ID   SYE_METM5               Reviewed;         555 AA.
AC   A4FXG8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=MmarC5_0583;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) 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; CP000609; ABO34897.1; -; Genomic_DNA.
DR   RefSeq; WP_011868351.1; NC_009135.1.
DR   AlphaFoldDB; A4FXG8; -.
DR   SMR; A4FXG8; -.
DR   STRING; 402880.MmarC5_0583; -.
DR   PRIDE; A4FXG8; -.
DR   EnsemblBacteria; ABO34897; ABO34897; MmarC5_0583.
DR   GeneID; 4929286; -.
DR   KEGG; mmq:MmarC5_0583; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   Proteomes; UP000000253; 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; 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_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.
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..555
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000331005"
FT   MOTIF           100..110
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   555 AA;  63943 MW;  A1645AF4531B1583 CRC64;
     MKDTVMAYLL ENSIKFKGKP NPKAAMGKIL GENPDLRSKV KEVNQVISEV VKEIETMSLE
     EQQAKLDELA PEGLGQKTER KRKEIELKNV KGNVVMRFAP NPSGPLHIGH ARASVLNDFF
     TKKYNGKLVL RLEDTDAKRV LPEAYEMIQE DLKWLGVKVD EVIVQSERLE TYYEYGRKLI
     EMGQAYVCDC DADEFRTLRE QGTLCKCRDT IPEENLKLWE KMLAGELDNV AVRLKTDIAH
     KNPSIRDFPI FRIERTPHPK NGIKYHVYPL MNLSVTVDDH LLGMTHVLRG KDHIVNTEKQ
     EYIYNYFGWE IPEYVHYGIL KIEGPVLSTS KMHAGILSGE YSGWDDARLG TLRALRKRGI
     RPEALYKLMV EIGIKQADVR FAWENLYAAN KDIIDKDARR FFFVESPKKL VISGADSRKI
     DLRMHPDRSE LGNRELLFDG EIYVSDDLEA GKMYRLMELF NIVVEKVEND ILYAKYDSDD
     FAIAKSNKAS IIHWIPVKDS VPVTVIDENA EKIEGFAEKD FAVVKEDDFV QFERFGFVRI
     DEKVDNGYTC YLTHK