ID SYE_CUPMC Reviewed; 465 AA. AC Q1LLF7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=Rmet_2140; OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / OS CH34) (Ralstonia metallidurans). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34; RX PubMed=20463976; DOI=10.1371/journal.pone.0010433; RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A., RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C., RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.; RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a RT master survivalist in harsh and anthropogenic environments."; RL PLoS ONE 5:E10433-E10433(2010). 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_00022}. 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_00022}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00022}. 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; CP000352; ABF09019.1; -; Genomic_DNA. DR RefSeq; WP_011516848.1; NC_007973.1. DR AlphaFoldDB; Q1LLF7; -. DR SMR; Q1LLF7; -. DR STRING; 266264.Rmet_2140; -. DR KEGG; rme:Rmet_2140; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_0_4; -. DR Proteomes; UP000002429; 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:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00808; GluRS_core; 1. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1. DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf. DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR033910; GluRS_core. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00464; gltX_bact; 1. DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1. DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF19269; Anticodon_2; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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; Reference proteome. FT CHAIN 1..465 FT /note="Glutamate--tRNA ligase" FT /id="PRO_1000001946" FT MOTIF 11..21 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 243..247 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 246 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 465 AA; 52295 MW; DC16FD3A2048AAFD CRC64; MTQRVRTRFA PSPTGFIHLG NIRSAFYPWA FARRMKGDFI LRIEDTDVER STDVAVDVIL ESMAWLDLDI DEGPFYQMQR MDRYREVVQQ MLDNELAYHC YMSTEELDAL REAQRAAGEK PRYNGFWRPE PGKVLPEPPA GVQPVVRFKN PIGGSVVWDD AVKGRIEISN DELDDLVIAR PDGTPTYNFC VVVDDLDMKI THVIRGDDHV NNTPRQINII RALGGEVPVY AHLPTVLNEQ GEKMSKRHGA LPVTGYRDEG YLPEAVLNYL ARLGWAHGDA EIFSREQFVE WFDLEHLGKS PAQYNPEKLA WLNNHYIKVG DNTRLADLTR PFIEALGGKV EGANLVDVIA LVKDRANTLK EVAQTAMLFY RGEPQADAAL KAEHLTDEIR PALQALATQL AALPEWKREA ISAAFKAVLA EFGLKMPKLA MPVRLLVAGQ LQTPSIDAVL ELFGRDTVLR RLAAA //