ID A0A1B8QE18_9GAMM Unreviewed; 357 AA.
AC A0A1B8QE18;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ECO:0000313|EMBL:STY95978.1};
GN ORFNames=A9306_08540 {ECO:0000313|EMBL:OBX79575.1}, A9308_04390
GN {ECO:0000313|EMBL:OBX79872.1}, NCTC11091_01788
GN {ECO:0000313|EMBL:STY95978.1};
OS Moraxella atlantae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=34059 {ECO:0000313|EMBL:OBX79872.1, ECO:0000313|Proteomes:UP000092508};
RN [1] {ECO:0000313|EMBL:OBX79575.1, ECO:0000313|Proteomes:UP000092616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 59586 {ECO:0000313|EMBL:OBX79575.1,
RC ECO:0000313|Proteomes:UP000092616};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella atlantae CCUG 59586.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OBX79872.1, ECO:0000313|Proteomes:UP000092508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 66109 {ECO:0000313|EMBL:OBX79872.1,
RC ECO:0000313|Proteomes:UP000092508};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella atlantae CCUG 66109.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:STY95978.1, ECO:0000313|Proteomes:UP000255193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11091 {ECO:0000313|EMBL:STY95978.1,
RC ECO:0000313|Proteomes:UP000255193};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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|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}.
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DR EMBL; LZNA01000041; OBX79575.1; -; Genomic_DNA.
DR EMBL; LZMZ01000009; OBX79872.1; -; Genomic_DNA.
DR EMBL; UGQA01000001; STY95978.1; -; Genomic_DNA.
DR RefSeq; WP_067059354.1; NZ_UGQA01000001.1.
DR AlphaFoldDB; A0A1B8QE18; -.
DR STRING; 34059.A9308_04390; -.
DR OrthoDB; 9800719at2; -.
DR Proteomes; UP000092508; Unassembled WGS sequence.
DR Proteomes; UP000092616; Unassembled WGS sequence.
DR Proteomes; UP000255193; 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_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}; Reference proteome {ECO:0000313|Proteomes:UP000092616}.
FT DOMAIN 142..355
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 275
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 357 AA; 39805 MW; 46C0E6AD27D28C35 CRC64;
MTDLTTSSDA RFDAFSLTLN ELDDAKLQAF GDDAIAWVAT ASTPQDLQTI RVALTGKKSH
LTTWSKQLGT LDADAKKTVG GWLHALRTRI QTALDDAQKQ LAAQALAAKL ASEAIDITLP
ARGQSVGNLH PITQTAERMQ AFFLQAGFEV ATGPEVESDY YNFEALNIPS HHPARAMHDT
FYFDASYVLR THTSSVQIRT MEQGNLPIRI ICPGRVYRND SDQTHSPMFH QLEGLYVSES
TNFAELKGLI DAFLQAFFGR KLHIRFRPSY FPFTEPSAEV DIWAEGDAAS GKGGRWLEVM
GCGMVHPQVL KNCGIDPSRY QGFAFGMGIE RFAMLYYGVQ DLRLFFQNDV RFLKQFA
//
