ID SYE_BORRA Reviewed; 506 AA. AC B5RRI1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 84. 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=BRE_371; OS Borrelia recurrentis (strain A1). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borrelia. OX NCBI_TaxID=412418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1; RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185; RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.; RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."; RL PLoS Genet. 4:E1000185-E1000185(2008). 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00022}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-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; CP000993; ACH94615.1; -; Genomic_DNA. DR AlphaFoldDB; B5RRI1; -. DR SMR; B5RRI1; -. DR KEGG; bre:BRE_371; -. DR HOGENOM; CLU_015768_6_3_12; -. DR Proteomes; UP000000612; 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:UniProtKB-UniRule. 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; 1.10.8.70; Glutamate-tRNA synthetase, class I, anticodon-binding domain 1; 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; IPR008925; aa_tRNA-synth_I_cd-bd_sf. DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito. DR InterPro; IPR020752; Glu-tRNA-synth_I_codon-bd_sub1. 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1..506 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000367620" FT MOTIF 24..34 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 266..270 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 121 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 269 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 506 AA; 58487 MW; C76EB3D9597B2950 CRC64; MIFQKRTFFI KRGCVLNIRV RYAPSPTGLQ HIGGIRTALF NYFFAKSFNG KFLLRIEDTD QTRYYKEAEE DLYQSLAWLG IDFDEGPTCG GSYSPYIQSQ RTEIYRKYAK ELIESGNAYY CYCSPDRLER IRKIQTINKM VPGYDRHCRH LNKDEIKDAL SLGISPVIRF KIPFDGETSF NDILLGKITW ANKDISPDPV ILKSDGFPTY HLANVVDDHL MEISHVLRAQ EWISSGSLHV LLYNAFGWNP PIYCHLPMVM GSDGQKLSKR HGATALKQFI DDGYLPEAII NYVTLLGWSY DGKSEFFTKN ELQKLFSIDK ISKSPAVFDY NKLDFFNSHY IRTKEDHELA ELLLPFLQKA GYIKKDSNSC DKEKLLLLVP LIKPRIRKLG DAVGMLRFFY TNISTWNVNE FLGKKKTVRD IYLLLEKIKP VLEGFETRIL SENEQIFYNF AKENNLKIGE VLIPIRIAVL GSKVSPPLFD SLQLLGKVKV FDRINKAQDF LKKYEL //