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   27-MAR-2024, entry version 149.
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}.
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; 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.Q9FEA2; -.
DR   PaxDb; 3702-AT5G64050-1; -.
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; AT5G64050; ERS.
DR   eggNOG; KOG1149; Eukaryota.
DR   HOGENOM; CLU_015768_6_3_1; -.
DR   InParanoid; Q9FEA2; -.
DR   OMA; PHWRFKL; -.
DR   OrthoDB; 5404395at2759; -.
DR   PhylomeDB; Q9FEA2; -.
DR   PRO; PR:Q9FEA2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FEA2; baseline and differential.
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; 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: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; HUPs; 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   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   Genevisible; Q9FEA2; AT.
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
//