ID SYE_AZOBR Reviewed; 446 AA. AC P45631; O07044; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 13-SEP-2023, entry version 109. 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}; OS Azospirillum brasilense. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Azospirillaceae; Azospirillum. OX NCBI_TaxID=192; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sp245; RA Costacurta A., Keijers V., Vanderleyden J.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7; RX PubMed=9608743; DOI=10.1007/s002849900317; RA Zimmer W., Wesche M., Timmermans L.; RT "Identification and isolation of the indole-3-pyruvate decarboxylase gene RT from Azospirillum brasilense Sp7: sequencing and functional analysis of the RT gene locus."; RL Curr. Microbiol. 36:327-331(1998). 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 -!- 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; U17699; AAA61907.1; -; Genomic_DNA. DR EMBL; X99587; CAA67900.1; -; Genomic_DNA. DR AlphaFoldDB; P45631; -. DR SMR; P45631; -. 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:InterPro. 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; 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; 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. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..446 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119496" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 240..244 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 243 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT CONFLICT 6 FT /note="P -> R (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 39 FT /note="V -> L (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 80..81 FT /note="AT -> RY (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="S -> V (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="A -> S (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="P -> R (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="S -> A (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 177 FT /note="A -> R (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="L -> V (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 220..223 FT /note="VGGA -> LTNSEGGGV (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="T -> A (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 382 FT /note="K -> E (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 423..424 FT /note="GQ -> PE (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" FT CONFLICT 438 FT /note="H -> E (in Ref. 1; AAA61907)" FT /evidence="ECO:0000305" SQ SEQUENCE 446 AA; 49179 MW; A7CE141B79416572 CRC64; MSVAVPFAPS PTGLLHVGNV RLALVNWLFA RKAGGNFLVR LDDTDEERSK PEYAEGIERD LTWLGLTWDR FARESDRYGA TDEVAAALKA SGRLYPCYET PEELNLKRAS LSSQGRPPIY DRAALRLGDA DRARLEAEGR KPHWRFKLEH TPVEWTDLVR GPVHFEGSAL SDPVLIAEDG RPLYTLTSVV DDADLAITHV IRGEDHLANT AVQIQIFEAV GGAVPVFAHL PLLTDATGQG LSKRLGSLSV ASLREEEGIE PMALASLLAK LGTSDAIEPR LTLDELVAEF DIAKVSRATP KFDPEELLRL NARILHLLPF ERVAGELAAS VWMMPTPAFW EAVPNLSRVA EARDWWAVTH APVARRRTIP LFLAEAATLL PKEPWDLSTW GTWTGAVKAK TGRKGKDLFL PLRRALTGRD HGGQLKNLLP LIGRTRAHKR LAGETA //