ID   GSTZ1_ARATH             Reviewed;         221 AA.
AC   Q9ZVQ3; Q0WWK7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=Glutathione S-transferase Z1;
DE            Short=AtGSTZ1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-zeta member 1;
DE   AltName: Full=Glutathione S-transferase 18;
DE   AltName: Full=Maleylacetone isomerase;
DE            Short=MAI;
DE            EC=5.2.1.-;
GN   Name=GSTZ1; Synonyms=GST18, GSTZ; OrderedLocusNames=At2g02390;
GN   ORFNames=T16F16.18;
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], FUNCTION, INDUCTION, GENE FAMILY, AND
RP   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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=11368331; DOI=10.1006/abbi.2000.2125;
RA   Dixon D.P., Cole D.J., Edwards R.;
RT   "Characterisation of a zeta class glutathione transferase from Arabidopsis
RT   thaliana with a putative role in tyrosine catabolism.";
RL   Arch. Biochem. Biophys. 384:407-412(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Chen D., Kawarasaki Y., Nakano H., Yamane T.;
RT   "Arabidopsis thaliana ecotype Columbia for glutathione S-transferase zeta
RT   (AtGSTZ) mRNA.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   PubMed=11352584; DOI=10.1006/jmbi.2001.4638;
RA   Thom R., Dixon D.P., Edwards R., Cole D.J., Lapthorn A.J.;
RT   "The structure of a zeta class glutathione S-transferase from Arabidopsis
RT   thaliana: characterisation of a GST with novel active-site architecture and
RT   a putative role in tyrosine catabolism.";
RL   J. Mol. Biol. 308:949-962(2001).
CC   -!- FUNCTION: Acts a maleylacetone isomerase. Also catalyzes the
CC       glutathione-dependent dehalogenation of dichloroacetic acid to
CC       glyoxylic acid. In vitro, possesses glutathione peroxidase activity
CC       toward cumene hydroperoxide and linoleic acid-13-hydroperoxide.
CC       {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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ZVQ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ZVQ3-2; Sequence=VSP_041936;
CC   -!- INDUCTION: By salicylic acid, methyl jasmonate, auxin, H(2)O(2), and
CC       the pathogen Hyaloperonospora parasitica.
CC       {ECO:0000269|PubMed:12090627}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR   EMBL; AF288182; AAG30131.1; -; mRNA.
DR   EMBL; AJ278293; CAC19475.1; -; mRNA.
DR   EMBL; AY208155; AAO60039.1; -; mRNA.
DR   EMBL; AC005312; AAC78521.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05573.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05575.1; -; Genomic_DNA.
DR   EMBL; AY052332; AAK96525.1; -; mRNA.
DR   EMBL; AY061901; AAL31228.1; -; mRNA.
DR   EMBL; AK226342; BAE98491.1; -; mRNA.
DR   PIR; B84436; B84436.
DR   RefSeq; NP_178344.1; NM_126296.5. [Q9ZVQ3-1]
DR   RefSeq; NP_973400.1; NM_201671.3. [Q9ZVQ3-2]
DR   PDB; 1E6B; X-ray; 1.65 A; A=1-221.
DR   PDBsum; 1E6B; -.
DR   AlphaFoldDB; Q9ZVQ3; -.
DR   SMR; Q9ZVQ3; -.
DR   STRING; 3702.Q9ZVQ3; -.
DR   PaxDb; 3702-AT2G02390-3; -.
DR   ProteomicsDB; 247331; -. [Q9ZVQ3-1]
DR   EnsemblPlants; AT2G02390.1; AT2G02390.1; AT2G02390. [Q9ZVQ3-1]
DR   EnsemblPlants; AT2G02390.3; AT2G02390.3; AT2G02390. [Q9ZVQ3-2]
DR   GeneID; 814770; -.
DR   Gramene; AT2G02390.1; AT2G02390.1; AT2G02390. [Q9ZVQ3-1]
DR   Gramene; AT2G02390.3; AT2G02390.3; AT2G02390. [Q9ZVQ3-2]
DR   KEGG; ath:AT2G02390; -.
DR   Araport; AT2G02390; -.
DR   TAIR; AT2G02390; GSTZ1.
DR   eggNOG; KOG0868; Eukaryota.
DR   HOGENOM; CLU_011226_20_1_1; -.
DR   InParanoid; Q9ZVQ3; -.
DR   OMA; VYNAHRF; -.
DR   OrthoDB; 986565at2759; -.
DR   PhylomeDB; Q9ZVQ3; -.
DR   BioCyc; ARA:AT2G02390-MONOMER; -.
DR   BRENDA; 5.2.1.2; 399.
DR   EvolutionaryTrace; Q9ZVQ3; -.
DR   PRO; PR:Q9ZVQ3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZVQ3; 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; IEA:UniProtKB-EC.
DR   GO; GO:0016034; F:maleylacetoacetate isomerase activity; IDA:TAIR.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:1902000; P:homogentisate catabolic process; IDA:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03191; GST_C_Zeta; 1.
DR   CDD; cd03042; GST_N_Zeta; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR034333; GST_Zeta_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01262; maiA; 1.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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; Q9ZVQ3; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Detoxification; Isomerase;
KW   Oxidoreductase; Peroxidase; Reference proteome; Stress response;
KW   Transferase.
FT   CHAIN           1..221
FT                   /note="Glutathione S-transferase Z1"
FT                   /id="PRO_0000186029"
FT   DOMAIN          7..88
FT                   /note="GST N-terminal"
FT   DOMAIN          93..218
FT                   /note="GST C-terminal"
FT   BINDING         17..22
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         17..18
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         46..47
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..118
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         49
FT                   /note="S -> SVYRFDLQ (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.7"
FT                   /id="VSP_041936"
FT   STRAND          10..13
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   TURN            41..44
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           49..54
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           94..109
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           166..182
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           190..199
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           203..208
FT                   /evidence="ECO:0007829|PDB:1E6B"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:1E6B"
SQ   SEQUENCE   221 AA;  24888 MW;  106BDC8EF3E745BF CRC64;
     MANSGEEKLK LYSYWRSSCA HRVRIALALK GLDYEYIPVN LLKGDQFDSD FKKINPMGTV
     PALVDGDVVI NDSFAIIMYL DEKYPEPPLL PRDLHKRAVN YQAMSIVLSG IQPHQNLAVI
     RYIEEKINVE EKTAWVNNAI TKGFTALEKL LVNCAGKHAT GDEIYLADLF LAPQIHGAIN
     RFQINMEPYP TLAKCYESYN ELPAFQNALP EKQPDAPSST I
//