ID SYE_SYMTH Reviewed; 482 AA. AC Q67TJ2; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 112. 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}; OrderedLocusNames=STH16; OS Symbiobacterium thermophilum (strain T / IAM 14863). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae; OC Symbiobacterium. OX NCBI_TaxID=292459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T / IAM 14863; RX PubMed=15383646; DOI=10.1093/nar/gkh830; RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., RA Ikeda H., Hattori M., Beppu T.; RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium RT that depends on microbial commensalism."; RL Nucleic Acids Res. 32:4937-4944(2004). 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; AP006840; BAD39001.1; -; Genomic_DNA. DR RefSeq; WP_011194151.1; NC_006177.1. DR AlphaFoldDB; Q67TJ2; -. DR SMR; Q67TJ2; -. DR STRING; 292459.STH16; -. DR KEGG; sth:STH16; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_9; -. DR OrthoDB; 9807503at2; -. DR Proteomes; UP000000417; 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; 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; 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. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. FT CHAIN 1..482 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119673" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 250..254 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 253 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 482 AA; 55490 MW; EEC40EB190A7FBFD CRC64; MTVRVRIAPS PTGPIHVGNV HTALFNWLFA RHHGGKFILR FEDTDLERSR PEWEQVIFED LKWLGIDWDE GPDIGGPYGP YRQTERLDLY RKYAQQLLES GHVYKCYCTK EEEDADRREA QAAGRPYQYK GRCRDLTPEQ QAAFEAEGRK PVLRFRVPRG EVIRFNDLVR GPIEVPTDSI GDFIIMRANG MPLYNFAVVV DDVTMNITHV LRGEGHIPNT PVQILIYQAL GFPVPEFGHL GHMTNPERGK LSKRKGEAAI RDYREQGYLP EAMLNFMSLL GWTPPGAESG REFLTKEELI REFDLSRVTK ASSVFDRNKL NWMNGVYIRK KSLEEFAELA LPFVVSAGLC TEEQARARWD WFKEVMAQVH ERVETLAEIP QHVDIFLKDE IEMDEKAARK FLTEAVKPFF QRVSEGLRSV EWSVPAIEQL VRSIQEEMGL TPKESFQPIR VAITGRTASP GLFETIYLIG RERVLERMAP YC //