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 27-MAR-2024, entry version 95. 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=UNCMA_28940; 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}. 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; AM114193; CAJ35281.1; -; Genomic_DNA. DR RefSeq; WP_012037209.1; NC_009464.1. DR AlphaFoldDB; Q0W8L2; -. DR SMR; Q0W8L2; -. DR STRING; 351160.LRC306; -. DR GeneID; 5143841; -. DR KEGG; rci:LRC306; -. DR PATRIC; fig|351160.9.peg.2972; -. DR eggNOG; arCOG04302; Archaea. DR OrthoDB; 10470at2157; -. 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; 2.40.240.100; -; 1. DR Gene3D; 3.40.50.620; HUPs; 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_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 PANTHER; PTHR43097:SF4; GLUTAMINE--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..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 //