SYE_METHJ
ID SYE_METHJ Reviewed; 561 AA.
AC Q2FTH6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=Mhun_2885;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD42577.1; -; Genomic_DNA.
DR RefSeq; WP_011449830.1; NC_007796.1.
DR AlphaFoldDB; Q2FTH6; -.
DR SMR; Q2FTH6; -.
DR STRING; 323259.Mhun_2885; -.
DR EnsemblBacteria; ABD42577; ABD42577; Mhun_2885.
DR GeneID; 3924180; -.
DR KEGG; mhu:Mhun_2885; -.
DR eggNOG; arCOG04302; Archaea.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OMA; MRFAPNP; -.
DR OrthoDB; 8922at2157; -.
DR Proteomes; UP000001941; 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..561
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000237424"
FT MOTIF 107..117
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ SEQUENCE 561 AA; 62639 MW; 0621797F09CB5DE0 CRC64;
MDDVRSVLLI AALSNAVKHK SVPAAGAVMG AILGTHPELR SKAGEIKGLL GSVLEEVSSL
SAEDREEKLK TIAPDQYASL FEKKEKKKIG LPDLPKAEGG VVMRFAPNPS GPLHLGHARA
AFLNDEYIRR YGGKYILRIE DTDPKRVDPD AYDMVREDIA WMGLSIAETI FQSDRFSKYY
EVGKELIQKG HAYVCRCDNE KFKDLKMHKT ACPCRSQSPE EALDLFDQML DGAFTEGEVG
VRLKTDLSHP DPAMRDYPLF RVLTSTPHQR VDAIVYPLMN LSVAVDDHLL GMTHVIRGKD
HIANTKRQEF IFRYMGWETP VYRHYGRMGI EGVVLSTSQM RAGIQSGEYS GWDDVRLGTL
RAMARRGIQP QAVRNAVVEI GIGETDIQFS WENLYAKNKE IIDSQADRFF FVPDPVLVPV
SGSDPVVAKA MRYPGDESRG YREIPFAGSL YLPKAELESG AAYIRLKDLF NIKVLYEGDI
IRGEYAGDDL QEARSKKAPI IQWLPENHAN PCTLKTPDGD VSGVCEPEAV TTQDRIVQFE
RVGFARIDAA GNPAVAYFTH R