ID A0A510HW86_THETH Unreviewed; 468 AA. AC A0A510HW86; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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 ECO:0000313|EMBL:BBL83984.1}; GN ORFNames=TthAA229_04650 {ECO:0000313|EMBL:BBL83984.1}; OS Thermus thermophilus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=274 {ECO:0000313|EMBL:BBL83984.1, ECO:0000313|Proteomes:UP000320875}; RN [1] {ECO:0000313|EMBL:BBL83984.1, ECO:0000313|Proteomes:UP000320875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AA2-29 {ECO:0000313|EMBL:BBL83984.1, RC ECO:0000313|Proteomes:UP000320875}; RA Miyazaki K., Tomariguchi N.; RT "Complete Genome Sequences of Thermus thermophilus Strains AA2-20 and RT AA2-29, Isolated from Arima Onsen in Japan."; RL Microbiol Resour Announc 8:e00820-19(2019). 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, ECO:0000256|SAAS:SAAS00986951}. 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, ECO:0000256|SAAS:SAAS01118679}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022, CC ECO:0000256|SAAS:SAAS00987457}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022, CC ECO:0000256|SAAS:SAAS00987444}. 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, ECO:0000256|SAAS:SAAS00986945}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-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; AP019794; BBL83984.1; -; Genomic_DNA. DR Proteomes; UP000320875; Chromosome. DR CDD; cd00808; GluRS_core; 1. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 1.10.8.70; -; 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; IPR020752; aa-tRNA-synth_I_codon-bd_sub1. 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; IPR020061; Glu_tRNA_lig_a-bdl. DR InterPro; IPR033910; GluRS_core. 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, ECO:0000256|SAAS:SAAS00987446}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00987456}; KW Complete proteome {ECO:0000313|Proteomes:UP000320875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|SAAS:SAAS00987453}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00987438, KW ECO:0000313|EMBL:BBL83984.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00987452}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00022, KW ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00987442}. FT DOMAIN 2 312 tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}. FT MOTIF 8 18 'HIGH' region. {ECO:0000256|HAMAP-Rule: FT MF_00022}. FT MOTIF 243 247 'KMSKS' region. {ECO:0000256|HAMAP-Rule: FT MF_00022}. FT BINDING 246 246 ATP. {ECO:0000256|HAMAP-Rule:MF_00022}. SQ SEQUENCE 468 AA; 53967 MW; D96C41B569CC43E3 CRC64; MVVTRIAPSP TGDPHVGTAY IALFNYAWAR KNGGRFIVRI EDTDRARYVP GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLRRG WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI EAFTWERVSL GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLRELYPR LRAQEEWTEV ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA //