ID   SYE_METTM               Reviewed;         552 AA.
AC   Q50543; D9PV87;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 119.
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};
GN   OrderedLocusNames=MTBMA_c05400;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8597593; DOI=10.1016/0167-4781(95)00234-0;
RA   Moore J.A., Chen A., Yan M., Hurlburt A.P., Poulter C.D.;
RT   "Identification of the gltX gene encoding glutamyl-tRNA synthetase from
RT   Methanobacterium thermoautotrophicum.";
RL   Biochim. Biophys. Acta 1305:113-116(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
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; U37405; AAC43972.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL58135.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50543; -.
DR   SMR; Q50543; -.
DR   STRING; 79929.MTBMA_c05400; -.
DR   PaxDb; 79929-MTBMA_c05400; -.
DR   KEGG; mmg:MTBMA_c05400; -.
DR   PATRIC; fig|79929.8.peg.524; -.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   Proteomes; UP000000345; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..552
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000119722"
FT   MOTIF           102..112
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   552 AA;  63238 MW;  882B6B97D2EF6576 CRC64;
     MMVEDLVYRY ALMNAVKHKG KANPGAVMGA VMSNEPELRK RAPEVKEAVQ AAVEKVNSLK
     PEEQQSEMER LGLEIRERKQ KKRQGLRNLP DVKGEVVLRF APNPSGPLHI GHARAAILNH
     EYARRYDGKL ILRIEDTDPR RVDPEAYDMI PSDLEWLGVE WDETIIQSDR MEIYYEYTER
     LIERGGAYVC TCTPEAFREF KNEGKACHCR DLGVRENLQR WREMFEMPEG SAVVRVKTDL
     QHPNPAIRDW VSMRIVEAEH PRTGTRYRVY PMMNFSVAVD DHLLGVTHVL RGKDHLANSE
     KQEYLYRHLG WEPPVFIHYG RLKMDDIALS TSGAREGIVE GKYSGWDDPR LGTIRAIARR
     GIRSDAIRKL MVEIGVKIAD STMSWKKIYG LNRNILEEEA RRYFFAADPV RFEIEGLPGP
     IRVERSLHPD KPELGNRILE LNGDVYLPRG DLREGPLRLI DAVNVIYSDG ELRYHSEGIE
     EARELQAAMI HWVPAESALK AVVVMPDASE IEGVIEGDAS ELEVDDVVQL ERFGFARVDS
     SGERLVFYYA HK
//