SYEM_ARATH
ID SYEM_ARATH Reviewed; 570 AA.
AC Q9FEA2; Q940P6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutamate--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.17 {ECO:0000305};
DE AltName: Full=AtERS {ECO:0000303|PubMed:16107332};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000305};
DE Short=GluRS {ECO:0000305};
DE AltName: Full=Protein OVULE ABORTION 3 {ECO:0000303|PubMed:16297076};
DE Flags: Precursor;
GN Name=OVA3 {ECO:0000303|PubMed:16297076}; OrderedLocusNames=At5g64050;
GN ORFNames=MHJ24.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chang W., Soell D.;
RT "Cloning and expression of Arabidopsis thaliana Glu-tRNA(Glu) synthetase
RT mRNA.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16107332; DOI=10.1074/jbc.m504805200;
RA Kim Y.K., Lee J.Y., Cho H.S., Lee S.S., Ha H.J., Kim S., Choi D., Pai H.S.;
RT "Inactivation of organellar glutamyl- and seryl-tRNA synthetases leads to
RT developmental arrest of chloroplasts and mitochondria in higher plants.";
RL J. Biol. Chem. 280:37098-37106(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17433818; DOI=10.1016/j.jmb.2007.03.015;
RA Pujol C., Marechal-Drouard L., Duchene A.M.;
RT "How can organellar protein N-terminal sequences be dual targeting signals?
RT In silico analysis and mutagenesis approach.";
RL J. Mol. Biol. 369:356-367(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-39.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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).
CC {ECO:0000250|UniProtKB:P46655}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16107332, ECO:0000269|PubMed:16251277,
CC ECO:0000269|PubMed:17433818, ECO:0000269|PubMed:18431481}.
CC Mitochondrion {ECO:0000269|PubMed:16107332,
CC ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818,
CC ECO:0000305|PubMed:25732537}.
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
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; AF241841; AAG29098.1; -; mRNA.
DR EMBL; AB008266; BAB10273.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97834.1; -; Genomic_DNA.
DR EMBL; AY054215; AAL06875.1; -; mRNA.
DR EMBL; AY062560; AAL32638.1; -; mRNA.
DR EMBL; AY114676; AAM47995.1; -; mRNA.
DR RefSeq; NP_201210.1; NM_125801.4.
DR AlphaFoldDB; Q9FEA2; -.
DR SMR; Q9FEA2; -.
DR BioGRID; 21768; 10.
DR IntAct; Q9FEA2; 1.
DR STRING; 3702.AT5G64050.1; -.
DR PaxDb; Q9FEA2; -.
DR PRIDE; Q9FEA2; -.
DR ProteomicsDB; 232979; -.
DR EnsemblPlants; AT5G64050.1; AT5G64050.1; AT5G64050.
DR GeneID; 836526; -.
DR Gramene; AT5G64050.1; AT5G64050.1; AT5G64050.
DR KEGG; ath:AT5G64050; -.
DR Araport; AT5G64050; -.
DR TAIR; locus:2164381; AT5G64050.
DR eggNOG; KOG1149; Eukaryota.
DR HOGENOM; CLU_015768_6_3_1; -.
DR InParanoid; Q9FEA2; -.
DR OMA; PHWRFKL; -.
DR OrthoDB; 879920at2759; -.
DR PhylomeDB; Q9FEA2; -.
DR PRO; PR:Q9FEA2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FEA2; baseline and differential.
DR Genevisible; Q9FEA2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0009658; P:chloroplast organization; TAS:TAIR.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; ISS:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; TAS:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 40..570
FT /note="Glutamate--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000119735"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 301..305
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 57..59
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 245..249
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 301..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 74
FT /note="A -> V (in Ref. 4; AAL06875/AAL32638/AAM47995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 63466 MW; 5EA70E3595F53587 CRC64;
MASLVYGTPW LRVRSLPELA PAFLRRRQSS LFYCSRRSFA VVACSTPVNN GGSVRVRFAP
SPTGNLHVGG ARTALFNYLF ARSKGGKFVL RIEDTDLERS TRESEAAVLQ DLSWLGLDWD
EGPGVSGDFG PYRQSERNAL YKQYAEKLLE SGHVYRCFCS SEELVKMKEN AKLKQLPPVY
TGKWATASDA EIEQELEKGT PFTYRFRVPK EGSLKINDLI RGEVCWNLDT LGDFVVMRSN
GQPVYNFCVT VDDATMAISH VIRAEEHLPN TLRQALIYKA LKFPMPQFAH VSLILAPDRS
KLSKRHGATS VGQYREMGYL PQGMVNYLAL LGWGDGTENE FFTLEDLVEK FSIERVNKSG
AIFDSTKLRW MNGQHLRALP NEKLTKLVGE RWKSAGILTE SEGSFVNEAV ELLKDGIELV
TDSDKVLLNL LSYPLHATLA SPEAKPAVED KLHEVAASLI AAYDSGEIPS ALEEGQGAWQ
KWVKAFGKSL KRKGKSLFMP LRVLLTGKLH GPEMGTSIVL IYKAGSPGIV VPQAGFVSME
ERFKILREID WEALNKDESV PLESTATVST
