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Glutathione S-transferase Z1 (AtGSTZ1) (EC 2.5.1.18) (GST class-zeta member 1) (Glutathione S-transferase 18) (Maleylacetone isomerase) (MAI) (EC 5.2.1.-)

 GSTZ1_ARATH             Reviewed;         221 AA.
Q9ZVQ3; Q0WWK7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Glutathione S-transferase Z1;
Short=AtGSTZ1;
EC=2.5.1.18;
AltName: Full=GST class-zeta member 1;
AltName: Full=Glutathione S-transferase 18;
AltName: Full=Maleylacetone isomerase;
Short=MAI;
EC=5.2.1.-;
Name=GSTZ1; Synonyms=GST18, GSTZ; OrderedLocusNames=At2g02390;
ORFNames=T16F16.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, GENE FAMILY, AND
NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12090627; DOI=10.1023/A:1015557300450;
Wagner U., Edwards R., Dixon D.P., Mauch F.;
"Probing the diversity of the Arabidopsis glutathione S-transferase
gene family.";
Plant Mol. Biol. 49:515-532(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=cv. Columbia;
PubMed=11368331; DOI=10.1006/abbi.2000.2125;
Dixon D.P., Cole D.J., Edwards R.;
"Characterisation of a zeta class glutathione transferase from
Arabidopsis thaliana with a putative role in tyrosine catabolism.";
Arch. Biochem. Biophys. 384:407-412(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Chen D., Kawarasaki Y., Nakano H., Yamane T.;
"Arabidopsis thaliana ecotype Columbia for glutathione S-transferase
zeta (AtGSTZ) mRNA.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
[8]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=11352584; DOI=10.1006/jmbi.2001.4638;
Thom R., Dixon D.P., Edwards R., Cole D.J., Lapthorn A.J.;
"The structure of a zeta class glutathione S-transferase from
Arabidopsis thaliana: characterisation of a GST with novel active-site
architecture and a putative role in tyrosine catabolism.";
J. Mol. Biol. 308:949-962(2001).
-!- FUNCTION: Acts a maleylacetone isomerase. Also catalyzes the
glutathione-dependent dehalogenation of dichloroacetic acid to
glyoxylic acid. In vitro, possesses glutathione peroxidase
activity toward cumene hydroperoxide and linoleic acid-13-
hydroperoxide. {ECO:0000269|PubMed:12090627}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ZVQ3-1; Sequence=Displayed;
Name=2;
IsoId=Q9ZVQ3-2; Sequence=VSP_041936;
Note=No experimental confirmation available.;
-!- INDUCTION: By salicylic acid, methyl jasmonate, auxin, H(2)O(2),
and the pathogen Hyaloperonospora parasitica.
{ECO:0000269|PubMed:12090627}.
-!- SIMILARITY: Belongs to the GST superfamily. Zeta family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF288182; AAG30131.1; -; mRNA.
EMBL; AJ278293; CAC19475.1; -; mRNA.
EMBL; AY208155; AAO60039.1; -; mRNA.
EMBL; AC005312; AAC78521.1; -; Genomic_DNA.
EMBL; CP002685; AEC05573.1; -; Genomic_DNA.
EMBL; CP002685; AEC05575.1; -; Genomic_DNA.
EMBL; AY052332; AAK96525.1; -; mRNA.
EMBL; AY061901; AAL31228.1; -; mRNA.
EMBL; AK226342; BAE98491.1; -; mRNA.
PIR; B84436; B84436.
RefSeq; NP_178344.1; NM_126296.5. [Q9ZVQ3-1]
RefSeq; NP_973400.1; NM_201671.3. [Q9ZVQ3-2]
UniGene; At.10192; -.
PDB; 1E6B; X-ray; 1.65 A; A=1-221.
PDBsum; 1E6B; -.
ProteinModelPortal; Q9ZVQ3; -.
SMR; Q9ZVQ3; -.
STRING; 3702.AT2G02390.3; -.
PaxDb; Q9ZVQ3; -.
