ID F2NM49_MARHT Unreviewed; 481 AA. AC F2NM49; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 02-APR-2025, entry version 72. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022}; DE Short=GluRS {ECO:0000256|HAMAP-Rule:MF_00022}; GN Name=gltX {ECO:0000256|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=Marky_0769 {ECO:0000313|EMBL:AEB11519.1}; OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Marinithermus. OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11519.1, ECO:0000313|Proteomes:UP000007030}; RN [1] {ECO:0000313|EMBL:AEB11519.1, ECO:0000313|Proteomes:UP000007030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030}; RX PubMed=22675595; DOI=10.4056/sigs.2435521; RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S., RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J., RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Woyke T.; RT "Complete genome sequence of the aerobic, heterotroph Marinithermus RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent RT chimney."; RL Stand. Genomic Sci. 6:21-30(2012). 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:0000256|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:0000256|HAMAP-Rule:MF_00022}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00022}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00022}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC Glutamate--tRNA ligase type 1 subfamily. CC {ECO:0000256|ARBA:ARBA00007894, ECO:0000256|HAMAP-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; CP002630; AEB11519.1; -; Genomic_DNA. DR RefSeq; WP_013703571.1; NC_015387.1. DR AlphaFoldDB; F2NM49; -. DR STRING; 869210.Marky_0769; -. DR KEGG; mhd:Marky_0769; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_0; -. DR OrthoDB; 9807503at2; -. DR Proteomes; UP000007030; Chromosome. 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 CDD; cd00808; GluRS_core; 1. DR FunFam; 3.40.50.620:FF:000045; Glutamate--tRNA ligase, mitochondrial; 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; IPR049940; GluQ/Sye. 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00022}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00022}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00022}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00022}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00022}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00022}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00022}; Reference proteome {ECO:0000313|Proteomes:UP000007030}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00022}. FT DOMAIN 2..318 FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib FT catalytic" FT /evidence="ECO:0000259|Pfam:PF00749" FT DOMAIN 333..473 FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF19269" FT MOTIF 8..18 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT MOTIF 249..253 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 252 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" SQ SEQUENCE 481 AA; 54638 MW; 1E509E024C5EA09C CRC64; MVTTRIAPSP TGDPHVGTAY IAIFNYVWAR KNNGKFIVRI EDTDRNRYVE GAEARIQEMI RWLGLDYDEG TDIGGPNGPY RQSERTAIYQ AHAAKLIETG AAYRCFCTPE RLEALREEQK KRGLPLGYDG HCRHIPPEEA EARAKAGEPH VVRLKVPRPG QTVVKDELRG LVTYDHAEVP DVVLLKSDGF PTYHLANVVD DHLMGVTDVI RGEEWLVSTP IHVLLYQAFG WEAPLWYHMP LLRAPGGAKL SKRTGHTSVD WYRERGILAE ALMNYLSLMG FSMPDGREIF TLQELIEAFS WERVSLGGPV FDYEKLKWMN GKYIREVLTL EDLTQRVKPF LERAGLEWGS DAYLQRVVAA MRIRFETLEE FVEKARYFFT EAYPFEEKAL KKLKAGLEYV VELKERLGTL PEMDPELTEP LIRGYAAEKG AKPGAVMQPL RAALTGTLQS PGMFELLELL GKDRVLKRLE RAIQTAEAEE A //