ID SYE_SHESR Reviewed; 469 AA. AC Q0HWS6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 04-NOV-2026, entry version 107. 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=Shewmr7_1430; OS Shewanella sp. (strain MR-7). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=60481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-7; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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=tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + CC diphosphate; Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA- CC COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; CC EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-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; CP000444; ABI42429.1; -; Genomic_DNA. DR SMR; Q0HWS6; -. DR KEGG; shm:Shewmr7_1430; -. DR HOGENOM; CLU_015768_6_3_6; -. DR OMA; AADDHYM; -. DR CDD; cd00808; GluRS_core; 1. DR FunFam; 1.10.10.350:FF:000001; Glutamate--tRNA ligase; 1. DR FunFam; 3.40.50.620:FF:000007; Glutamate--tRNA ligase; 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; IPR049940; GluQ/Sye. DR InterPro; IPR033910; GluRS_core. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. 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 NCBIfam; TIGR00464; gltX_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 AlphaFoldDB; Q0HWS6; -. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1..469 FT /note="Glutamate--tRNA ligase" FT /id="PRO_1000001963" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 236..240 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 469 AA; 52474 MW; C658740E5154FE3A CRC64; MTTKTRFAPS PTGFLHVGGA RTALYSWLQA RANNGEFVLR IEDTDIERST QAACDAILEG MNWLGLTWDE GPYYQTKRFD RYNEIIAQML EQGTAYKCYC SRERIDALRE AQAANGEAQK YDGCCRDLPA RDTDEPFVVR FKNPIGGSVV FDDHVRGRIE FSNDALDDLI IARTDGVPTY NFCVVVDDWD MGITCVVRGE DHINNTPRQI NILKALGAPI PEYAHVSMIL GDDGAKLSKR HGAVSVMQYR DDGYLPEALL NYLVRLGWSH GDQEVFSLEE MKQLFKLDDI NKAPSAFNTE KLVWLNQHYI KTLDPEYVAS HLQWHMDDQK IDTSNGPALS AVVTALAERA KTLKELAASS RYFYEDFAEF DAEQAKKHLR GVALEPLQLV QQKLAALTEW TVEAIHQAIE ATATELEVGM GKVGMPLRVA VTGAGQSPGL DITLFLIGKA RSEQRISKAI EFVADRINS //