ID   SYE_THEON               Reviewed;         573 AA.
AC   B6YSY7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 84.
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}; OrderedLocusNames=TON_0189;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-
CC         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; CP000855; ACJ15674.1; -; Genomic_DNA.
DR   RefSeq; WP_012571147.1; NC_011529.1.
DR   AlphaFoldDB; B6YSY7; -.
DR   SMR; B6YSY7; -.
DR   STRING; 523850.TON_0189; -.
DR   EnsemblBacteria; ACJ15674; ACJ15674; TON_0189.
DR   GeneID; 7017846; -.
DR   KEGG; ton:TON_0189; -.
DR   PATRIC; fig|523850.10.peg.190; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.40.240.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
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_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00463; gltX_arch; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..573
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367806"
FT   MOTIF           106..116
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   573 AA;  66498 MW;  5111B5733FF636EC CRC64;
     MNVEELIMKY ALINAISHKG KANPKAVIGK VLGENPELRP KAKEIIPLVN QIVEQVNGMD
     IEEQEAKLKE IYPEFFEAKK EKKEEKKGLP PLPKAEKGKV VTRFAPNPDG AFHLGNARAA
     ILSHEYARLY GGKFILRFDD TDPKVKRPEP KFYEWIIEDL KWLGFQIDEI HIASDRLEIY
     YKYAEELIKM GKAYVCTCPP EKFRELRDNG IACPHREEPV EVQLERWRKM LNGEYKEGEA
     VVRIKTDLKH PNPAVRDWPA LRIIDNPSHP RTGDKYRVWP LYNFASAIDD HELGVTHIFR
     GQEHAENETR QRYIYDYFGW EYPVTVHHGR LSIEGVILSK SKTRKGIDEG KYFGWDDPRL
     GTIRALKRRG IRPEAIRELI IEVGLKRSDT TISWDNLAAI NRRIVEPIAN RYFFVADPIP
     MYIEGYDEEF VAEIPLHPDH PDRGVRKLKF EPGRPVYVSK DDMELFKPGS FVRLKDLFNV
     EILEVSEEGI KARFHSIEYE IARENRWRMV HWVTEGRACG VLIPQGDELI VRKGLLESDA
     NVKVDDVVQF ERFGFVRIDD VTPEKVVAIF AHK