SYE_HORVU
ID SYE_HORVU Reviewed; 560 AA.
AC Q43768;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamate--tRNA ligase, chloroplastic/mitochondrial;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Svalofs Bonus; TISSUE=Leaf;
RA Andersen R.V.;
RL Submitted (DEC-1994) 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:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Mitochondrion
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X83523; CAA58505.1; -; mRNA.
DR PIR; S51684; S51684.
DR AlphaFoldDB; Q43768; -.
DR SMR; Q43768; -.
DR EnsemblPlants; HORVU.MOREX.r2.6HG0456870.1.mrna1; HORVU.MOREX.r2.6HG0456870.1.mrna1; HORVU.MOREX.r2.6HG0456870.1.
DR Gramene; HORVU.MOREX.r2.6HG0456870.1.mrna1; HORVU.MOREX.r2.6HG0456870.1.mrna1; HORVU.MOREX.r2.6HG0456870.1.
DR ExpressionAtlas; Q43768; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0048481; P:plant ovule development; IEA:EnsemblPlants.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..560
FT /note="Glutamate--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000119736"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT MOTIF 291..295
FT /note="'KMSKS' region"
FT BINDING 47..49
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 235..239
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 291..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 560 AA; 61862 MW; 2F9F830D3A457B9B CRC64;
MAASNFMGSS ARLRVGLLPS VTPRLSRRAL ATRASADSGG SGPVRVRFAP SPTGNLHVGG
ARTALFNYLF ARSRGGKFVL RVEDTDLERS TKKSEEAVLT DLSWLGLDWD EGPDIGGDFG
PYRQSERNAL YKEHAQKLME SGAVYRCFCS NEELEKMKET ANRMKIPPVY MGKWATASDA
EVQQELEKGT PYTYRFRVPK EGSLKINDLI RGEVSWNLNT LGDFVIMRSN GQPVYNFCVT
VDDATMRISH VIRAEEHLPN TLRQALIYKA LGFAMPLFAH VSLILAPDKS KLSKRHGATS
VGQYKEMGYL PQAMVNYLAL LGWGDGTENE FFTIDDLVEK FTIDRVNKSG AVFDATKLKW
MNGQHLRSLP SDLLIKDFED QWRSTGILLE SESGFAKEAA ELLKEGIDLI TDADAALCKL
LSYPLHETLS SDEAKSVVED KLSEVASGLI SAYDSGELDQ ALAEGHDGWK KWVKSFGKTH
KRKGKSLFMP LRVLLTGKLH GPAMDSTVIL VHKAGTSGAV APQSGFVSLD ERFKILKEVN
WESLQKQQES PVESAVPAAS
