ID   SYE_METTP               Reviewed;         564 AA.
AC   A0B966;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Mthe_1466;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) 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_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}.
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DR   EMBL; CP000477; ABK15240.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B966; -.
DR   SMR; A0B966; -.
DR   STRING; 349307.Mthe_1466; -.
DR   EnsemblBacteria; ABK15240; ABK15240; Mthe_1466.
DR   KEGG; mtp:Mthe_1466; -.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OMA; MRFAPNP; -.
DR   Proteomes; UP000000674; 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   Gene3D; 2.40.240.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
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_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00463; gltX_arch; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..564
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000331010"
FT   MOTIF           107..117
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   564 AA;  64383 MW;  1D3BE679CE0D901F CRC64;
     MTEEIRELIE KFALQNAVKY RSAPNHGAVM GKLMGERPDL RPRAREIAPL ITSVLNEIER
     MSPEQWESRL REMAPELIEE ISARKEPAKG LQPLEGAEGG VVMRFAPNPN GPPTLGSARG
     IIINSEYVKM YGGKFILRFD DTDPVNKRPM IEAYDWYIED CKWLGAEPHE IVAASQRVEK
     YYEVAEELIR RGGAYVCLCE QTAFKALKDA AMPCPHRDQT VDENMALWNK MLDGSFQEGE
     AVLRVKTDIK HKDPAMRDWA GFRIVTKSHP LVGERYRVWP LLDFESAVED HLLGVTHILR
     GKDLIDSERR QRYLYDHMGW VYPRVLHWGR VKIFQFGAFS TSKLRKAIEA GEYSGWDDPR
     LPTVRAMRRR GITAEALRKF MIDLGVGETD ISISMDSIYA ENRRIVDPIA NRRFFVWDPV
     EIEIKGEVPE VAEAPLHPTI DRGTRRIRAG GRLLLCKEDV AGLAPGSRIR LKDLCNIEIK
     EIFPLRAELI DLSPETAKRL KLRIIHWAPV EGIPVRVLGP DKTDTGIGEH GISDELDRIV
     QFERYGFVRI DSVGEEVVAY FAHR