ID   GSTU7_ARATH             Reviewed;         227 AA.
AC   Q9ZW24;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Glutathione S-transferase U7;
DE            Short=AtGSTU7;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 7;
DE   AltName: Full=Glutathione S-transferase 25;
GN   Name=GSTU7; Synonyms=GST25; OrderedLocusNames=At2g29420;
GN   ORFNames=F16P2.20;
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   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.
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; AF288188; AAG30137.1; -; mRNA.
DR   EMBL; AC004561; AAC95196.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08252.1; -; Genomic_DNA.
DR   EMBL; AY045679; AAK74037.1; -; mRNA.
DR   EMBL; AY056086; AAL06974.1; -; mRNA.
DR   EMBL; AY086358; AAM64426.1; -; mRNA.
DR   PIR; B84696; B84696.
DR   RefSeq; NP_180503.1; NM_128496.2.
DR   AlphaFoldDB; Q9ZW24; -.
DR   SMR; Q9ZW24; -.
DR   BioGRID; 2841; 4.
DR   IntAct; Q9ZW24; 4.
DR   STRING; 3702.Q9ZW24; -.
DR   iPTMnet; Q9ZW24; -.
DR   PaxDb; 3702-AT2G29420-1; -.
DR   ProteomicsDB; 247336; -.
DR   EnsemblPlants; AT2G29420.1; AT2G29420.1; AT2G29420.
DR   GeneID; 817491; -.
DR   Gramene; AT2G29420.1; AT2G29420.1; AT2G29420.
DR   KEGG; ath:AT2G29420; -.
DR   Araport; AT2G29420; -.
DR   TAIR; AT2G29420; GSTU7.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_1_1; -.
DR   InParanoid; Q9ZW24; -.
DR   OMA; IDDTWQN; -.
DR   OrthoDB; 767442at2759; -.
DR   PhylomeDB; Q9ZW24; -.
DR   BioCyc; ARA:AT2G29420-MONOMER; -.
DR   PRO; PR:Q9ZW24; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZW24; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; TAS:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0009751; P:response to salicylic acid; 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; 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:SF673; GLUTATHIONE S-TRANSFERASE U7; 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; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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; Q9ZW24; AT.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Detoxification; Reference proteome; Transferase.
FT   CHAIN           1..227
FT                   /note="Glutathione S-transferase U7"
FT                   /id="PRO_0000413553"
FT   DOMAIN          8..87
FT                   /note="GST N-terminal"
FT   DOMAIN          92..215
FT                   /note="GST C-terminal"
FT   BINDING         18..19
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  26113 MW;  FE3DC828644E0999 CRC64;
     MAERSNSEEV KLLGMWASPF SRRIEIALTL KGVSYEFLEQ DITNKSSLLL QLNPVHKMIP
     VLVHNGKPIS ESLVILEYID ETWRDNPILP QDPYERTMAR FWSKFVDEQI YVTAMKVVGK
     TGKERDAVVE ATRDLLMFLE KELVGKDFLG GKSLGFVDIV ATLVAFWLMR TEEIVGVKVV
     PVEKFPEIHR WVKNLLGNDV IKKCIPPEDE HLKYIRARME KLNIKSA
//