ID SYE_METTH Reviewed; 553 AA. AC O26157; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02076}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_02076}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02076}; DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_02076}; GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_02076}; OrderedLocusNames=MTH_51; OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H; RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997; RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., RA Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: RT functional analysis and comparative genomics."; RL J. Bacteriol. 179:7135-7155(1997). 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_02076}. 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_02076}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02076}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_02076}. 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; AE000666; AAB84558.1; -; Genomic_DNA. DR PIR; B69167; B69167. DR RefSeq; WP_010875691.1; NC_000916.1. DR PDB; 3AII; X-ray; 1.65 A; A=1-553. DR PDBsum; 3AII; -. DR AlphaFoldDB; O26157; -. DR SMR; O26157; -. DR STRING; 187420.MTH_51; -. DR PaxDb; 187420-MTH_51; -. DR EnsemblBacteria; AAB84558; AAB84558; MTH_51. DR GeneID; 1470013; -. DR KEGG; mth:MTH_51; -. DR PATRIC; fig|187420.15.peg.49; -. DR HOGENOM; CLU_001882_1_3_2; -. DR InParanoid; O26157; -. DR BRENDA; 6.1.1.17; 7219. DR Proteomes; UP000005223; 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd09287; GluRS_non_core; 1. DR Gene3D; 2.40.240.100; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N. DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR049437; tRNA-synt_1c_C2. DR NCBIfam; TIGR00463; gltX_arch; 1. DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1. DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF20974; tRNA-synt_1c_C2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 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..553 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119721" FT MOTIF 103..113 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 111..126 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 147..158 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 168..171 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 195..203 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:3AII" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 274..284 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 299..310 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 333..341 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 365..375 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 386..397 FT /evidence="ECO:0007829|PDB:3AII" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 402..404 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 406..416 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 422..428 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 433..435 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 437..449 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 455..460 FT /evidence="ECO:0007829|PDB:3AII" FT TURN 461..463 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 464..469 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 472..477 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 480..486 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 500..505 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 511..516 FT /evidence="ECO:0007829|PDB:3AII" FT HELIX 518..522 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 528..531 FT /evidence="ECO:0007829|PDB:3AII" FT TURN 532..534 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 535..541 FT /evidence="ECO:0007829|PDB:3AII" FT STRAND 543..552 FT /evidence="ECO:0007829|PDB:3AII" SQ SEQUENCE 553 AA; 63090 MW; C6DB8AE92C2FEE6B CRC64; MVPVEDLVYR YALLNAVKHR GRANPGAVMG AVMSNEPELR KMAPQVKEAV EAAVERVNSL SPEEQQQEME RLGLEITERK QKKRKGLREL AGVKGEVVLR FAPNPSGPLH IGHARAAILN HEYARKYDGR LILRIEDTDP RRVDPEAYDM IPADLEWLGV EWDETVIQSD RMETYYEYTE KLIERGGAYV CTCRPEEFRE LKNRGEACHC RSLGFRENLQ RWREMFEMKE GSAVVRVKTD LNHPNPAIRD WVSMRIVEAE HPRTGTRYRV YPMMNFSVAV DDHLLGVTHV LRGKDHLANR EKQEYLYRHL GWEPPEFIHY GRLKMDDVAL STSGAREGIL RGEYSGWDDP RLGTLRAIAR RGIRPEAIRK LMVEIGVKIA DSTMSWKKIY GLNRSILEEE ARRYFFAADP VKLEVVGLPG PVRVERPLHP DHPEIGNRVL ELRGEVYLPG DDLGEGPLRL IDAVNVIYSG GELRYHSEGI EEARELGASM IHWVPAESAL EAEVIMPDAS RVRGVIEADA SELEVDDVVQ LERFGFARLD SAGPGMVFYY AHK //