ID   SYE_THEPD               Reviewed;         569 AA.
AC   A1RYD7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-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=Tpen_0816;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL78217.1; -; Genomic_DNA.
DR   RefSeq; WP_011752482.1; NC_008698.1.
DR   AlphaFoldDB; A1RYD7; -.
DR   SMR; A1RYD7; -.
DR   STRING; 368408.Tpen_0816; -.
DR   EnsemblBacteria; ABL78217; ABL78217; Tpen_0816.
DR   GeneID; 4601986; -.
DR   KEGG; tpe:Tpen_0816; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   Proteomes; UP000000641; 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..569
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_1000001982"
FT   MOTIF           108..118
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   569 AA;  64322 MW;  BCA13B7C3A20DCB9 CRC64;
     MEVDIRRVAL KHALANAVKF GGKARVDSVV SKVFAEVPEA RKAAKEVVEL VKEVVEEVNS
     MSPESQASLL SELWPEALSG ERKVEVKRLP PLPGAEEVGG KVVTRFAPNP DFVLHLGSAR
     PAILNYYYAK KMYNGKFILR FEDTDPRTKR PMPEAYDLIR EDLRWLGTPW DEEYIQSQRM
     EVYYEVAEAL IKSGNAYVCT HSQDEIKAFR DAGKPDPCSF LPPEEHMERW EKMLSGEYPE
     GAAVLRIKTD PAHPNPSVRD WIAFRVLDTE KTPHPLTGDK YRVWPTYNFA CAVDDHMLGV
     THVLRGEEHA VNTLKQEYVY RHMGWKPPVS IHFGRMNLEG MVLSKSVIRR GIEKGLFSSI
     DDIRLGTLRA LRRRGILPEA IWDLVLEVGI KPSTARVSVD KLHAFNRKYL EPRANRYMFV
     PEPAKVASIE GLEAPITAEV IVHPSFPERG RRRITFSKPE VYLPSDVASS MVRLMGLGNF
     EVVDGGSKLR YLNNDVSFAK KHELPIVQWA PVESSVRGRV LKAAGTKIEE ISGYGEPSLA
     ELPPGEQVQF VRLGFVRVEG PETYIFTHD