ID SYE_METJA Reviewed; 553 AA.
AC Q58772;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 129.
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=MJ1377;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB99384.1; -; Genomic_DNA.
DR PIR; H64471; H64471.
DR RefSeq; WP_010870894.1; NC_000909.1.
DR AlphaFoldDB; Q58772; -.
DR SMR; Q58772; -.
DR STRING; 243232.MJ_1377; -.
DR PaxDb; 243232-MJ_1377; -.
DR EnsemblBacteria; AAB99384; AAB99384; MJ_1377.
DR GeneID; 1452280; -.
DR KEGG; mja:MJ_1377; -.
DR eggNOG; arCOG04302; Archaea.
DR HOGENOM; CLU_001882_1_3_2; -.
DR InParanoid; Q58772; -.
DR OrthoDB; 10470at2157; -.
DR PhylomeDB; Q58772; -.
DR Proteomes; UP000000805; 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 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; 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_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.
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..553
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119717"
FT MOTIF 98..108
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ SEQUENCE 553 AA; 64577 MW; B19D4177990454A0 CRC64;
MEEKILPIAL RNAIKYNGKA NPKAVLGIFL SENPEYRSKA KEVMPIVEKV VEEVNKLSLD
EIKKKLEELG EDVKKKEKKE KGLELPNVKD KVVMRFAPNP SGPLHIGHAR AAVLNDYFVK
KYGGKLILRL EDTDPKRVLP EAYDMIKEDL DWLGVKVDEV VIQSDRIELY YEYGRKLIEM
GHAYVCDCNP EEFRELRNKG VPCKCRDRAI EDNLELWEKM LNGELENVAV RLKTDIKHKN
PSIRDFPIFR VEKTPHPRTG DKYCVYPLMN FSVPVDDHLL GMTHVLRGKD HIVNTEKQAY
IYKYFGWEMP EFIHYGILKI EDIVLSTSSM YKGIKEGLYS GWDDVRLGTL RALRRRGIKP
EAIYEIMKRI GIKQADVKFS WENLYAINKE LIDKDARRFF FVWNPKKLII EGAEKKVLKL
RMHPDRPEFG ERELIFDGEV YVVGDELEEN KMYRLMELFN IVVEKVDDIA LAKYHSDDFK
IARKNKAKII HWIPVKDSVK VKVLMPDGEI KEGFAEKDFA KVEVDDIIQF ERFGFVRIDK
KDNDGFVCCY AHR
//
