ID SYE_XANOR Reviewed; 467 AA. AC Q5H2R3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 103. 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=XOO1504; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., RA Go S.-J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the RT bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). 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; AE013598; AAW74758.1; -; Genomic_DNA. DR PDB; 5H4V; X-ray; 3.00 A; A/B/C/D/E/F=1-467. DR PDBsum; 5H4V; -. DR AlphaFoldDB; Q5H2R3; -. DR SMR; Q5H2R3; -. DR STRING; 291331.XOO1504; -. DR KEGG; xoo:XOO1504; -. DR HOGENOM; CLU_015768_6_3_6; -. DR Proteomes; UP000006735; 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 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..467 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119705" FT MOTIF 9..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 237..241 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 240 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 17..32 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 46..49 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 51..64 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 79..91 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 102..113 FT /evidence="ECO:0007829|PDB:5H4V" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 146..154 FT /evidence="ECO:0007829|PDB:5H4V" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 181..191 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:5H4V" FT TURN 201..206 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 207..217 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 257..265 FT /evidence="ECO:0007829|PDB:5H4V" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 279..285 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 300..313 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 316..329 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 340..347 FT /evidence="ECO:0007829|PDB:5H4V" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 354..365 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 385..395 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 405..416 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 421..433 FT /evidence="ECO:0007829|PDB:5H4V" FT STRAND 434..436 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 441..447 FT /evidence="ECO:0007829|PDB:5H4V" FT HELIX 449..464 FT /evidence="ECO:0007829|PDB:5H4V" SQ SEQUENCE 467 AA; 51649 MW; 083DB8ACD9431ADF CRC64; MACRTRFAPS PTGYLHIGGA RTALYCWLEA RRRGGQFVLR IEDTDRQRST QAAIDAILEA MQWLGLGYDE GPIYQTQRVA RYQEVAEQLL AQGKAYYAYE TREELDAMRE AAMAKQEKPR YDGAAREQNL PYRDDPNRVI RFKNPIGGTV VFDDLIKGRI EIANSELDDM VIFRPDGLPT YNFAVVVDDW DMGITEVIRG DDHINNTPRQ INIYAALGAP VPKFAHMPMI LDEQGTKLSK RTGAADVMQY KDAGYLPHAL INYLARLGWS HGDQELFTPQ ELLDLFDVKD VNSKAARLDM AKLGWVNQHY LKTDDPASIA PQLEYQLAKL GVDLAAGPAA ADVVVALRER VHTLKEMAEK AVVWYQPLET YDAAAVMKHL KLGAEVPLGK ARELLAAVDQ WSVDSVSAAL HDAAAALELG MGKVAQPLRV AITGTQVSPD ISQTVYLAGR EGALKRIDAA LTKIGAA //