GSTU1_ARATH
ID GSTU1_ARATH Reviewed; 224 AA.
AC Q9ZW30;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glutathione S-transferase U1;
DE Short=AtGSTU1;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 1;
DE AltName: Full=Glutathione S-transferase 19;
GN Name=GSTU1; Synonyms=GST19; OrderedLocusNames=At2g29490; ORFNames=F16P2.13;
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=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 INDUCTION.
RX PubMed=15923336; DOI=10.1104/pp.104.056168;
RA Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L., Schnoor J.L.;
RT "Gene expression and microscopic analysis of Arabidopsis exposed to
RT chloroacetanilide herbicides and explosive compounds. A phytoremediation
RT approach.";
RL Plant Physiol. 138:858-869(2005).
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 -!- INDUCTION: By acetochlor, metolachlor and 2,4,6-trinitrotoluene (TNT).
CC {ECO:0000269|PubMed:15923336}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR EMBL; AF288183; AAG30132.1; -; mRNA.
DR EMBL; AC004561; AAC95189.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08260.1; -; Genomic_DNA.
DR EMBL; AF428387; AAL16155.1; -; mRNA.
DR EMBL; BT010162; AAQ22631.1; -; mRNA.
DR PIR; A84697; A84697.
DR RefSeq; NP_180510.1; NM_128503.3.
DR AlphaFoldDB; Q9ZW30; -.
DR SMR; Q9ZW30; -.
DR BioGRID; 2848; 6.
DR IntAct; Q9ZW30; 6.
DR STRING; 3702.AT2G29490.1; -.
DR PaxDb; Q9ZW30; -.
DR PRIDE; Q9ZW30; -.
DR ProteomicsDB; 247138; -.
DR EnsemblPlants; AT2G29490.1; AT2G29490.1; AT2G29490.
DR GeneID; 817498; -.
DR Gramene; AT2G29490.1; AT2G29490.1; AT2G29490.
DR KEGG; ath:AT2G29490; -.
DR Araport; AT2G29490; -.
DR TAIR; locus:2042987; AT2G29490.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q9ZW30; -.
DR OMA; RDEYTNC; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9ZW30; -.
DR BioCyc; ARA:AT2G29490-MON; -.
DR PRO; PR:Q9ZW30; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW30; baseline and differential.
DR Genevisible; Q9ZW30; 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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
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; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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;
KW Stress response; Transferase.
FT CHAIN 1..224
FT /note="Glutathione S-transferase U1"
FT /id="PRO_0000413548"
FT DOMAIN 6..85
FT /note="GST N-terminal"
FT DOMAIN 90..217
FT /note="GST C-terminal"
FT BINDING 16..17
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 56..57
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
SQ SEQUENCE 224 AA; 25914 MW; 5BD722371683FED8 CRC64;
MAEKEESVKL LGFWASPFSR RVEMALKLKG VPYEYLEEDL PNKTPLLLEL NPLHKKVPVL
VHNDKILLES HLILEYIDQT WKNSPILPQD PYEKAMARFW AKFIDDQILT LGFRSLVKAE
KGREVAIEET RELLMFLEKE VTGKDFFGGK TIGFLDMIAG SMIPFCLARL WKGIGIDMIP
EEKFPELNRW IKNLEEVEAV RGCIPPREKQ IERMTKIAET IKSA