EnsemblPlants; AT2G02390.1; AT2G02390.1; AT2G02390. [Q9ZVQ3-1]
EnsemblPlants; AT2G02390.3; AT2G02390.3; AT2G02390. [Q9ZVQ3-2]
GeneID; 814770; -.
Gramene; AT2G02390.1; AT2G02390.1; AT2G02390.
Gramene; AT2G02390.3; AT2G02390.3; AT2G02390.
KEGG; ath:AT2G02390; -.
Araport; AT2G02390; -.
TAIR; locus:2056161; AT2G02390.
eggNOG; KOG0868; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125758; -.
InParanoid; Q9ZVQ3; -.
KO; K01800; -.
OMA; CRQPDTP; -.
PhylomeDB; Q9ZVQ3; -.
BioCyc; ARA:AT2G02390-MONOMER; -.
BRENDA; 5.2.1.2; 399.
Reactome; R-ATH-156590; Glutathione conjugation.
Reactome; R-ATH-71182; Phenylalanine and tyrosine catabolism.
EvolutionaryTrace; Q9ZVQ3; -.
PRO; PR:Q9ZVQ3; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9ZVQ3; baseline and differential.
Genevisible; Q9ZVQ3; AT.
GO; GO:0005737; C:cytoplasm; NAS:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
GO; GO:0016034; F:maleylacetoacetate isomerase activity; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
GO; GO:1902000; P:homogentisate catabolic process; IDA:TAIR.
GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
CDD; cd03191; GST_C_Zeta; 1.
CDD; cd03042; GST_N_Zeta; 1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR005955; GST_Zeta.
InterPro; IPR034330; GST_Zeta_C.
InterPro; IPR034333; GST_Zeta_N.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF13409; GST_N_2; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR01262; maiA; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Detoxification; Isomerase; Oxidoreductase; Peroxidase;
Reference proteome; Stress response; Transferase.
CHAIN 1 221 Glutathione S-transferase Z1.
/FTId=PRO_0000186029.
DOMAIN 7 88 GST N-terminal.
DOMAIN 93 218 GST C-terminal.
REGION 17 22 Glutathione binding. {ECO:0000250}.
REGION 17 18 Glutathione binding. {ECO:0000250}.
REGION 46 47 Glutathione binding. {ECO:0000250}.
REGION 59 60 Glutathione binding. {ECO:0000250}.
REGION 72 73 Glutathione binding. {ECO:0000250}.
REGION 116 118 Glutathione binding. {ECO:0000250}.
BINDING 46 46 Glutathione. {ECO:0000250}.
BINDING 60 60 Glutathione; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
BINDING 112 112 Glutathione. {ECO:0000250}.
VAR_SEQ 49 49 S -> SVYRFDLQ (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_041936.
STRAND 10 13 {ECO:0000244|PDB:1E6B}.
HELIX 18 29 {ECO:0000244|PDB:1E6B}.
STRAND 35 38 {ECO:0000244|PDB:1E6B}.
TURN 41 44 {ECO:0000244|PDB:1E6B}.
HELIX 45 47 {ECO:0000244|PDB:1E6B}.
HELIX 49 54 {ECO:0000244|PDB:1E6B}.
STRAND 60 65 {ECO:0000244|PDB:1E6B}.
STRAND 68 72 {ECO:0000244|PDB:1E6B}.
HELIX 73 83 {ECO:0000244|PDB:1E6B}.
HELIX 94 109 {ECO:0000244|PDB:1E6B}.
HELIX 138 151 {ECO:0000244|PDB:1E6B}.
STRAND 156 158 {ECO:0000244|PDB:1E6B}.
STRAND 161 163 {ECO:0000244|PDB:1E6B}.
HELIX 166 182 {ECO:0000244|PDB:1E6B}.
HELIX 190 199 {ECO:0000244|PDB:1E6B}.
HELIX 203 208 {ECO:0000244|PDB:1E6B}.
HELIX 210 212 {ECO:0000244|PDB:1E6B}.
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


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