ID SYE_THEVB Reviewed; 485 AA. AC Q8DLI5; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Glutamate--tRNA ligase; DE EC=6.1.1.17; DE AltName: Full=Glutamyl-tRNA synthetase; DE Short=GluRS; GN Name=gltX; OrderedLocusNames=tll0506; OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1). OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales; OC Thermosynechococcaceae; Thermosynechococcus. OX NCBI_TaxID=197221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-2133 / IAM M-273 / BP-1; RX PubMed=12240834; DOI=10.1093/dnares/9.4.123; RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the thermophilic cyanobacterium RT Thermosynechococcus elongatus BP-1."; RL DNA Res. 9:123-130(2002). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION, RP ABSENCE OF COFACTOR REQUIREMENT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16876193; DOI=10.1016/j.jmb.2006.06.054; RA Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D., RA Heinz D.W.; RT "Crystal structure of a non-discriminating glutamyl-tRNA synthetase."; RL J. Mol. Biol. 361:888-897(2006). CC -!- FUNCTION: Non-discriminating glutamyl-tRNA synthetase. Catalyzes the CC attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate CC is first activated by ATP to form Glu-AMP and then transferred to the CC acceptor end of tRNA(Glu). Acylates both tRNA(Glu) and tRNA(Gln) with CC glutamate, but has 13-fold higher efficiency with tRNA(Glu). CC {ECO:0000269|PubMed:16876193}. 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; CC -!- COFACTOR: CC Note=Does not require zinc.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.79 uM for tRNA-Glu {ECO:0000269|PubMed:16876193}; CC KM=3.7 uM for tRNA-Gln {ECO:0000269|PubMed:16876193}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: This organism lacks a tRNA synthetase for tRNA(Gln). CC Instead, tRNA(Gln) is first charged with Glu, and then the bound CC glutamate is converted to glutamine by GatCAB. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}. 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; BA000039; BAC08058.1; -; Genomic_DNA. DR RefSeq; NP_681296.1; NC_004113.1. DR RefSeq; WP_011056357.1; NC_004113.1. DR PDB; 2CFO; X-ray; 2.45 A; A/B=2-485. DR PDBsum; 2CFO; -. DR AlphaFoldDB; Q8DLI5; -. DR SMR; Q8DLI5; -. DR STRING; 197221.gene:10747095; -. DR EnsemblBacteria; BAC08058; BAC08058; BAC08058. DR KEGG; tel:tll0506; -. DR PATRIC; fig|197221.4.peg.533; -. DR eggNOG; COG0008; Bacteria. DR SABIO-RK; Q8DLI5; -. DR EvolutionaryTrace; Q8DLI5; -. DR Proteomes; UP000000440; 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; IPR020061; Glu_tRNA_lig_a-bdl. 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..485 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119674" FT MOTIF 9..19 FT /note="'HIGH' region" FT MOTIF 248..252 FT /note="'KMSKS' region" FT BINDING 6 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16876193" FT BINDING 192 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16876193" FT BINDING 210..214 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 251 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 17..32 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 51..63 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 79..91 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 102..115 FT /evidence="ECO:0007829|PDB:2CFO" FT TURN 124..127 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:2CFO" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 169..172 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 192..202 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 212..216 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 217..227 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 258..263 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:2CFO" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 292..298 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 313..324 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 329..342 FT /evidence="ECO:0007829|PDB:2CFO" FT TURN 349..352 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 353..363 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 373..381 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 389..395 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 400..410 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 419..433 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 437..449 FT /evidence="ECO:0007829|PDB:2CFO" FT STRAND 450..453 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 457..466 FT /evidence="ECO:0007829|PDB:2CFO" FT HELIX 470..484 FT /evidence="ECO:0007829|PDB:2CFO" SQ SEQUENCE 485 AA; 54362 MW; C3547C6415FDDCBA CRC64; MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR PEYTENILEG LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC TPEELEALRA EQKAKGQAPR YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR AAPRGEIGYP LYNLVVVVDD IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL ILNSTGQKLS KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE RDRPWLFDLA QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS ATILAYLLEH LPAEPALTVA MGQQLIQQAA KAAGVKKGAT MRTLRAALTG AVHGPDLMAA WQILHQRGWD EPRLAAALKQ AQTTS //