Planococcus donghaensis MPA1U2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA88717.1, ECO:0000313|Proteomes:UP000003052};
RN [1] {ECO:0000313|EMBL:EGA88717.1, ECO:0000313|Proteomes:UP000003052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA88717.1,
RC ECO:0000313|Proteomes:UP000003052};
RX PubMed=21994932; DOI=10.1128/JB.05983-11;
RA Pearson M.D., Noller H.F.;
RT "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT Pathways Controlled by a Conserved Spo0A Regulon.";
RL J. Bacteriol. 193:6106-6106(2011).
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|ARBA:ARBA00000395, ECO:0000256|HAMAP-
CC Rule:MF_00281};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00281};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00281};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00281}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00281}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010207, ECO:0000256|HAMAP-Rule:MF_00281}.
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:EGA88717.1}.
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DR EMBL; AEPB01000052; EGA88717.1; -; Genomic_DNA.
DR RefSeq; WP_008432271.1; NZ_AEPB01000052.1.
DR AlphaFoldDB; E7RJX5; -.
DR eggNOG; COG0016; Bacteria.
DR OrthoDB; 9800719at2; -.
DR Proteomes; UP000003052; 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: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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00281};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00281};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00281};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00281};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00281}.
FT DOMAIN 111..319
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00281"
SQ SEQUENCE 345 AA; 38685 MW; AB19DFD0E46B55D2 CRC64;
MEAQLQELKT QALEKIAEAS TVKELNDVRV AYLGKKGPIT DLLKGMGKLP AEERPKMGAL
VNVVREEVTT QLEARMVLLE EEAINAKLQS ETIDITLPGR PVKTGNAHPL TRVVEEIEDL
FISMGYEVAE GPEVEKDYYN FEALNLPKGH PARDMQDSFY ITEDVLLRTH TSPVQARTME
AKGGEPIKII CPGKVYRRDS DDATHSHQFT QIEGLVIGED IRMSDLKGTL SVFAKKMFGD
DREIRLRPSF FPFTEPSVEM DISCFKCGGS GCNVCKKTGW IEILGAGMVH PNVLEMAGYD
SKRLTGFAFG MGPERIAMLK YGVEDIRHFY TNDVRFLSQF QRTEL
//
