ID   SYE_METAR               Reviewed;         572 AA.
AC   Q0W8L2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=UNCMA_28940;
GN   ORFNames=LRC306;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ35281.1; -; Genomic_DNA.
DR   RefSeq; WP_012037209.1; NC_009464.1.
DR   AlphaFoldDB; Q0W8L2; -.
DR   SMR; Q0W8L2; -.
DR   STRING; 351160.LRC306; -.
DR   EnsemblBacteria; CAJ35281; CAJ35281; LRC306.
DR   GeneID; 5143841; -.
DR   KEGG; rci:LRC306; -.
DR   PATRIC; fig|351160.9.peg.2972; -.
DR   eggNOG; arCOG04302; Archaea.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   Proteomes; UP000000663; 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; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367807"
FT   MOTIF           112..122
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   572 AA;  64577 MW;  286BE9D8D32127DC CRC64;
     METKDIEILI QKFALQNAYK HGSVPQAGAV TGKLLGTHPE LRPHAKELMP IVQKVLADIG
     QMSQDEIKAK LSEIAPELIE ELSVKKEVRR GLPPLDTSML KPGQKVTLRI APNPNGPPSL
     GNARGIIVNH EYARMYDGVF IMRFDDTDPS IKKPMIEAYT WYVEHAKWLG CPPDKVVAAS
     DRLPLYYEQA EKLIDLGKAY VCTCDNEVFH DLKEAGKPCP HRETPPAENM EKWKKMLAGG
     YGGKEAVLRI KTDIAHKDPA MRDWVAFRIV TEPHPKTGTK YMVWPMLDFE SAMEDHFLGV
     THIIRGKDLM KTADKQKYIY RYLGWEYPHV SHWGRVRLLG FGKFSTSVMK KGIEAGEYRG
     WDDPQLPTVV ALKRRGIEPE AIRNVMINMG VTETDIEFSM DTLYAENRKI VDPKANRYFF
     VPDPVVLKVN GAPFTTAKAP LHPQDHKRGF REMCVAENPE ILIPKSDADN ARPGDILRLK
     DLYNVRITGS DPLTGDYIGN DLSVLKQGAK IVQWVTREGG VPTRVIGPDG EFHGIAECDI
     RNELNNVVQF ERFAFVRIDT INGVVLAYYT HP