ID SYE_TREPS Reviewed; 537 AA. AC B2S3R2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 91. 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=TPASS_0673; OS Treponema pallidum subsp. pallidum (strain SS14). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae; OC Treponema. OX NCBI_TaxID=455434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS14; RX PubMed=18482458; DOI=10.1186/1471-2180-8-76; RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T., RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A., RA Molla M.N., Albert T.J., Weinstock G.M.; RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14 RT determined with oligonucleotide arrays."; RL BMC Microbiol. 8:76-76(2008). 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; CP000805; ACD71091.1; -; Genomic_DNA. DR RefSeq; WP_010882118.1; NC_021508.1. DR AlphaFoldDB; B2S3R2; -. DR SMR; B2S3R2; -. DR GeneID; 57879197; -. DR KEGG; tpp:TPASS_0673; -. DR PATRIC; fig|455434.6.peg.666; -. DR Proteomes; UP000001202; 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; 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1..537 FT /note="Glutamate--tRNA ligase" FT /id="PRO_1000090117" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 270..274 FT /note="'KMSKS' region" 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 152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 273 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 537 AA; 59840 MW; BD9D58C627BAE37F CRC64; MEVRVRYAPS PTGLQHIGGI RTALFNFLFA RAHAGVFVLR VEDTDRSRCT AAFEQNLYDT LRWLGVSWDE GGGCPETAVK QGARGDGRSV AHAGGAYGPY TQSARTDLYR AQVARLVETG QAYYCFCDAS RLERVRKIRT LNRMPPGYDR HCRELLPEEV RECLASGVPH VIRFKVPLEG STHFRDALLG DIEWQNEEIN PDPILLKSDG FPTYHLANVV DDHAMRITHV LRAQEWVPST PLHLLLYRAF GWQPPLFCHL PMVMGADGHK LSKRHGATSC DEFRNAGYLP EALLNYVAML GCSYGEGQDL FTREQLCAHF SLSRLNKSPA VFDYKKLAWF NGQYIRAKSD EQLCALVWPF IANAGVCGHI PADVEAGAVR TRRFADEAPC APTEAQRSML MRVIPLIKER LRFLTDAPEL VRCFFQEPSL PEQGVFVPKR LDVAQVRAVL VRARGLVHEI VSASEPDVEV LLRAEAEKFG IKLGDFLMPI RVALTGATVS APLVGTIRIL GASRSCARIE HVIRERFSDD SQGVGGG //