GSTZ1_ARATH
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 03-AUG-2022, entry version 165.
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.AT2G02390.3; -.
DR PaxDb; Q9ZVQ3; -.
DR PRIDE; Q9ZVQ3; -.
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; locus:2056161; AT2G02390.
DR eggNOG; KOG0868; Eukaryota.
DR HOGENOM; CLU_011226_20_1_1; -.
DR InParanoid; Q9ZVQ3; -.
DR OMA; VYNAHRF; -.
DR OrthoDB; 1283865at2759; -.
DR PhylomeDB; Q9ZVQ3; -.
DR BioCyc; ARA:AT2G02390-MON; -.
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 Genevisible; Q9ZVQ3; AT.
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; IBA:GO_Central.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; IDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:1902000; P:homogentisate catabolic process; IDA:TAIR.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
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 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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01262; maiA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
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
