ID SYE2_EHRRW Reviewed; 470 AA. AC Q5HB98; Q5FEZ6; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 110. 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=Erum4310, ERWE_CDS_04490; OS Ehrlichia ruminantium (strain Welgevonden). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=254945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=15637156; DOI=10.1073/pnas.0406633102; RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T., RA Allsopp B.A.; RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple RT tandem repeats of actively variable copy number."; RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium RT reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). 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; CR767821; CAH58157.1; -; Genomic_DNA. DR EMBL; CR925678; CAI26943.1; -; Genomic_DNA. DR RefSeq; WP_011155113.1; NC_006832.1. DR AlphaFoldDB; Q5HB98; -. DR SMR; Q5HB98; -. DR KEGG; eru:Erum4310; -. DR KEGG; erw:ERWE_CDS_04490; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_0_5; -. DR Proteomes; UP000001021; 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..470 FT /note="Glutamate--tRNA ligase 2" FT /id="PRO_0000119561" FT MOTIF 11..21 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 238..242 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 470 AA; 54081 MW; ECF29C177C2889AC CRC64; MLNHVVTRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDSKR SSKELIDSII NSMIWLNIQH DGDIILQSSR ISRHIEIANQ LILNDKAYYC YCSEEEINLE KEEYTKKGLH YKHNCIWKNR NPPIGNCSKV IRLHSDTEGI TEFKDKVYGT IAVNNVQLDD MVLLRSNNTP TYLLSVVVDD YDMGITHIIR GTDHLTNTAR QLLIYNALGW KPPEFAHIPL IHDENGNKLS KRHHALGIHE YKNAGILPEA LLNYLLRMGW SHGNDEVITI DEAIRWFSID KVGQSPARLD SKKLEFLNNH YINATNNATI IEMIIPIIEK TIGYKVNTEK IGYLLNGINE LKKRTKNLVN LANESLFYVE DIPISFDQES LIIIKSNHDI LSILYDNLSK VLNDDWNNST LTSMIKNIVK DYNTKIHNIY HCLRASIIGR INAPSIIDIM VNFQREECLN RIKYARDMVK //