SYE_TOBAC
ID SYE_TOBAC Reviewed; 569 AA.
AC Q43794;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1; 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}.
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DR EMBL; X83524; CAA58506.1; -; mRNA.
DR PIR; S51685; S51685.
DR RefSeq; NP_001312310.1; NM_001325381.1.
DR AlphaFoldDB; Q43794; -.
DR SMR; Q43794; -.
DR STRING; 4097.Q43794; -.
DR GeneID; 107784556; -.
DR KEGG; nta:107784556; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
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; Reference proteome;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..569
FT /note="Glutamate--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000119737"
FT MOTIF 62..72
FT /note="'HIGH' region"
FT MOTIF 303..307
FT /note="'KMSKS' region"
FT BINDING 59..61
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 247..251
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 303..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 569 AA; 63338 MW; F2E81D73460A1844 CRC64;
MATLAAAPWF RVRLIPELKN SQSLLYCRGN HSYRQSLCSR RRSFSVYASA GDGGDVRVRF
APSPTGNLHV GGARTALFNY LYARAKGGKF ILRIEDTDLE RSTKESEEAV LRDLSWLGPA
WDEGPGIGGE YGPYRQSERN ALYKQFAEKL LQSGHVYRCF CSNEELEKMK EIAKLKQLPP
VYTGRWASAT EEEVVEELAK GTPYTYRFRV PKEGSLKIDD LIRGEVSWNL DTLGDFVIMR
SNGQPVYNFC VTVDDATMAI SHVIRAEEHL PNTLRQALIY KALGFPMPHF AHVSLILAPD
RSKLSKRHGA TSVGQFRDMG YLPQAMVNYL ALLGWGDGTE NEFFTLEQLV EKFTIERVNK
SGAIFDSTKL RWMNGQHLRS LPSEELNRII GERWKDAGIA TESQGIFIQD AVLLLKDGID
LITDSEKALS SLLSYPLYET LASAEGKPIL EDGVSEVAKS LLAAYDSGEL SGALAEGQPG
WQKWAKNFGK LLKRKGKSLF MPLRVLLTGK LHGPDIGATT VLLYKAGTSG SVVPQAGFVT
FDERFKILRE VQWESFSTDV PLSAGAVTR
