ID   SYE_NATPD               Reviewed;         571 AA.
AC   Q3IPL2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02076};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_02076};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02076};
DE            Short=GluRS {ECO:0000255|HAMAP-Rule:MF_02076};
GN   Name=gltX {ECO:0000255|HAMAP-Rule:MF_02076};
GN   OrderedLocusNames=NP_3694A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Natronomonadaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC   NCIMB 2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC       step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC       then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-
CC       Rule:MF_02076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-
CC         COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215;
CC         EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_02076};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02076}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_02076}.
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DR   EMBL; CR936257; CAI49938.1; -; Genomic_DNA.
DR   RefSeq; WP_011323556.1; NC_007426.1.
DR   AlphaFoldDB; Q3IPL2; -.
DR   SMR; Q3IPL2; -.
DR   STRING; 348780.NP_3694A; -.
DR   EnsemblBacteria; CAI49938; CAI49938; NP_3694A.
DR   GeneID; 3702761; -.
DR   KEGG; nph:NP_3694A; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OrthoDB; 10470at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.240.100; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.240.10; Ribosomal Protein L25, Chain P; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   InterPro; IPR050132; Gln/Glu-tRNA_Ligase.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   NCBIfam; NF003169; PRK04156.1; 1.
DR   PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..571
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000237425"
FT   REGION          431..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           114..124
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   571 AA;  64418 MW;  80D88F8AB47E9D12 CRC64;
     MDEDLRERIE REAETAALFN ALKHESDAQV GAILGPMMGE NPDFRPHGDE IPGIISPVIE
     RVNGLSDEEK RERLEELAPE KVEALAAEDE GDDRPLPELP NADAYDDVRM RLAPNPNGPW
     HVGHARMPAV IGTYKDRYDG WFCVRFDDTD PETKRPDLDA YGEILDAIDY LGFEPDEVVK
     ASDRVETYYE YGRKLIKAGG AYTCSCDAES FSELKNNAEA CPHRDKDIET TLSEFEAMID
     GEYSAGEMVL RVRTDIEHKN PALRDWVAFR MVDTPHPREE AADYRCWPML DFQSGIDDHE
     FGISHIIRGI DLQDSAKRQQ FVYEYFDWEY PEVIHWGHVQ IDAYDIEMST STIKQLIDDG
     ELDDWDDPRA PTVASLKRRG IRGQAIVNAM VELGTSTSNV DLAMSSVYAE NREFVDDEAD
     RRFFVRDGVE KPLAGGPESA SPPLHPNDED RGRREIPVGD AVYVEPDDVP ADGERVWLKG
     LGPVRHEDGA FVATDDDIEV VRDGAVDVVH WVPAQESVPL RLRTVDGDEA GHAEPGIETY
     DADDIVQFER IGFARIDRHD DEESVAYFAH P
//