SYE_HALSA
ID SYE_HALSA Reviewed; 586 AA.
AC Q9HQI1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=VNG_1153G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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}.
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DR EMBL; AE004437; AAG19534.1; -; Genomic_DNA.
DR PIR; B84271; B84271.
DR RefSeq; WP_010902829.1; NC_002607.1.
DR AlphaFoldDB; Q9HQI1; -.
DR SMR; Q9HQI1; -.
DR STRING; 64091.VNG_1153G; -.
DR PaxDb; Q9HQI1; -.
DR EnsemblBacteria; AAG19534; AAG19534; VNG_1153G.
DR GeneID; 5952846; -.
DR KEGG; hal:VNG_1153G; -.
DR PATRIC; fig|64091.14.peg.881; -.
DR HOGENOM; CLU_001882_1_3_2; -.
DR InParanoid; Q9HQI1; -.
DR OMA; MRFAPNP; -.
DR OrthoDB; 8922at2157; -.
DR PhylomeDB; Q9HQI1; -.
DR Proteomes; UP000000554; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..586
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119715"
FT REGION 431..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..124
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
FT COMPBIAS 431..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65312 MW; E844ED37F8F46776 CRC64;
MDDELRERVR RAAERAALFN ALKHGSDAQV GAIMGPMMGE HPDFRAHGDE IPGVIAPVIE
DVNGMSDDEQ RARLAELAPE DVEELDSEDE GDDHALPALP NAEAYDEVRM RCAPNPNGPW
HVGHARMPSV IGTYKQRYDG SFVVRFDDTD PETKRPDLDA YDQILEDLSY LGFEADEVLT
ASDRVETYYE HARRLIGMGG AYTCSCPGAE FSDLKNSGEA CPHRDKDPET VADEFEAMVD
GEYNSGEMVL RVKTDITHKN PALRDWVAFR MVDTPHPRDA ASGYRCWPML DFQSGVDDHR
TGVTHIIRGI DLQDSAKRQR FLYEYFGWEY PEVVHWGHVQ LDAYDVAMST STIKERIAAG
ELEGWDDPRA PTMQSIRRRG IRGAAVVDAM VELGTSSSDV ELAMSAVYAN NRDLVDDTAP
RQFLVRDGFE ARGEGPEESH EAVEVPVDDG PDEATPQVHP EHPDRGDREI PVGERVLVEA
TDLPAAGDRV WLKGYGPVRY DGERFAFLDA DIDIVREEGV DVVQWVPAEH NVDVRLRTMD
GDVTGYAEPG FADRDADEIV QFVRVGFARV DAHRDGGASV AYFTHP
