ID   SYE_AERPE               Reviewed;         574 AA.
AC   Q9Y9H1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 126.
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};
GN   OrderedLocusNames=APE_2317.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA81329.2; -; Genomic_DNA.
DR   PIR; A72459; A72459.
DR   AlphaFoldDB; Q9Y9H1; -.
DR   SMR; Q9Y9H1; -.
DR   STRING; 272557.APE_2317.1; -.
DR   EnsemblBacteria; BAA81329; BAA81329; APE_2317.1.
DR   KEGG; ape:APE_2317.1; -.
DR   PATRIC; fig|272557.25.peg.1546; -.
DR   eggNOG; arCOG04302; Archaea.
DR   Proteomes; UP000002518; 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   CDD; cd09287; GluRS_non_core; 1.
DR   Gene3D; 2.40.240.100; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..574
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000119712"
FT   MOTIF           109..119
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   574 AA;  66034 MW;  8C86B100C8F01176 CRC64;
     MGSEDLERLL LGYALRDAVK HGGRASVGSV MSMLLGDHPE LRSRAREIAS LAARVVEQVN
     SMPAGEQKRL LSEQYPELAR FEEQREKGDK GLPPLPGAVE GRVKLRFAPN PDFVIHMGNA
     RPAIVNHEYA RMYKGRMVLR FEDTDPRTKT PLREAYDLIR QDLKWLGVSW DEEYIQSLRM
     EVFYSVARRA IERGCAYVDN CGREGKELLS RGEYCPTRDL GPEDNLELFE KMLEGEFYEG
     EAVVRMKTDP RHPNPSLRDW VAMRIIDTEK HPHPLVGSRY LVWPTYNFAV SVDDHMMEIT
     HVLRGKEHQL NTEKQLAVYR CMGWRPPYFI HFGRLKLEGF ILSKSKIRKL LEERPGEFMG
     YDDPRFGTIA GLRRRGVLAE AIRQIILEVG VKPTDATISW ANLAAANRKL LDERADRIMY
     VEDPVEMEVE LAQVECRAAE IPFHPSRPQR KRRITLCTGD KVLLTREDAV EGRQLRLMGL
     SNFTVSQGIL REVDPSLEYA RRMKLPIVQW VKKGGEASVE VLEPVELELR RHQGYAEDAI
     RGYGVDSRLQ FVRYGFVRVD SVEDGVYRVI YTHK
//