ID SYE_MARMS Reviewed; 493 AA. AC A6VZB3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Mmwyl1_2880; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Oceanospirillaceae; Marinomonas. OX NCBI_TaxID=400668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., RA Richardson P.; RT "Complete sequence of Marinomonas sp. MWYL1."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000749; ABR71792.1; -; Genomic_DNA. DR AlphaFoldDB; A6VZB3; -. DR SMR; A6VZB3; -. DR STRING; 400668.Mmwyl1_2880; -. DR KEGG; mmw:Mmwyl1_2880; -. DR eggNOG; COG0008; Bacteria. DR eggNOG; COG1384; Bacteria. DR HOGENOM; CLU_015768_6_3_6; -. DR OrthoDB; 9807503at2; -. 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..493 FT /note="Glutamate--tRNA ligase" FT /id="PRO_1000090087" FT MOTIF 10..20 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 251..255 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 493 AA; 56490 MW; 88CD0B0023004FEA CRC64; MSEVRTRIAP SPTGDPHVGT AYIALFNMAF ARKMGGKFIL RIEDTDQTRS TPESEKMILD ALRWLGLDWA EGPDVGGPYG PYRQSERGDI YGQYAQELID KGHAFYAFET TEELDQMRNE QKEQGLPQKY DGRALNLTAE EVQAKLDAGV PYVIRMKIPE EGTCVVQDML RGTIEIDWAQ VDMQVLLKAD GMPTYHLANV VDDHLMKITH VIRGEEWINS APKHILLYQY FGWDMPTLCH MPLLRNPDKS KLSKRKNPTS ILYYQRMGYM SEAVINYLGR MGWSMPDERE KFSLDEMIEH FDIQRVSLGG PVFDVEKLSW LNGMWIRENL TPETFAQKYV EWALNPEYLM KILPLVIPRV ETFSDVADVA GFFLKGMLPI TKEDFSSIKL EEETLRKAMQ FALWRLEALS KWEKDEIFNE MKALAQVMEI KPKDFFAPLF VAISGTTASV SVFDSMAILG SDISRARMRT AVNVLGGPSK KEAKRWEKEY ADL //