ID SYE1_METCA Reviewed; 466 AA. AC Q60BG7; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 103. 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}; Synonyms=gltX-1; GN OrderedLocusNames=MCA0510; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J., RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). 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; AE017282; AAU93301.1; -; Genomic_DNA. DR RefSeq; WP_010959858.1; NC_002977.6. DR AlphaFoldDB; Q60BG7; -. DR SMR; Q60BG7; -. DR STRING; 243233.MCA0510; -. DR KEGG; mca:MCA0510; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_015768_6_3_6; -. DR Proteomes; UP000006821; 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:UniProtKB-UniRule. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. 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; 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..466 FT /note="Glutamate--tRNA ligase 1" FT /id="PRO_0000119597" FT MOTIF 10..20 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 247..251 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 466 AA; 52121 MW; ABF0C016F522C4D1 CRC64; MSAIKTRFAP SPTGLIHLGN ARTALFSALG GDVFVLRIED TDLERSRAEF VAELMNDLRW LGLDWQEGPR GAEPDPDWYQ SRRGEIYATY YRLLEEKGLA YPCFCTPLEL EVSRKVQLGS GRPPRYSGRC AHLPADEVRR RHEEGLAATL RFRVPKDRVV EFEDEVRGPQ RFAGEDIGDF IIRRADGSPA FFFCNAIDDA LMGITRVLRG EDHLANTPRQ LMILAALDLP RPRYAHISLI VGDDGAPLSK RNGSRSIKQL REEGYFPEAV VNMLARLGHH YDSAELLGLP ALRAGFDIRR LGRSPARFDV SHLDHWQGLA VRGAADDTLW HWLHTETRAV VPDAHRAGFL DLVRSNCLFP KEADAWARIL FTDELELAAD IAAVAQAAGE AFYLAAIDAA TESPDDFAAF LAGLKRRSGA KGKHLFLPLR AALTGSLDGP ELAKIYQMLD KPRLHRRLAE FTYESE //