ID SYE_METVS Reviewed; 555 AA. AC A6UP25; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=Mevan_0338; OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 OS / SB). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=406327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus vannielii SB."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000742; ABR54247.1; -; Genomic_DNA. DR RefSeq; WP_011972150.1; NC_009634.1. DR AlphaFoldDB; A6UP25; -. DR SMR; A6UP25; -. DR STRING; 406327.Mevan_0338; -. DR GeneID; 5325912; -. DR KEGG; mvn:Mevan_0338; -. DR eggNOG; arCOG04302; Archaea. DR HOGENOM; CLU_001882_1_3_2; -. DR OrthoDB; 10470at2157; -. DR Proteomes; UP000001107; 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 CDD; cd09287; GluRS_non_core; 1. 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; IPR001412; aa-tRNA-synth_I_CS. 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. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..555 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000331007" FT MOTIF 100..110 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076" SQ SEQUENCE 555 AA; 64288 MW; C262B9BFF02900BB CRC64; MKDTVMVYLL ENSIKFNGKP NPKAVMGKIL GGNPDLRNRV NELNEVISKV LKEIEVMSLE EQQIKLNEIA PEGLVQKTER KRKEIELKNA KDKVVMRFAP NPSGPLHIGH ARASVLNDFF AKKYNGKLIL RLEDTDAKRV LPEAYEMIEE DLKWLGIKVD EVIIQSERLE IYYGYGRKLI EMSYAYVCDC NPEEFKELRE KGIPCKCRET TPETNLKLWE KMLAGELDNV AVRLKTDIGH KNPSIRDFPI FRIEKTPHPK NGTKYHVYPL MNLSVTIDDH LMGMTHVLRG KDHIINTEKQ EYIYKYFGWE SPEYIHYGIL KIEGPVLSTS KMHTGILSGE YSGWDDARLG TLRALKKRGI KPEALYKLMV EIGIKQADVK FAWENLNAAN KEIIDKDAKR FFFVDSPKKV IITGFKNKKI NLRMHPDRSD FGNRELLFDG EIYVSDDLEA GKMYRLMELF NIVVEKIENG VIYAHYDSDD ISVARTNKAN IIHWIPIKDS VKVTVIDENA EKIEGFAEKD FLITEEDDFV QFERFGFVRI DEKLDDGYIC YYTHK //