GSTUP_ARATH
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 03-AUG-2022, entry version 144.
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.AT1G17180.1; -.
DR iPTMnet; Q9SHH7; -.
DR PaxDb; Q9SHH7; -.
DR PRIDE; Q9SHH7; -.
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; locus:2020312; AT1G17180.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_2_1; -.
DR InParanoid; Q9SHH7; -.
DR OMA; YIEERWP; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9SHH7; -.
DR BioCyc; ARA:AT1G17180-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9SHH7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHH7; baseline and differential.
DR Genevisible; Q9SHH7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 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; PTHR11260; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
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
