ID   GSTU5_ARATH             Reviewed;         224 AA.
AC   P46421;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Glutathione S-transferase U5;
DE            Short=AtGSTU5;
DE            EC=2.5.1.18;
DE   AltName: Full=AtGSTU1;
DE   AltName: Full=GST class-tau member 5;
DE   AltName: Full=Glutathione S-transferase 103-1A;
GN   Name=GSTU5; Synonyms=GSTU1; OrderedLocusNames=At2g29450;
GN   ORFNames=F16P2.17;
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 [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8624414; DOI=10.1007/bf00019016;
RA   van der Kop D.A.M., Schuyer M., Scheres B., van der Zaal B.J.,
RA   Hooykaas P.J.J.;
RT   "Isolation and characterization of an auxin-inducible glutathione S-
RT   transferase gene of Arabidopsis thaliana.";
RL   Plant Mol. Biol. 30:839-844(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Cotyledon, and Hypocotyl;
RA   Watahiki M., Yamamoto K.;
RT   "Auxins and their related substances competitively inhibit enzymatic
RT   activity of an Arabidopsis glutathione S-transferase isozyme expressed in
RT   Escherichia coli.";
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sopory S.K.;
RT   "Nucleotide sequence of glutathione S-transferase cDNA from Arabidopsis
RT   thaliana.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, 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).
CC   -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC).
CC       May be involved in the conjugation of reduced glutathione to a wide
CC       number of exogenous and endogenous hydrophobic electrophiles and have a
CC       detoxification role against certain herbicides.
CC       {ECO:0000269|PubMed:12090627}.
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 auxin.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {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; X89216; CAA61504.1; -; Genomic_DNA.
DR   EMBL; U30489; AAA74019.1; -; Genomic_DNA.
DR   EMBL; D44465; BAA07917.1; -; mRNA.
DR   EMBL; AF144382; AAD34992.1; -; mRNA.
DR   EMBL; AC004561; AAC95193.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08255.1; -; Genomic_DNA.
DR   EMBL; AY062676; AAL32754.1; -; mRNA.
DR   EMBL; BT001228; AAN65115.1; -; mRNA.
DR   EMBL; AY088413; AAM65950.1; -; mRNA.
DR   PIR; S66354; S66354.
DR   RefSeq; NP_180506.1; NM_128499.5.
DR   AlphaFoldDB; P46421; -.
DR   SMR; P46421; -.
DR   STRING; 3702.P46421; -.
DR   PaxDb; 3702-AT2G29450-1; -.
DR   ProteomicsDB; 247334; -.
DR   EnsemblPlants; AT2G29450.1; AT2G29450.1; AT2G29450.
DR   GeneID; 817494; -.
DR   Gramene; AT2G29450.1; AT2G29450.1; AT2G29450.
DR   KEGG; ath:AT2G29450; -.
DR   Araport; AT2G29450; -.
DR   TAIR; AT2G29450; GSTU5.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_1_1; -.
DR   InParanoid; P46421; -.
DR   OMA; NYMAERV; -.
DR   OrthoDB; 986565at2759; -.
DR   PhylomeDB; P46421; -.
DR   BioCyc; ARA:AT2G29450-MONOMER; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:P46421; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P46421; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   CDD; cd03058; GST_N_Tau; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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:SF533; GLUTATHIONE S-TRANSFERASE U5-RELATED; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 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; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; P46421; AT.
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 U5"
FT                   /id="PRO_0000185860"
FT   DOMAIN          5..84
FT                   /note="GST N-terminal"
FT   DOMAIN          89..217
FT                   /note="GST C-terminal"
FT   BINDING         15..16
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         55..56
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..69
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;  26000 MW;  BA2F5C06B94FFCC4 CRC64;
     MAEKEEVKLL GIWASPFSRR VEMALKLKGI PYEYVEEILE NKSPLLLALN PIHKKVPVLV
     HNGKTILESH VILEYIDETW PQNPILPQDP YERSKARFFA KLVDEQIMNV GFISMARADE
     KGREVLAEQV RELIMYLEKE LVGKDYFGGK TVGFLDFVAG SLIPFCLERG WEGIGLEVIT
     EEKFPEFKRW VRNLEKVEIV KDCVPPREEH VEHMNYMAER VRSS
//