SYE_THEAC
ID SYE_THEAC Reviewed; 548 AA.
AC Q9HJM5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 25-MAY-2022, entry version 108.
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=Ta0942;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAC12071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445066; CAC12071.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9HJM5; -.
DR SMR; Q9HJM5; -.
DR STRING; 273075.Ta0942; -.
DR EnsemblBacteria; CAC12071; CAC12071; CAC12071.
DR KEGG; tac:Ta0942; -.
DR eggNOG; arCOG04302; Archaea.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OMA; MRFAPNP; -.
DR OrthoDB; 8922at2157; -.
DR Proteomes; UP000001024; 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..548
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119733"
FT MOTIF 102..112
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ SEQUENCE 548 AA; 63450 MW; 1736628A27C73D60 CRC64;
MYEDDIRRIA LINAYQHEGK ADLKSVMGKV MAEIPDLRRD PRSAREMVSR IVDEVNSMSA
YEIRETVETR YTSSIRKEKK VEEHRLPDLE GVNGPVVMRM APSPSGPLHI GHTRMAILND
EYVKRYGGEL ILRIEDTNPK NIDPDAYHMI PEDLEWLGVN VTKIVIQSDR FDLYYAEAKK
LMENGHMYVC TCPREEFKKR KLESIPCKDR DNPPETNLEL FDKMIDGTIK EGDAVAVVKT
DLKHPNPSVR DWIAFRIIEA RHPRVDDKYR VYPMMSFSVA VDDHYLGLTH VLRGKDQLTN
TDKQRYIFDY NGWKKPYYYH YGMIKFPGIK LKTSLMKKGI LSGQYEGWSD IRLGTVRAFA
KRGYRPETFR RYWINSGLRE IDAIFSIEIF DSINREIVDP RAYRFSFVKD PVPVRIEGMP
NISAKLPLHP THPEYGFREY EVKGSVYIAS RDFAAISEGE RIRLKDLCYI RKKGNGIIYD
GVEMTEKTKI INWCPEGSRD FSVLKPDGSK DSGLIEPKSS GYRGIAQLER YGYVNFADGD
DLAYFTHP