ID SYE_ACTSZ Reviewed; 480 AA. AC A6VLT3; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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}; GN OrderedLocusNames=Asuc_0555; OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / OS 130Z). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes for RT industrial succinate production."; RL BMC Genomics 11:680-680(2010). 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00022}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-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; CP000746; ABR73930.1; -; Genomic_DNA. DR AlphaFoldDB; A6VLT3; -. DR SMR; A6VLT3; -. DR STRING; 339671.Asuc_0555; -. DR KEGG; asu:Asuc_0555; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_0_6; -. DR OrthoDB; 9807503at2; -. DR Proteomes; UP000001114; 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; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. FT CHAIN 1..480 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000330949" FT MOTIF 21..31 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 248..252 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 139 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 251 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 480 AA; 54466 MW; FEDA7B42225A1088 CRC64; MKLEPLFDLD PNVTVRTRFA PSPTGYLHVG GARTALYSWL FAKHHHGEFV LRIEDTDLER STPEATAAII EGMEWLNLAW EHGPYFQTKR FTRYNQVIDQ MIEQGLAYRC YCTKERLEEL RHSQEANKEK PRYDRHCLHD HSHSPDEPHV VRFKNPQEGS VIFDDAVRGR IEISNSELDD LIIRRTDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILNALGA PIPTYAHVSM INGDDGQKLS KRHGAVSVMQ YRDDGYLPEA LVNYLVRLGW GHGDQEIFSR EEMINLFELE HVSKSASAFN TEKLQWLNQH YMRELPADYV ANHLAWQYRD LGIDTANGPA LTDIVSMLAE RSKTLREMAL SSRYFFEEFE TFDETAAKKH LKAAAVQPLE KVKEKLTALS VWDAHSTHEA IEQTAADLDV GMGKVGMPLR VAVTGAGQSP SMDVTLAAIG RERVLARIDK AIAFIKAKAA //