ID SYE2_EHRCR Reviewed; 469 AA. AC Q2GGL8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 25-MAY-2022, entry version 90. 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}; Synonyms=gltX-2; GN OrderedLocusNames=ECH_0605; OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=205920; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC CRL-10679 / Arkansas; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(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; CP000236; ABD45013.1; -; Genomic_DNA. DR RefSeq; WP_006011666.1; NC_007799.1. DR AlphaFoldDB; Q2GGL8; -. DR SMR; Q2GGL8; -. DR STRING; 205920.ECH_0605; -. DR EnsemblBacteria; ABD45013; ABD45013; ECH_0605. DR KEGG; ech:ECH_0605; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_0_5; -. DR OMA; WDEGPFF; -. DR OrthoDB; 1409413at2; -. DR Proteomes; UP000008320; 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; -; 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 Pfam; PF19269; Anticodon_2; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00464; gltX_bact; 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..469 FT /note="Glutamate--tRNA ligase 2" FT /id="PRO_0000237363" 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 /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 469 AA; 54319 MW; FC59CCB762FB49A0 CRC64; MSHNVITRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDKKR SSKELIDSII NAMSWLKIPY DGEIVLQSKN ISRHIEIANQ LILNNKAYYC YCSEEEINKE KEEFSKKGLY YKHNCIWKNK NFTIDNLTRV IRLRSPTEGV TSFDDKVYGN ITVSNTQLDD MVLLRSDNTP TYLLSVVVDD HDMNITHIIR GTDHLTNTAR QLLIYNALEW NPPKFAHIPL IHDEDGNKLS KRHQAIGIHE YKNLGILPEA ISNYLLRMGW SHEDDEIISM DQAIKWFSIK NIGQSPARLD NKKLEFLNNH YISLTEDEVI LNMIIPIIEK KIGYMLNEVK KGYLLKGLYE LKKRTKNLVN LANESLFYVE DVPISIDQEA SAIIKDYKHV FSILYNNLSR ISEKEWNNSI LTSTIKNISQ NLDIKISNIY HCLRASIVGR MNAPSIIEIM INLQQEECLK RIKYAQNIE //