GSTU3_ARATH
ID GSTU3_ARATH Reviewed; 225 AA.
AC Q9ZW28;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutathione S-transferase U3;
DE Short=AtGSTU3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 3;
DE AltName: Full=Glutathione S-transferase 21;
GN Name=GSTU3; Synonyms=GST21; OrderedLocusNames=At2g29470; ORFNames=F16P2.15;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR EMBL; AF288185; AAG30134.1; -; mRNA.
DR EMBL; AC004561; AAC95191.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08258.1; -; Genomic_DNA.
DR EMBL; AK117612; BAC42268.1; -; mRNA.
DR PIR; G84696; G84696.
DR RefSeq; NP_180508.1; NM_128501.4.
DR AlphaFoldDB; Q9ZW28; -.
DR SMR; Q9ZW28; -.
DR STRING; 3702.AT2G29470.1; -.
DR PaxDb; Q9ZW28; -.
DR PRIDE; Q9ZW28; -.
DR ProteomicsDB; 247260; -.
DR EnsemblPlants; AT2G29470.1; AT2G29470.1; AT2G29470.
DR GeneID; 817496; -.
DR Gramene; AT2G29470.1; AT2G29470.1; AT2G29470.
DR KEGG; ath:AT2G29470; -.
DR Araport; AT2G29470; -.
DR TAIR; locus:2043007; AT2G29470.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_1_1; -.
DR InParanoid; Q9ZW28; -.
DR OMA; HIEHMMK; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9ZW28; -.
DR BioCyc; ARA:AT2G29470-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9ZW28; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW28; baseline and differential.
DR Genevisible; Q9ZW28; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; PTHR11260; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..225
FT /note="Glutathione S-transferase U3"
FT /id="PRO_0000413550"
FT DOMAIN 6..86
FT /note="GST N-terminal"
FT DOMAIN 91..218
FT /note="GST C-terminal"
FT BINDING 16..17
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 57..58
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 70..71
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
SQ SEQUENCE 225 AA; 25941 MW; 612AD3270285CD03 CRC64;
MAEKEEGVKL IGSWASPFSR RVEMALKLKG VPYDYLDEDY LVVKSPLLLQ LNPVYKKVPV
LVHNGKILPE SQLILEYIDQ TWTNNPILPQ SPYDKAMARF WAKFVDEQVT MIGLRSLVKS
EKRIDVAIEE VQELIMLLEN QITGKKLFGG ETIGFLDMVV GSMIPFCLAR AWEGMGIDMI
PEEKFPELNR WIKNLKEIEI VRECIPDREK HIEHMMKIVG RIKAV
