ID SYE1_HYPNA Reviewed; 486 AA. AC Q0C1A6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=HNE_1783; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444; RX PubMed=16980487; DOI=10.1128/jb.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., RA Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). 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; CP000158; ABI77242.1; -; Genomic_DNA. DR AlphaFoldDB; Q0C1A6; -. DR SMR; Q0C1A6; -. DR STRING; 228405.HNE_1783; -. DR KEGG; hne:HNE_1783; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_5; -. DR Proteomes; UP000001959; 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: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; Reference proteome. FT CHAIN 1..486 FT /note="Glutamate--tRNA ligase 1" FT /id="PRO_0000367691" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 259..263 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 486 AA; 53324 MW; 29EB8DAC026742F2 CRC64; MSVVTRFAPS PTGMLHIGGA RTALFNYLFA RRNGGRFLLR IEDTDRERST QEATDAILDA MEWLGLTPDE PPVMQSAQVD RHAAVAHDMV ARGTAFRCYV TPEELQARRD LGEEKRQAAK QEGISDAEKE ALLAEASQLL APFRSPYRDG ASPPSPDAPF TVRLRAPESG PRTVEDGVQG TVTIDASEID DLVMLRADGT PTYMLAVVVD DHDMGITHVI RGDDHLRNTF RQVPIYEAMG WSVPNFSHVP MIHGNDGAKL SKRHGALSTT AYRDMGYLPE AMKAYLLRLG WSHGDQEIFT DEEAVQVFDV SGINKAPARL DLDKLATVNA HFMRLAADER LFDLICPVLS KNCSLSDAEV ARIRAALPHM KDRGSTLIEL ANAFAFLYAK RPLELNKNAV KALSDEGKLR LKGLYDDLQR MSQWSGASIS ETIKSYCAAT GLSMGQIGPP LRAALTGGLP APDLAPVMDW LGREETLARI DDQLAG //