ID SYE_THET8 Reviewed; 468 AA. AC P27000; Q5SL55; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 155. 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=TTHA0438; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1541262; DOI=10.1111/j.1432-1033.1992.tb16656.x; RA Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T., RA Shimizu T., Morikawa K., Miyazawa T., Yokoyama S.; RT "Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning RT of the gltX gene and crystallization of the overproduced protein."; RL Eur. J. Biochem. 204:465-472(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=7701318; DOI=10.1126/science.7701318; RA Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T., RA Miyazawa T., Yokoyama S., Morikawa K.; RT "Architectures of class-defining and specific domains of glutamyl-tRNA RT synthetase."; RL Science 267:1958-1965(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-358. RX PubMed=11224561; DOI=10.1038/84927; RA Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S.; RT "Structural basis for anticodon recognition by discriminating glutamyl-tRNA RT synthetase."; RL Nat. Struct. Biol. 8:203-206(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND RP TRNA. RX PubMed=12554668; DOI=10.1093/emboj/cdg053; RA Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J., RA Vassylyev D.G., Yokoyama S.; RT "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode RT by tRNA binding."; RL EMBO J. 22:676-688(2003). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND RP TRNA, FUNCTION, AND ACTIVITY REGULATION. RX PubMed=17161369; DOI=10.1016/j.str.2006.10.005; RA Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S.; RT "Structural bases of transfer RNA-dependent amino acid recognition and RT activation by glutamyl-tRNA synthetase."; RL Structure 14:1791-1799(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, ECO:0000269|PubMed:11224561, CC ECO:0000269|PubMed:17161369}. 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 -!- ACTIVITY REGULATION: In the absence of bound tRNA, ATP is bound in a CC non-productive mode, and the enzyme cannot activate amino acids. CC {ECO:0000269|PubMed:17161369}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.7 uM for tRNA-Glu {ECO:0000269|PubMed:11224561}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022, CC ECO:0000269|PubMed:11224561}. 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; X64557; CAA45854.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70261.1; -; Genomic_DNA. DR RefSeq; WP_011227935.1; NC_006461.1. DR RefSeq; YP_143704.1; NC_006461.1. DR PDB; 1G59; X-ray; 2.40 A; A/C=1-468. DR PDB; 1GLN; X-ray; 2.50 A; A=1-468. DR PDB; 1J09; X-ray; 1.80 A; A=1-468. DR PDB; 1N75; X-ray; 1.90 A; A=1-468. DR PDB; 1N77; X-ray; 2.40 A; A/B=1-468. DR PDB; 1N78; X-ray; 2.10 A; A/B=1-468. DR PDB; 2CUZ; X-ray; 1.98 A; A=1-468. DR PDB; 2CV0; X-ray; 2.40 A; A/B=1-468. DR PDB; 2CV1; X-ray; 2.41 A; A/B=1-468. DR PDB; 2CV2; X-ray; 2.69 A; A/B=1-468. DR PDB; 2DXI; X-ray; 2.20 A; A/B=1-468. DR PDBsum; 1G59; -. DR PDBsum; 1GLN; -. DR PDBsum; 1J09; -. DR PDBsum; 1N75; -. DR PDBsum; 1N77; -. DR PDBsum; 1N78; -. DR PDBsum; 2CUZ; -. DR PDBsum; 2CV0; -. DR PDBsum; 2CV1; -. DR PDBsum; 2CV2; -. DR PDBsum; 2DXI; -. DR AlphaFoldDB; P27000; -. DR SMR; P27000; -. DR DIP; DIP-29168N; -. DR EnsemblBacteria; BAD70261; BAD70261; BAD70261. DR GeneID; 3168748; -. DR KEGG; ttj:TTHA0438; -. DR PATRIC; fig|300852.9.peg.438; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_0; -. DR PhylomeDB; P27000; -. DR BRENDA; 6.1.1.17; 2305. DR SABIO-RK; P27000; -. DR EvolutionaryTrace; P27000; -. DR Proteomes; UP000000532; 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; 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 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..468 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119683" FT REGION 432..447 FT /note="Interaction with tRNA" FT MOTIF 8..18 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 243..247 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 5..7 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 41 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 187..191 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 205 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 243..247 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 246 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT SITE 354 FT /note="Interaction with tRNA; via carbonyl oxygen" FT SITE 358 FT /note="Essential for discrimination between tRNA(Glu) and FT tRNA(Gln)" FT MUTAGEN 358 FT /note="R->Q: Reduces affinity for tRNA and abolishes the FT ability to discriminate between tRNA(Glu) and tRNA(Gln)." FT /evidence="ECO:0000269|PubMed:11224561" FT CONFLICT 74..77 FT /note="GGPH -> AAPT (in Ref. 1; CAA45854)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 16..31 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:1J09" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:1N75" FT HELIX 52..62 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:1J09" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1G59" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 86..98 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 109..119 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 131..139 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:1J09" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 207..212 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 213..223 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:1J09" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:2CUZ" FT TURN 246..248 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 263..273 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 307..320 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 324..337 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 345..355 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 364..368 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 381..403 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 409..423 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 427..439 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 447..453 FT /evidence="ECO:0007829|PDB:1J09" FT HELIX 456..467 FT /evidence="ECO:0007829|PDB:1J09" SQ SEQUENCE 468 AA; 53910 MW; 920E7F3363AF19E9 CRC64; MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR LRAQEEWTEA ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA //