ID   GSTT2_ARATH             Reviewed;         591 AA.
AC   Q8L727; Q9FHD9; Q9FHE0; Q9ZRR6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Glutathione S-transferase T2;
DE            Short=AtGSTT2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta member 2;
DE   AltName: Full=Glutathione S-transferase 10B;
GN   Name=GSTT2; Synonyms=GST10B; OrderedLocusNames=At5g41240/At5g41230;
GN   ORFNames=K1O13.3/K1O13.2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-245.
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
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=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: 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: Peroxisome {ECO:0000269|PubMed:19174456}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11099.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g41230 and At5g41240.; Evidence={ECO:0000305};
CC       Sequence=BAB11100.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g41230 and At5g41240.; Evidence={ECO:0000305};
CC       Sequence=CAA10662.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AB019225; BAB11099.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB019225; BAB11100.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94656.1; -; Genomic_DNA.
DR   EMBL; AY139996; AAM98138.1; -; mRNA.
DR   EMBL; BT008361; AAP37720.1; -; mRNA.
DR   EMBL; AJ132398; CAA10662.1; ALT_SEQ; mRNA.
DR   PIR; T52580; T52580.
DR   RefSeq; NP_198940.3; NM_123489.4.
DR   AlphaFoldDB; Q8L727; -.
DR   SMR; Q8L727; -.
DR   STRING; 3702.Q8L727; -.
DR   PaxDb; 3702-AT5G41240-1; -.
DR   ProteomicsDB; 248518; -.
DR   EnsemblPlants; AT5G41240.1; AT5G41240.1; AT5G41240.
DR   GeneID; 834125; -.
DR   Gramene; AT5G41240.1; AT5G41240.1; AT5G41240.
DR   KEGG; ath:AT5G41240; -.
DR   Araport; AT5G41240; -.
DR   TAIR; AT5G41240; GSTT2.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_462617_0_0_1; -.
DR   InParanoid; Q8L727; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; Q8L727; -.
DR   BioCyc; ARA:AT5G41240-MONOMER; -.
DR   PRO; PR:Q8L727; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L727; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR043377; GSTT1/2/3.
DR   InterPro; IPR001005; SANT/Myb.
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; PF13410; GST_C_2; 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   PROSITE; PS50090; MYB_LIKE; 1.
DR   Genevisible; Q8L727; AT.
PE   2: Evidence at transcript level;
KW   Detoxification; Peroxisome; Reference proteome; Transferase.
FT   CHAIN           1..591
FT                   /note="Glutathione S-transferase T2"
FT                   /id="PRO_0000413575"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          89..226
FT                   /note="GST C-terminal"
FT   DOMAIN          265..338
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   REGION          229..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11..12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1
FT                   /note="M -> MM (in Ref. 4; CAA10662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        9
FT                   /note="R -> K (in Ref. 4; CAA10662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="G -> S (in Ref. 4; CAA10662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="I -> M (in Ref. 4; CAA10662)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   591 AA;  67689 MW;  D1F401C7FDA853D9 CRC64;
     MKLKVYADRM SQPSRAVLIF CKVNEIQFDE ILISLGKRQQ LSPEFKEINP MGKVPAIVDG
     RLKLFESHAI LIYLSSAYAS VVDHWYPNDL SKRAKIHSVL DWHHTNLRPG ASGYVLNSVL
     APALGLPLNP KAAAEAENIL TNSLSTLETF WLKGSAKFLL GGKQPSIADL SLVCELMQLQ
     VLDDKDRLRL LSPHKKVEQW IESTRKATMP HSDEVHEVLF RAKDRFQKQR EMATASKPGP
     QSKIIQFSSI GGTSDGPNLV QDTTDRKARR RKWSPPDDVI LISAWLNTSK DRKVVVYDEQ
     QAHTFWKRIG AHVSNSASLA NLPKREWNHC RQRWRKINDY VCKFVGCYDQ ALNQRASGQS
     EDDVFQVAYQ LYYNNYMSNF KLEHAWRELR HNKKWCSTYT SENSKGGGSS KRTKLNGGGV
     YSSSCNPESV PIALDGEEQV MDRPLGVKSS KQKEKKVATK TMLEEREADS RSRLENLWVL
     DEEEQVMDLP LGVKSSKQKE RKVATKTMIE EREAANFRSR LGNLWLLKEK EEREADSRSR
     LENLWALKEK DIEEQKKLTR MEVLKSLLGR RTGETSEKEE TLKNKLIDEM L
//