SYEC_ARATH
ID SYEC_ARATH Reviewed; 719 AA.
AC O82462; O65253;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glutamate--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.17 {ECO:0000305};
DE AltName: Full=GluRSAt {ECO:0000303|PubMed:9765600};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000305};
DE Short=GluRS {ECO:0000305};
GN OrderedLocusNames=At5g26710 {ECO:0000312|Araport:AT5G26710};
GN ORFNames=F21E10.12 {ECO:0000312|EMBL:AAC13597.1};
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].
RX PubMed=9765600; DOI=10.1016/s0167-4781(98)00113-4;
RA Day I.S., Golovkin M., Reddy A.S.;
RT "Cloning of the cDNA for glutamyl-tRNA synthetase from Arabidopsis
RT thaliana.";
RL Biochim. Biophys. Acta 1399:219-224(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
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 INTERACTION WITH GLN2; COL4 AND RPP13L4/ZAR1.
RX PubMed=20043823; DOI=10.1186/1471-2105-10-454;
RA Brandao M.M., Dantas L.L., Silva-Filho M.C.;
RT "AtPIN: Arabidopsis thaliana protein interaction network.";
RL BMC Bioinformatics 10:454-454(2009).
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 -!- SUBUNIT: Interacts with GLN2, COL4 AND RPP13L4/ZAR1.
CC {ECO:0000269|PubMed:20043823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF067773; AAC36469.1; -; mRNA.
DR EMBL; AF058914; AAC13597.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93573.1; -; Genomic_DNA.
DR EMBL; AY099592; AAM20443.1; -; mRNA.
DR EMBL; BT000248; AAN15567.1; -; mRNA.
DR EMBL; AK226448; BAE98590.1; -; mRNA.
DR PIR; T01200; T01200.
DR PIR; T52043; T52043.
DR RefSeq; NP_850874.1; NM_180543.3.
DR AlphaFoldDB; O82462; -.
DR SMR; O82462; -.
DR DIP; DIP-48341N; -.
DR IntAct; O82462; 3.
DR STRING; 3702.AT5G26710.1; -.
DR MetOSite; O82462; -.
DR PaxDb; O82462; -.
DR PRIDE; O82462; -.
DR ProteomicsDB; 246385; -.
DR EnsemblPlants; AT5G26710.1; AT5G26710.1; AT5G26710.
DR GeneID; 832718; -.
DR Gramene; AT5G26710.1; AT5G26710.1; AT5G26710.
DR KEGG; ath:AT5G26710; -.
DR Araport; AT5G26710; -.
DR TAIR; locus:2146769; AT5G26710.
DR eggNOG; KOG1147; Eukaryota.
DR HOGENOM; CLU_001882_1_2_1; -.
DR InParanoid; O82462; -.
DR OMA; NLTRWFT; -.
DR OrthoDB; 809861at2759; -.
DR PhylomeDB; O82462; -.
DR BRENDA; 6.1.1.17; 399.
DR PRO; PR:O82462; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82462; baseline and differential.
DR Genevisible; O82462; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IBA:GO_Central.
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: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 Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..719
FT /note="Glutamate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000433543"
FT REGION 176..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 220..230
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 448..452
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT COMPBIAS 191..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 217..219
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 393..397
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 448..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 719 AA; 81065 MW; 0778C243219DA24C CRC64;
MDGMKLSFPP ESPPLSVIVA LSLSASPVTI DSSAAATTVP SFVFSDGRKL NGATVLLRYV
GRSAKKLPDF YGNNAFDSSQ IDEWVDYASV FSSGSEFENA CGRVDKYLES STFLVGHSLS
IADVAIWSAL AGTGQRWESL RKSKKYQSLV RWFNSILDEY SEVLNKVLAT YVKKGSGKPV
AAPKSKDSQQ AVKGDGQDKG KPEVDLPEAE IGKVKLRFAP EPSGYLHIGH AKAALLNKYF
AERYQGEVIV RFDDTNPAKE SNEFVDNLVK DIGTLGIKYE KVTYTSDYFP ELMDMAEKLM
REGKAYVDDT PREQMQKERM DGIDSKCRNH SVEENLKLWK EMIAGSERGL QCCVRGKFNM
QDPNKAMRDP VYYRCNPMSH HRIGDKYKIY PTYDFACPFV DSLEGITHAL RSSEYHDRNA
QYFKVLEDMG LRQVQLYEFS RLNLVFTLLS KRKLLWFVQT GLVDGWDDPR FPTVQGIVRR
GLKIEALIQF ILEQGASKNL NLMEWDKLWS INKRIIDPVC PRHTAVVAER RVLFTLTDGP
DEPFVRMIPK HKKFEGAGEK ATTFTKSIWL EEADASAISV GEEVTLMDWG NAIVKEITKD
EEGRVTALSG VLNLQGSVKT TKLKLTWLPD TNELVNLTLT EFDYLITKKK LEDDDEVADF
VNPNTKKETL ALGDSNMRNL KCGDVIQLER KGYFRCDVPF VKSSKPIVLF SIPDGRAAK
