ID SYE_BURTA Reviewed; 469 AA. AC Q2SX36; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 104. 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=BTH_I1984; OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / OS CIP 106301 / E264). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(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; CP000086; ABC37833.1; -; Genomic_DNA. DR RefSeq; WP_009890362.1; NZ_CP008785.1. DR PDB; 4G6Z; X-ray; 2.05 A; A=1-469. DR PDBsum; 4G6Z; -. DR AlphaFoldDB; Q2SX36; -. DR SMR; Q2SX36; -. DR GeneID; 66547525; -. DR KEGG; bte:BTH_I1984; -. DR HOGENOM; CLU_015768_6_0_4; -. DR Proteomes; UP000001930; Chromosome I. 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 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..469 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000237349" FT REGION 118..138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 19..34 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 53..65 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 81..93 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 153..160 FT /evidence="ECO:0007829|PDB:4G6Z" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 207..212 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 213..222 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:4G6Z" FT TURN 246..249 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 263..271 FT /evidence="ECO:0007829|PDB:4G6Z" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 285..291 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 306..319 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 322..334 FT /evidence="ECO:0007829|PDB:4G6Z" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 340..345 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 349..356 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 363..370 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 448..454 FT /evidence="ECO:0007829|PDB:4G6Z" FT HELIX 457..465 FT /evidence="ECO:0007829|PDB:4G6Z" SQ SEQUENCE 469 AA; 52046 MW; EEE0D68248D730E0 CRC64; MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC YMSTEELDAL RERQRAAGEK PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN PLTGTVAWDD AVKGRVEISN EELDDLVVAR PDGTPMYNFC VVVDDLDMGI THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ GEKMSKRHGA MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV SVMGLMKDRA STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA AALKTVEWTK EAIAAALKAV LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLLLFGRDVV VSRIEAALA //