ID   SYE_THEKO               Reviewed;         573 AA.
AC   Q5JH16;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=TK1408;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(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=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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006878; BAD85597.1; -; Genomic_DNA.
DR   RefSeq; WP_011250359.1; NC_006624.1.
DR   AlphaFoldDB; Q5JH16; -.
DR   SMR; Q5JH16; -.
DR   STRING; 69014.TK1408; -.
DR   PRIDE; Q5JH16; -.
DR   EnsemblBacteria; BAD85597; BAD85597; TK1408.
DR   GeneID; 3234725; -.
DR   KEGG; tko:TK1408; -.
DR   PATRIC; fig|69014.16.peg.1370; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   InParanoid; Q5JH16; -.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   PhylomeDB; Q5JH16; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043604; P:amide biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..573
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000119729"
FT   MOTIF           107..117
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   573 AA;  67143 MW;  C7E5A3C000C2D2D2 CRC64;
     MEEIRELVLK YALINAYTHR GKANPKAVIG KVLGENPELR KRAKEIIPLV NEVVNEVNSL
     SLEEQEAKLR EIYPEFFEEK NEKKEEKKGL PPLPKAERGK VVTRFAPNPD GAFHLGNARA
     AILSHEYARM YDGKFILRFD DTDPKVKRPE PIFYEWIKED LEWLGFRIDE IHIASDRLEI
     YYDYAEKLIK MGKAYVCTCP PEKFRELRDK GIACPHREEP VEVQLERWRK MLNGEYREGE
     AVVRIKTDLN HPNPAVRDWP ALRIIDNPNH PRTGNKYRVW PLYNFASAID DHELGVTHIF
     RGQEHAENET RQRYVYEYFG WEYPVTVHHG RLSIEGVILS KSKTRKGIEE GKYLGWDDPR
     LGTIRALRRR GIKPEAIREL IIEVGLKRSD TTISWDNLAA INRKIIEPIA NRYFFVADPI
     PMYVEGAQEF TAEIPLHPDY PERGVRRLKF EPDKPVYVSK DDMELFKPGN FVRLKDLFNV
     EIMEVNENGI RARFHSFEYE VARENRWRMV HWVTEGKACE VWVPEGDELI IREGLLESDA
     DVKVDDIVQF ERFGFVRIDD VRPEKVVAIF AHK