GEK1_ARATH
ID GEK1_ARATH Reviewed; 317 AA.
AC Q9ZPQ3; Q0WQB9; Q76KI8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000303|PubMed:17251192};
DE EC=3.1.1.96 {ECO:0000269|PubMed:17251192};
DE AltName: Full=Ethanol tolerance protein GEKO1;
GN Name=GEK1; OrderedLocusNames=At2g03800; ORFNames=F19B11.25;
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15215500; DOI=10.1093/pcp/pch086;
RA Fujishige N., Nishimura N., Iuchi S., Kunii T., Shinozaki K., Hirayama T.;
RT "A novel Arabidopsis gene required for ethanol tolerance is conserved among
RT plants and Archaea.";
RL Plant Cell Physiol. 45:659-666(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE.
RX PubMed=15215505; DOI=10.1093/pcp/pch078;
RA Hirayama T., Fujishige N., Kunii T., Nishimura N., Iuchi S., Shinozaki K.;
RT "A novel ethanol-hypersensitive mutant of Arabidopsis.";
RL Plant Cell Physiol. 45:703-711(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17251192; DOI=10.1093/nar/gkl1145;
RA Wydau S., Ferri-Fioni M.-L., Blanquet S., Plateau P.;
RT "GEK1, a gene product of Arabidopsis thaliana involved in ethanol
RT tolerance, is a D-aminoacyl-tRNA deacylase.";
RL Nucleic Acids Res. 35:930-938(2007).
CC -!- FUNCTION: Hydrolyzes D-aminoacyl-tRNA into D-amino acid and free tRNA.
CC Broad specificity toward the amino acid, but strict specificity toward
CC the D-isomer. Seems to be required for ethanol tolerance.
CC {ECO:0000269|PubMed:15215500, ECO:0000269|PubMed:17251192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000269|PubMed:17251192};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000269|PubMed:17251192};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17251192};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:17251192};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for D-tyrosyl-tRNA(Tyr) {ECO:0000269|PubMed:17251192};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15215500}. Cytoplasm
CC {ECO:0000269|PubMed:15215500}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15215500}.
CC -!- INDUCTION: Not induced by abscisic acid, paraquat, 1-aminocyclopropane-
CC 1-carboxylate, ethanol, salt, sorbitol, cold, heat or low oxygen
CC stresses. {ECO:0000269|PubMed:15215500}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to acetaldehyde and
CC hypersensitivity to ethanol. {ECO:0000269|PubMed:15215505}.
CC -!- SIMILARITY: Belongs to the DtdA deacylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20081.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB091252; BAC65101.1; -; mRNA.
DR EMBL; AC006836; AAD20081.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC05749.1; -; Genomic_DNA.
DR EMBL; BT022079; AAY27066.1; -; mRNA.
DR EMBL; AK228782; BAF00680.1; -; mRNA.
DR PIR; D84452; D84452.
DR RefSeq; NP_001325274.1; NM_001335203.1.
DR RefSeq; NP_178474.2; NM_126426.5.
DR AlphaFoldDB; Q9ZPQ3; -.
DR SMR; Q9ZPQ3; -.
DR BioGRID; 307; 1.
DR STRING; 3702.AT2G03800.1; -.
DR PaxDb; Q9ZPQ3; -.
DR PRIDE; Q9ZPQ3; -.
DR ProteomicsDB; 224768; -.
DR EnsemblPlants; AT2G03800.1; AT2G03800.1; AT2G03800.
DR GeneID; 814906; -.
DR Gramene; AT2G03800.1; AT2G03800.1; AT2G03800.
DR KEGG; ath:AT2G03800; -.
DR Araport; AT2G03800; -.
DR TAIR; locus:2044279; AT2G03800.
DR eggNOG; ENOG502QRIE; Eukaryota.
DR HOGENOM; CLU_056464_0_0_1; -.
DR InParanoid; Q9ZPQ3; -.
DR OMA; WQPGPHF; -.
DR OrthoDB; 994056at2759; -.
DR PhylomeDB; Q9ZPQ3; -.
DR BRENDA; 3.1.1.96; 399.
DR PRO; PR:Q9ZPQ3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPQ3; baseline and differential.
DR Genevisible; Q9ZPQ3; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:InterPro.
DR InterPro; IPR018033; Deacylase_DtdA_archaea.
DR InterPro; IPR007508; DtdA.
DR PANTHER; PTHR34667; PTHR34667; 1.
DR Pfam; PF04414; tRNA_deacylase; 1.
DR PIRSF; PIRSF016210; UCP016210; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..317
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000158979"
SQ SEQUENCE 317 AA; 34732 MW; C3E953CDE4015D4D CRC64;
MVTLIVATTA DPASINPAAA LLAMPGWTAG PILPPDIKSF SNKQTRVIQH DRSIVKEDDL
DLRWEEATGE VVDEVIFLSR HTAVSNRPAL TVHPIGVLHL KDGESPPQGG KPGWAALPST
RIGPWFRLLK KMAEAHGLVP EFEITLEATH HGPITNKPTM FLEIGSTEEY WKRQDAAQVM
ALLMWEGLGL GGSEEVGKWK SETGKRKVLL GIGGGHYAPR HMDIALKDDI WVGHLLSGYS
LPMEDPTQTK TTPGENYIGG NWRQSIKAAF EATKASFPGG EILAHLDHKS FKGWQKKAIT
EFLAEESINV GKPNDFT
