ID   SYE_NANEQ               Reviewed;         562 AA.
AC   Q74MU5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=NEQ302;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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; AE017199; AAR39150.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74MU5; -.
DR   SMR; Q74MU5; -.
DR   STRING; 228908.NEQ302; -.
DR   EnsemblBacteria; AAR39150; AAR39150; NEQ302.
DR   KEGG; neq:NEQ302; -.
DR   PATRIC; fig|228908.8.peg.308; -.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OMA; INNFCAQ; -.
DR   Proteomes; UP000000578; 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; Reference proteome.
FT   CHAIN           1..562
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000119723"
FT   MOTIF           90..100
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   562 AA;  66631 MW;  03E496D7DA5E6507 CRC64;
     MYKEIIAYLK LKYGKVKPQS VIGKIIAKNP ELKAKIKELI PIIEQEIKEV EQMDIEQIKE
     LAKAYEQTIE KKEKDIEIPV KDKVITRFAP NPSGLLHIGH ARAIVLNHYI AKKYNGQFIL
     RIEDTDPDVK KPMIEAYELI PKDVEWLIQE KPDKIVVQSD RLDIYYKYIE ELIKQGKAYV
     CLCKAEEFRE YRNKGLPCPH RNQSIEENLE LWSKMLKGEF KKGEAVVRLK TDLTHKDPGV
     RDFPIARIVE NPHPRIGYKP VFPLYNFAVV IDDHLLGITH VIRMKEHTNN AIKQSFIYKA
     FGWEEPIYLE YGALLTDMPT HKSEIRKLIE QKQIEGWDDI RLPTLIALRR RGILPEAIYE
     YIVKDVGLNK ADIKVDWNKI YYYHKIRIDK QTPRYFMIRD PIAIVIENYD DIIDKFEIKN
     GIPYKKISKH PDVDLGYREL PIKEVLYIDK RDAERLKQKP LRLFELFNIK FVGEIEIEYG
     DEYSKTKEKA YAVRVISFDV QEAIKNKYPI VQWLPEYEET TLFELDGYKK AYVEPNIKEN
     YVHFIREGYY KRENDKWIFS VK