ID   SYE_NITMS               Reviewed;         569 AA.
AC   A9A423;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Nmar_0311;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(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; CP000866; ABX12207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A423; -.
DR   SMR; A9A423; -.
DR   STRING; 436308.Nmar_0311; -.
DR   EnsemblBacteria; ABX12207; ABX12207; Nmar_0311.
DR   KEGG; nmr:Nmar_0311; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_2_3_2; -.
DR   OMA; MRFAPNP; -.
DR   PhylomeDB; A9A423; -.
DR   Proteomes; UP000000792; 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_0000367804"
FT   MOTIF           107..117
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   569 AA;  65521 MW;  E323770539C1B725 CRC64;
     MDEEIKHEIR KMALQNAFEH GGQTQDKIIL GKILGTKPEF RTKVKEISGE ISEIVASVNQ
     LSPEEQQKEM EEKFPEALAP KEKIEEREGL PELKDAIQGK VVTRFPPEPN GYPHIGHAKA
     AIINSEYAKM YGGKFILRMD DTNPEAERME YHAAIKVGLE WLGIEFDQVK STSDDMEVFY
     EKGIELINSG KAYVCTCKRE DISQNRRERK ACKCSMEDVG KNNKNWEKMQ NKFKPGEAIV
     RFRGDMKADN AVMRDPVLLR IIDEKHYTVG DKYRIWPSYD FAVAIEDSID GVTHAFRSKE
     FELRKELIDA ILDALGMRKP QQGFFSRLEF KGMPISKRII KPLIEEGKVS WYDDPRLPTL
     EALRRRGIKP EAIRKFIMSL GLTKANTLAP FDALEAFNRK FVDADSMRLF MVKNAKKLKI
     KNLQSTIVEV PNHPINDLGK RKIEITEDFY ISGDDSEAIK EQSTIRLLGL GNVKITKIGN
     ELEGEFERDG DSSNILKIQW VPQKTAHEIK MIIPKILFND EEFNEDSLEE LDVYTEPQYL
     QLKEGEEIQF VRFGYCRKDS QNQAIFTHK