GSTZ2_ARATH
ID GSTZ2_ARATH Reviewed; 223 AA.
AC Q9ZVQ4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutathione S-transferase Z2;
DE Short=AtGSTZ2;
DE EC=2.5.1.18;
DE AltName: Full=GST class-zeta member 2;
GN Name=GSTZ2; OrderedLocusNames=At2g02380; ORFNames=T16F16.17;
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=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 [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 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).
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:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR EMBL; AC005312; AAC78520.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05572.1; -; Genomic_DNA.
DR PIR; A84436; A84436.
DR RefSeq; NP_178343.1; NM_126295.1.
DR AlphaFoldDB; Q9ZVQ4; -.
DR SMR; Q9ZVQ4; -.
DR STRING; 3702.AT2G02380.1; -.
DR PaxDb; Q9ZVQ4; -.
DR PRIDE; Q9ZVQ4; -.
DR EnsemblPlants; AT2G02380.1; AT2G02380.1; AT2G02380.
DR GeneID; 814769; -.
DR Gramene; AT2G02380.1; AT2G02380.1; AT2G02380.
DR KEGG; ath:AT2G02380; -.
DR Araport; AT2G02380; -.
DR TAIR; locus:2056261; AT2G02380.
DR eggNOG; KOG0868; Eukaryota.
DR HOGENOM; CLU_011226_20_1_1; -.
DR InParanoid; Q9ZVQ4; -.
DR OMA; LHIDNHT; -.
DR OrthoDB; 1283865at2759; -.
DR PhylomeDB; Q9ZVQ4; -.
DR BioCyc; ARA:AT2G02380-MON; -.
DR PRO; PR:Q9ZVQ4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVQ4; baseline and differential.
DR Genevisible; Q9ZVQ4; 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; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; PF13417; GST_N_3; 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 3: Inferred from homology;
KW Cytoplasm; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..223
FT /note="Glutathione S-transferase Z2"
FT /id="PRO_0000186030"
FT DOMAIN 10..91
FT /note="GST N-terminal"
FT DOMAIN 96..221
FT /note="GST C-terminal"
FT BINDING 20..25
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 20..21
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 49..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 62..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 119..121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 25352 MW; AAE7E85746610512 CRC64;
MSYVTDFYQA KLKLYSYWRS SCAHRVRIAL TLKGLDYEYI PVNLLKGDQS DSDFKKINPM
GTVPALVDGD VVINDSFAII MYLDDKYPEP PLLPSDYHKR AVNYQATSIV MSGIQPHQNM
ALFRYLEDKI NAEEKTAWIT NAITKGFTAL EKLLVSCAGK YATGDEVYLA DLFLAPQIHA
AFNRFHINME PFPTLARFYE SYNELPAFQN AVPEKQPDTP STI
