ID SYE2_WOLTR Reviewed; 453 AA. AC Q5GSI3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 24-JAN-2024, entry version 107. DE RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=Wbm0453; OS Wolbachia sp. subsp. Brugia malayi (strain TRS). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=292805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TRS; RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121; RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S., RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., RA Koonin E., Slatko B.; RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a RT human pathogenic nematode."; RL PLoS Biol. 3:599-614(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_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; AE017321; AAW71041.1; -; Genomic_DNA. DR RefSeq; WP_011256651.1; NC_006833.1. DR AlphaFoldDB; Q5GSI3; -. DR SMR; Q5GSI3; -. DR STRING; 292805.Wbm0453; -. DR KEGG; wbm:Wbm0453; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_5; -. DR OMA; WDEGPFF; -. DR Proteomes; UP000000534; 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. FT CHAIN 1..453 FT /note="Glutamate--tRNA ligase 2" FT /id="PRO_0000119702" FT MOTIF 10..20 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 232..236 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 453 AA; 51501 MW; E5B511D840657C7A CRC64; MPNIVTRFAP SPTGFLHIGG ARTALFNWLY AKHHGGRFLL RIEDTDRKRS TQEAIDAIIN GLKWLGVSYD GEIVYQSKRI ERHIEVANLL VEKGKAYCCC CPEDKVAEKK AKAREERKIY KHKCTSVIPD AKPVVRFNVP DSQEIIVDDK IYGHIKVNSD QLDDMVILRS DNTPTYIFAV VVDDHDAGIT DIIRGSDHLT NTFKQVLIYQ ALDFDIPRFA HVPLIHGRDG NKLSKRHGAT SVCDYEKMGI LPKAMRNYLL RLGWSHGNDE IISNEQAVKW FNLESIGRSP ARLNFKKLEH LNNHYINNMS NEDILTLMLG ESTLTNKKKN YLLQGLTELK KRANYLTELL DLAQFYIKDP PFDLSEEAEQ VVKSNLDIIK LLASFLSNIG DKNWNKGFLS SQVKEFSKLH SAKISDIYHS LRAPITGVMD APGIIDIMII LGKDECIRRL QAV //