ID   GSTUJ_ARATH             Reviewed;         219 AA.
AC   Q9ZRW8; Q8LBS1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Glutathione S-transferase U19;
DE            Short=AtGSTU19;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 19;
DE   AltName: Full=Glutathione S-transferase 8;
GN   Name=GSTU19; Synonyms=GST8; OrderedLocusNames=At1g78380;
GN   ORFNames=F3F9.11;
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], AND INDUCTION.
RX   PubMed=12207667; DOI=10.1034/j.1399-3054.2002.1160112.x;
RA   Bianchi M.W., Roux C., Vartanian N.;
RT   "Drought regulation of GST8, encoding the Arabidopsis homologue of
RT   ParC/Nt107 glutathione transferase/peroxidase.";
RL   Physiol. Plantarum 116:96-105(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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.
RN   [6]
RP   FUNCTION, INDUCTION, 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   [7]
RP   INDUCTION.
RX   PubMed=12428014; DOI=10.1104/pp.010066;
RA   DeRidder B.P., Dixon D.P., Beussman D.J., Edwards R., Goldsbrough P.B.;
RT   "Induction of glutathione S-transferases in Arabidopsis by herbicide
RT   safeners.";
RL   Plant Physiol. 130:1497-1505(2002).
RN   [8]
RP   INDUCTION.
RX   PubMed=15069083; DOI=10.1074/jbc.m402807200;
RA   Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E.,
RA   Goldsbrough P.B.;
RT   "Proteomic analysis of Arabidopsis glutathione S-transferases from
RT   benoxacor- and copper-treated seedlings.";
RL   J. Biol. Chem. 279:26098-26104(2004).
RN   [9]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16361527; DOI=10.1104/pp.105.067199;
RA   DeRidder B.P., Goldsbrough P.B.;
RT   "Organ-specific expression of glutathione S-transferases and the efficacy
RT   of herbicide safeners in Arabidopsis.";
RL   Plant Physiol. 140:167-175(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=19520850; DOI=10.1074/jbc.m109.020107;
RA   Dixon D.P., Edwards R.;
RT   "Selective binding of glutathione conjugates of fatty acid derivatives by
RT   plant glutathione transferases.";
RL   J. Biol. Chem. 284:21249-21256(2009).
RN   [11]
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).
RN   [12]
RP   INDUCTION.
RX   PubMed=20031254; DOI=10.1016/j.jplph.2009.11.006;
RA   Hara M., Yatsuzuka Y., Tabata K., Kuboi T.;
RT   "Exogenously applied isothiocyanates enhance glutathione S-transferase
RT   expression in Arabidopsis but act as herbicides at higher concentrations.";
RL   J. Plant Physiol. 167:643-649(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22092075; DOI=10.1021/pr200917t;
RA   Aryal U.K., Krochko J.E., Ross A.R.;
RT   "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT   polyethylene glycol fractionation, immobilized metal-ion affinity
RT   chromatography, two-dimensional gel electrophoresis and mass
RT   spectrometry.";
RL   J. Proteome Res. 11:425-437(2012).
CC   -!- FUNCTION: Catalyzes the glutathionylation of 12-oxophytodienoate
CC       (OPDA). In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC),
CC       and glutathione peroxidase activity toward cumene hydroperoxide.
CC       {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16361527,
CC       ECO:0000269|PubMed:19520850}.
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:0000269|PubMed:19174456}.
CC   -!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
CC       jasmonate, auxin, H(2)O(2), copper, benoxacor, isothiocyanates and the
CC       pathogen Hyaloperonospora parasitica. {ECO:0000269|PubMed:12090627,
CC       ECO:0000269|PubMed:12207667, ECO:0000269|PubMed:12428014,
CC       ECO:0000269|PubMed:15069083, ECO:0000269|PubMed:16361527,
CC       ECO:0000269|PubMed:20031254}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR   EMBL; AJ012571; CAA10060.1; -; mRNA.
DR   EMBL; AC013430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE36099.1; -; Genomic_DNA.
DR   EMBL; AF385691; AAK60284.1; -; mRNA.
DR   EMBL; AY078012; AAL77713.1; -; mRNA.
DR   EMBL; AY087032; AAM64593.1; -; mRNA.
DR   PIR; T51607; T51607.
DR   RefSeq; NP_565178.1; NM_106485.4.
DR   AlphaFoldDB; Q9ZRW8; -.
DR   SMR; Q9ZRW8; -.
DR   BioGRID; 29393; 26.
DR   IntAct; Q9ZRW8; 23.
DR   STRING; 3702.Q9ZRW8; -.
DR   iPTMnet; Q9ZRW8; -.
DR   SwissPalm; Q9ZRW8; -.
DR   PaxDb; 3702-AT1G78380-1; -.
DR   ProteomicsDB; 247232; -.
DR   EnsemblPlants; AT1G78380.1; AT1G78380.1; AT1G78380.
DR   GeneID; 844174; -.
DR   Gramene; AT1G78380.1; AT1G78380.1; AT1G78380.
DR   KEGG; ath:AT1G78380; -.
DR   Araport; AT1G78380; -.
DR   TAIR; AT1G78380; GSTU19.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_2_1; -.
DR   InParanoid; Q9ZRW8; -.
DR   OMA; TWTTKGE; -.
DR   OrthoDB; 767442at2759; -.
DR   PhylomeDB; Q9ZRW8; -.
DR   BioCyc; ARA:AT1G78380-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G78380-MONOMER; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:Q9ZRW8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZRW8; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:TAIR.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
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; 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:SF787; GLUTATHIONE S-TRANSFERASE U19; 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; Q9ZRW8; AT.
PE   1: Evidence at protein level;
KW   Cytoplasm; Detoxification; Oxidoreductase; Peroxidase; Phosphoprotein;
KW   Reference proteome; Stress response; Transferase.
FT   CHAIN           1..219
FT                   /note="Glutathione S-transferase U19"
FT                   /id="PRO_0000413565"
FT   DOMAIN          3..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..208
FT                   /note="GST C-terminal"
FT   BINDING         13..14
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..40
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   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   CONFLICT        16
FT                   /note="G -> R (in Ref. 5; AAM64593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   219 AA;  25651 MW;  E79AABD8C14C6F15 CRC64;
     MANEVILLDF WPSMFGMRTR IALREKGVEF EYREEDLRNK SPLLLQMNPI HKKIPVLIHN
     GKPVNESIIQ VQYIDEVWSH KNPILPSDPY LRAQARFWAD FIDKKLYDAQ RKVWATKGEE
     QEAGKKDFIE ILKTLESELG DKPYFSGDDF GYVDIALIGF YTWFPAYEKF ANFSIESEVP
     KLIAWVKKCL QRESVAKSLP DPEKVTEFVS ELRKKFVPE
//