ID A0A1Q1FF23_9EURY Unreviewed; 590 AA.
AC A0A1Q1FF23;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02076};
DE EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_02076};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02076};
DE Short=GluRS {ECO:0000256|HAMAP-Rule:MF_02076};
GN Name=gltX {ECO:0000256|HAMAP-Rule:MF_02076};
GN ORFNames=BV210_01215 {ECO:0000313|EMBL:AQL41415.1};
OS Halorientalis sp. IM1011.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=1932360 {ECO:0000313|EMBL:AQL41415.1, ECO:0000313|Proteomes:UP000187924};
RN [1] {ECO:0000313|EMBL:AQL41415.1, ECO:0000313|Proteomes:UP000187924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM1011 {ECO:0000313|EMBL:AQL41415.1,
RC ECO:0000313|Proteomes:UP000187924};
RA Zhao D., Kumar S., Zhou J., Wang R., Xiang H.;
RT "Isolation and genome sequence of Halorientalis hydrocarbonoclasticus sp.
RT nov., a hydrocarbon-degrading haloarchaeon.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_02076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02076}.
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DR EMBL; CP019067; AQL41415.1; -; Genomic_DNA.
DR RefSeq; WP_077204880.1; NZ_CP019067.1.
DR AlphaFoldDB; A0A1Q1FF23; -.
DR STRING; 1932360.BV210_01215; -.
DR GeneID; 30958272; -.
DR KEGG; hali:BV210_01215; -.
DR OrthoDB; 10470at2157; -.
DR Proteomes; UP000187924; 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; 2.40.240.100; -; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02076};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02076}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02076};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02076};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02076};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02076}; Reference proteome {ECO:0000313|Proteomes:UP000187924}.
FT DOMAIN 107..414
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 420..489
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 508..557
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 432..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..124
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02076"
FT COMPBIAS 564..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 66657 MW; 6572D8FA2E9C0C3E CRC64;
MDDEVRERVE EAAEKNALFN ALKHDSDPQV GAIMGPLMGE NPEFREYGDE IPEVIGPVVG
KIGNMSTEER RERLEELDPD LVAELDAEDE EDEHDLPDLP NAEEYDEIRL RAAPNPNGPW
HLGHARMPSV IGTYKDRYDG SFVVRFDDTD PETKRPDLDA YDEILDAIDY LGFEPDEVIR
ASDRLETYYD HARELIDLGG AYTCSCPQGE FSDMKNSGEA CPHRDKDIET TREEFEAMID
GEYSAGEKVL RVKTDIEHKN PALRDWVAFR MIDTPHPREE ASEYRCWPML DFQSGVDDHL
TGISHIIRGI DLQDSAKRQR FVYDYFDWEY PEVIHWGHVQ VEDYDVSMST STIKEQIEAG
ELDGWDDPRA PTLASLRRRG IRGQAIVDAM VELGTSTSNV DLAMSSVYAN NRDLIDEDTD
RRFLVRDGEE FPIEGGPDAA HPPIHPNHED RGERDIPVGE AVLLEPDDVP AEGERVWLKG
FGPVRRDGDA LEYTDDDIDV VRSGDVDVIH WVPAEGSQPL RLRTMDGDVS GHAEPGITDY
DADAVVQFER IGFARIDGVP EQGTERSSGE DGEPRDKHED DDTVAYYAHS
//
