ID   GSTT1_ARATH             Reviewed;         245 AA.
AC   Q9ZRT5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Glutathione S-transferase T1;
DE            Short=AtGSTT1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta member 1;
DE   AltName: Full=Glutathione S-transferase 10;
GN   Name=GSTT1; Synonyms=GST10; OrderedLocusNames=At5g41210;
GN   ORFNames=MEE6.28;
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].
RC   STRAIN=cv. Columbia;
RA   Dixon D.P., Cole D.J., Edwards R.;
RT   "Identification and cloning of AtGST 10, members of a novel type of plant
RT   glutathione transferases.";
RL   (er) Plant Gene Register PGR99-053(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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   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).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA   Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA   Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT   peptides, metabolic pathways, and defense mechanisms.";
RL   Plant Cell 19:3170-3193(2007).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19174456; DOI=10.1093/jxb/ern365;
RA   Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT   "Enzyme activities and subcellular localization of members of the
RT   Arabidopsis glutathione transferase superfamily.";
RL   J. Exp. Bot. 60:1207-1218(2009).
CC   -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrobenzyl chloride (pNBC),
CC       and glutathione peroxidase activity toward cumene hydroperoxide and
CC       linoleic acid-13-hydroperoxide. May be involved in the conjugation of
CC       reduced glutathione to a wide number of exogenous and endogenous
CC       hydrophobic electrophiles and have a detoxification role against
CC       certain herbicides. {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: Nucleus {ECO:0000269|PubMed:19174456}. Peroxisome
CC       {ECO:0000269|PubMed:17951448}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; AJ131580; CAA10457.1; -; mRNA.
DR   EMBL; AB010072; BAB09723.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94654.1; -; Genomic_DNA.
DR   EMBL; AY054659; AAK96850.1; -; mRNA.
DR   EMBL; AY072466; AAL66881.1; -; mRNA.
DR   PIR; T51594; T51594.
DR   RefSeq; NP_198937.1; NM_123486.4.
DR   AlphaFoldDB; Q9ZRT5; -.
DR   SMR; Q9ZRT5; -.
DR   BioGRID; 19374; 2.
DR   IntAct; Q9ZRT5; 1.
DR   STRING; 3702.Q9ZRT5; -.
DR   iPTMnet; Q9ZRT5; -.
DR   PaxDb; 3702-AT5G41210-1; -.
DR   ProteomicsDB; 247308; -.
DR   DNASU; 834123; -.
DR   EnsemblPlants; AT5G41210.1; AT5G41210.1; AT5G41210.
DR   GeneID; 834123; -.
DR   Gramene; AT5G41210.1; AT5G41210.1; AT5G41210.
DR   KEGG; ath:AT5G41210; -.
DR   Araport; AT5G41210; -.
DR   TAIR; AT5G41210; GSTT1.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; Q9ZRT5; -.
DR   OMA; LMDGEHF; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; Q9ZRT5; -.
DR   BioCyc; ARA:AT5G41210-MONOMER; -.
DR   PRO; PR:Q9ZRT5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9ZRT5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 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; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR043377; GSTT1/2/3.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44750; GLUTATHIONE S-TRANSFERASE T1-RELATED; 1.
DR   PANTHER; PTHR44750:SF1; GLUTATHIONE S-TRANSFERASE T1-RELATED; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-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; Q9ZRT5; AT.
PE   2: Evidence at transcript level;
KW   Detoxification; Nucleus; Oxidoreductase; Peroxidase; Peroxisome;
KW   Reference proteome; Transferase.
FT   CHAIN           1..245
FT                   /note="Glutathione S-transferase T1"
FT                   /id="PRO_0000413574"
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT   DOMAIN          90..233
FT                   /note="GST C-terminal"
FT   MOTIF           243..245
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         12..13
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         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  27653 MW;  6F16FE1399E793B7 CRC64;
     MMKLKVYADR MSQPSRAVII FCKVNGIQFD EVLISLAKRQ QLSPEFKDIN PLGKVPAIVD
     GRLKLFESHA ILIYLSSAFP SVADHWYPND LSKRAKIHSV LDWHHTNLRR GAAGYVLNSV
     LGPALGLPLN PKAAAEAEQL LTKSLSTLET FWLKGNAKFL LGSNQPSIAD LSLVCELMQL
     QVLDDKDRLR LLSTHKKVEQ WIENTKKATM PHFDETHEIL FKVKEGFQKR REMGTLSKPG
     LQSKI
//