GSTT1_ARATH
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 03-AUG-2022, entry version 143.
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; 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.AT5G41210.1; -.
DR iPTMnet; Q9ZRT5; -.
DR PaxDb; Q9ZRT5; -.
DR PRIDE; Q9ZRT5; -.
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; locus:2163096; AT5G41210.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_2_0_1; -.
DR InParanoid; Q9ZRT5; -.
DR OMA; INDNGYK; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9ZRT5; -.
DR BioCyc; ARA:AT5G41210-MON; -.
DR PRO; PR:Q9ZRT5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZRT5; baseline and differential.
DR Genevisible; Q9ZRT5; AT.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
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 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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44750; PTHR44750; 1.
DR Pfam; PF02798; GST_N; 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 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
