ID A0A1V3BRH7_9GAMM Unreviewed; 476 AA. AC A0A1V3BRH7; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 07-APR-2021, entry version 14. 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 ORFNames=B0684_06540 {ECO:0000313|EMBL:OOC48917.1}; OS Thioalkalivibrio versutus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=106634 {ECO:0000313|EMBL:OOC48917.1, ECO:0000313|Proteomes:UP000188549}; RN [1] {ECO:0000313|EMBL:OOC48917.1, ECO:0000313|Proteomes:UP000188549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AL 2 {ECO:0000313|EMBL:OOC48917.1, RC ECO:0000313|Proteomes:UP000188549}; RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T., RA Sorokin D.Y., Muyzer G.; RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio."; RL Submitted (FEB-2017) 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:0000256|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:0000256|HAMAP- CC 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OOC48917.1}. 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; MVAR01000018; OOC48917.1; -; Genomic_DNA. DR RefSeq; WP_018176100.1; NZ_MVAR01000018.1. DR EnsemblBacteria; OOC48917; OOC48917; B0684_06540. DR Proteomes; UP000188549; Unassembled WGS sequence. 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. 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; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00464; gltX_bact; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, 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}. FT DOMAIN 9..323 FT /note="tRNA-synt_1c" FT /evidence="ECO:0000259|Pfam:PF00749" FT MOTIF 15..25 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT MOTIF 256..260 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" FT BINDING 259 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022" SQ SEQUENCE 476 AA; 52324 MW; 30B66422DE0459F0 CRC64; MRAMTNSIIR TRFAPSPTGL LHLGNVRTAL FSALRARSRG GHFLLRIEDT DAERSRPEFV DALQRDLRWL GLDWDEGFGA GGDAGPYAQS ERGELYDGYY RQLTEQGLAY PCFCSSAELE RGRKRMRAQG KPPRYPGTCA QLSAEEVARR EGEGQKPTLR FRVPLGRTVR FEDGVRGPVS FRTDEIGDFV IRRSDGTPAF FFSNAIDDAL MGVTDVVRGE DHIANTPRQM LLLEALGLAA PAYHHLPLVM GQDGAPLSKR NGSASVEELR TKGYLPVAIL NHLARLGHRY ESDALLSPTE LAAGFSPERI GHSAARHDPQ QLDHWQSEAL RSLSDAEMQA YLEAAGVLEA VAAEQRPALA RLLRDNITRA EEAPLWVAAF AADPAPYSAA AREELTAAGA EFFSAGLEAL DAAEDFPALA KAVGQATERK GRKLFMPLRA ALSGQTFGPE LPRIWEYLGR ERVRLRLEAA RRHAAG //