ID A0A1V3BRH7_9GAMM Unreviewed; 476 AA. AC A0A1V3BRH7; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 20-DEC-2017, entry version 5. 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 RT Thioalkalivibrio."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a CC two-step reaction: glutamate is first activated by ATP to form CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu). CC {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + CC diphosphate + L-glutamyl-tRNA(Glu). {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 CC family. Glutamate--tRNA ligase type 1 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00022}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0016874; F:ligase activity; IEA:UniProtKB-KW. 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; 1.10.1160.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. 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; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. 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|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037}; KW Complete proteome {ECO:0000313|Proteomes:UP000188549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037, ECO:0000313|EMBL:OOC48917.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037}. FT DOMAIN 9 323 tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}. FT MOTIF 15 25 "HIGH" region. {ECO:0000256|HAMAP-Rule: FT MF_00022}. FT MOTIF 256 260 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_00022}. FT BINDING 259 259 ATP. {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 //