ID   GSTUP_ARATH             Reviewed;         221 AA.
AC   Q9SHH7;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Glutathione S-transferase U25;
DE            Short=AtGSTU25;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 25;
GN   Name=GSTU25; OrderedLocusNames=At1g17180; ORFNames=F20D23.12A;
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=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   [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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   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   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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; AC007651; AAD50015.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29555.1; -; Genomic_DNA.
DR   EMBL; AK118907; BAC43490.1; -; mRNA.
DR   EMBL; BT005643; AAO64063.1; -; mRNA.
DR   PIR; H86307; H86307.
DR   RefSeq; NP_173161.1; NM_101579.4.
DR   PDB; 5G5A; X-ray; 1.95 A; A/B/C/D=1-221.
DR   PDBsum; 5G5A; -.
DR   AlphaFoldDB; Q9SHH7; -.
DR   SMR; Q9SHH7; -.
DR   BioGRID; 23529; 3.
DR   IntAct; Q9SHH7; 2.
DR   STRING; 3702.Q9SHH7; -.
DR   iPTMnet; Q9SHH7; -.
DR   PaxDb; 3702-AT1G17180-1; -.
DR   ProteomicsDB; 247143; -.
DR   EnsemblPlants; AT1G17180.1; AT1G17180.1; AT1G17180.
DR   GeneID; 838289; -.
DR   Gramene; AT1G17180.1; AT1G17180.1; AT1G17180.
DR   KEGG; ath:AT1G17180; -.
DR   Araport; AT1G17180; -.
DR   TAIR; AT1G17180; GSTU25.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_2_1; -.
DR   InParanoid; Q9SHH7; -.
DR   OMA; WVNACLE; -.
DR   OrthoDB; 2077634at2759; -.
DR   PhylomeDB; Q9SHH7; -.
DR   BioCyc; ARA:AT1G17180-MONOMER; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:Q9SHH7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHH7; 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; IDA:TAIR.
DR   GO; GO:0046256; P:2,4,6-trinitrotoluene catabolic process; IDA:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF593; GLUTATHIONE S-TRANSFERASE U25; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF13410; GST_C_2; 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; Q9SHH7; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Detoxification; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..221
FT                   /note="Glutathione S-transferase U25"
FT                   /id="PRO_0000413570"
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         149
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZW27"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           89..115
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           118..139
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           164..171
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:5G5A"
FT   HELIX           202..215
FT                   /evidence="ECO:0007829|PDB:5G5A"
SQ   SEQUENCE   221 AA;  25591 MW;  BCEB3254B39364A8 CRC64;
     MADEVILLDF WPSMFGMRTR IALEEKNVKF DYREQDLWNK SPILLEMNPV HKKIPVLIHN
     GNPVCESLIQ IEYIDEVWPS KTPLLPSDPY QRAQAKFWGD FIDKKVYASA RLIWGAKGEE
     HEAGKKEFIE ILKTLESELG DKTYFGGETF GYVDIALIGF YSWFEAYEKF GSFSIEAECP
     KLIAWGKRCV ERESVAKSLP DSEKIIKFVP ELRKKLGIEI E
//