ID   SYE_KORCO               Reviewed;         569 AA.
AC   B1L5U2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Kcr_1075;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000968; ACB07821.1; -; Genomic_DNA.
DR   RefSeq; WP_012309718.1; NC_010482.1.
DR   AlphaFoldDB; B1L5U2; -.
DR   SMR; B1L5U2; -.
DR   STRING; 374847.Kcr_1075; -.
DR   PRIDE; B1L5U2; -.
DR   EnsemblBacteria; ACB07821; ACB07821; Kcr_1075.
DR   GeneID; 6094352; -.
DR   KEGG; kcr:Kcr_1075; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_2_3_2; -.
DR   InParanoid; B1L5U2; -.
DR   OMA; MRFAPNP; -.
DR   OrthoDB; 8922at2157; -.
DR   PhylomeDB; B1L5U2; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043604; P:amide biosynthetic process; IBA:GO_Central.
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..569
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367802"
FT   MOTIF           99..109
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   569 AA;  65142 MW;  AD8CCE18820588F2 CRC64;
     MEDVKELIVR LAAENALKYG KADTKAVIGK ILYMRPDLKQ NVRELIPLVE EAVRAVNEMP
     KEALEGIVGE VKKEKKEEVR KWPDLPKAER GKVVTRVAPE PNGYPTLGHA KGLLVPFIYA
     RLYDGKFLLR FEDTNPRVER LEYYEAIRNE FSRLLEACEE ELGLSPGRWD EEIIESYHLE
     EMYSLAKKLI EAGKAYVCTC PAAEVRKRRK LGISCDHRDQ PIEKNLELWE KMLNGGFREG
     EAHLRLKTDM SHPNVTMRDP GIFRVIEAEH PIHGDKYRVY PVYDFSVSVM DSLTGVTHAF
     RSKEFEPHVD VQRHIVRALG LREYEMIQFG RITVEGIPLS KRYIRPLVES GILEGWDDPR
     IPTLRGLFRR GINPRAIVRF FYELGPSKVD ATVNMEAIAS INRKILDPIA ERYMFVPNPI
     KAKIEGLTPP VIAQVEVHPD SKRKREIRLD ESEVFIASSD LEGLKPGDEL RLRGLVNVTI
     RSVNPDEVSL RVSEEQRVKG VKIIQWAPVR NGVPARLFVP ESPYSFRMLG GYGEPALRGI
     KEGEIVQFVR VGFARLDRRD PLTFILSHD