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Q9ZVQ3 (GSTZ1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Z1

Short name=AtGSTZ1
EC=2.5.1.18
Alternative name(s):
GST class-zeta member 1
Glutathione S-transferase 18
Maleylacetone isomerase
Short name=MAI
EC=5.2.1.-
Gene names
Name:GSTZ1
Synonyms:GST18, GSTZ
Ordered Locus Names:At2g02390
ORF Names:T16F16.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer.

Subcellular location

Cytoplasmcytosol By similarity.

Induction

By salicylic acid, methyl jasmonate, auxin, H2O2, and the pathogen Hyaloperonospora parasitica. Ref.1

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ZVQ3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ZVQ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-49: S → SVYRFDLQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Glutathione S-transferase Z1
PRO_0000186029

Regions

Domain7 – 8882GST N-terminal
Domain93 – 218126GST C-terminal
Region17 – 226Glutathione binding By similarity
Region17 – 182Glutathione binding By similarity
Region46 – 472Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity
Region116 – 1183Glutathione binding By similarity

Sites

Binding site461Glutathione By similarity
Binding site601Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1121Glutathione By similarity

Natural variations

Alternative sequence491S → SVYRFDLQ in isoform 2.
VSP_041936

Secondary structure

................................. 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 106BDC8EF3E745BF

FASTA22124,888
        10         20         30         40         50         60 
MANSGEEKLK LYSYWRSSCA HRVRIALALK GLDYEYIPVN LLKGDQFDSD FKKINPMGTV 

        70         80         90        100        110        120 
PALVDGDVVI NDSFAIIMYL DEKYPEPPLL PRDLHKRAVN YQAMSIVLSG IQPHQNLAVI 

       130        140        150        160        170        180 
RYIEEKINVE EKTAWVNNAI TKGFTALEKL LVNCAGKHAT GDEIYLADLF LAPQIHGAIN 

       190        200        210        220 
RFQINMEPYP TLAKCYESYN ELPAFQNALP EKQPDAPSST I 

« Hide

Isoform 2 [UniParc].

Checksum: 80B56ED20594C9E8
Show »

FASTA22825,810

References

« Hide 'large scale' references
[1]"Probing the diversity of the Arabidopsis glutathione S-transferase gene family."
Wagner U., Edwards R., Dixon D.P., Mauch F.
Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[2]"Characterisation of a zeta class glutathione transferase from Arabidopsis thaliana with a putative role in tyrosine catabolism."
Dixon D.P., Cole D.J., Edwards R.
Arch. Biochem. Biophys. 384:407-412(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: cv. Columbia.
[3]"Arabidopsis thaliana ecotype Columbia for glutathione S-transferase zeta (AtGSTZ) mRNA."
Chen D., Kawarasaki Y., Nakano H., Yamane T.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[8]"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."
Thom R., Dixon D.P., Edwards R., Cole D.J., Lapthorn A.J.
J. Mol. Biol. 308:949-962(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF288182 mRNA. Translation: AAG30131.1.
AJ278293 mRNA. Translation: CAC19475.1.
AY208155 mRNA. Translation: AAO60039.1.
AC005312 Genomic DNA. Translation: AAC78521.1.
CP002685 Genomic DNA. Translation: AEC05573.1.
CP002685 Genomic DNA. Translation: AEC05575.1.
AY052332 mRNA. Translation: AAK96525.1.
AY061901 mRNA. Translation: AAL31228.1.
AK226342 mRNA. Translation: BAE98491.1.
PIRB84436.
RefSeqNP_178344.1. NM_126296.4. [Q9ZVQ3-1]
NP_973400.1. NM_201671.2. [Q9ZVQ3-2]
UniGeneAt.10192.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6BX-ray1.65A1-221[»]
ProteinModelPortalQ9ZVQ3.
SMRQ9ZVQ3. Positions 8-220.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9ZVQ3.
PRIDEQ9ZVQ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G02390.1; AT2G02390.1; AT2G02390. [Q9ZVQ3-1]
GeneID814770.
KEGGath:AT2G02390.

Organism-specific databases

TAIRAT2G02390.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125758.
InParanoidQ9ZVQ3.
KOK01800.
OMADACTRLP.
PhylomeDBQ9ZVQ3.

Enzyme and pathway databases

BioCycARA:AT2G02390-MONOMER.
ARA:GQT-1345-MONOMER.
ARA:GQT-1346-MONOMER.
BRENDA5.2.1.2. 399.

Gene expression databases

ArrayExpressQ9ZVQ3.
GenevestigatorQ9ZVQ3.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01262. maiA. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZVQ3.
PROQ9ZVQ3.

Entry information

Entry nameGSTZ1_ARATH
AccessionPrimary (citable) accession number: Q9ZVQ3
Secondary accession number(s): Q0WWK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names