Q9ZVQ3 (GSTZ1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol 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.

Ontologies

Keywords
Biological process	Detoxification Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Isomerase Oxidoreductase Peroxidase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family metabolic process Inferred from electronic annotation. Source: InterPro homogentisate catabolic process Inferred from direct assay PubMed 22980205. Source: TAIR response to stress Inferred from electronic annotation. Source: UniProtKB-KW response to toxic substance Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.1. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW maleylacetoacetate isomerase activity Inferred from direct assay PubMed 22980205. Source: TAIR peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Glutathione S-transferase Z1

PRO_0000186029

Regions

Domain

7 – 88

82

GST N-terminal

Domain

93 – 218

126

GST C-terminal

Region

17 – 22

6

Glutathione binding By similarity

Region

17 – 18

2

Glutathione binding By similarity

Region

46 – 47

2

Glutathione binding By similarity

Region

59 – 60

2

Glutathione binding By similarity

Region

72 – 73

2

Glutathione binding By similarity

Region

116 – 118

3

Glutathione binding By similarity

Sites

Binding site

46

1

Glutathione By similarity

Binding site

60

1

Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Binding site

112

1

Glutathione By similarity

Natural variations

Alternative sequence

49

1

S → SVYRFDLQ in isoform 2.

VSP_041936

Secondary structure

1

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221

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Helix

18 – 29

12

Beta strand

35 – 38

4

Turn

41 – 44

4

Helix

45 – 47

3

Helix

49 – 54

6

Beta strand

60 – 65

6

Beta strand

68 – 72

5

Helix

73 – 83

11

Helix

94 – 109

16

Helix

138 – 151

14

Beta strand

156 – 158

3

Beta strand

161 – 163

3

Helix

166 – 182

17

Helix

190 – 199

10

Helix

203 – 208

6

Helix

210 – 212

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 106BDC8EF3E745BF	FASTA	221	24,888
	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
	Isoform 2 [UniParc]. Checksum: 80B56ED20594C9E8	FASTA	228	25,810
	10 20 30 40 50 60 MANSGEEKLK LYSYWRSSCA HRVRIALALK GLDYEYIPVN LLKGDQFDSV YRFDLQDFKK 70 80 90 100 110 120 INPMGTVPAL VDGDVVINDS FAIIMYLDEK YPEPPLLPRD LHKRAVNYQA MSIVLSGIQP 130 140 150 160 170 180 HQNLAVIRYI EEKINVEEKT AWVNNAITKG FTALEKLLVN CAGKHATGDE IYLADLFLAP 190 200 210 220 QIHGAINRFQ INMEPYPTLA KCYESYNELP AFQNALPEKQ PDAPSSTI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00546895.

PIR

B84436.

RefSeq

NP_178344.1. NM_126296.4.
NP_973400.1. NM_201671.2.

UniGene

At.10192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6B	X-ray	1.65	A	1-221	[»]

ProteinModelPortal

Q9ZVQ3.

SMR

Q9ZVQ3. Positions 8-220.

ModBase

Search...

Proteomic databases

PaxDb

Q9ZVQ3.

PRIDE

Q9ZVQ3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT2G02390.1; AT2G02390.1; AT2G02390.

GeneID

814770.

KEGG

ath:AT2G02390.

Organism-specific databases

TAIR

At2g02390.

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000125758.

InParanoid

Q9ZVQ3.

KO

K01800.

OMA

RAQVRMI.

PhylomeDB

Q9ZVQ3.

ProtClustDB

CLSN2683685.

Enzyme and pathway databases

BRENDA

5.2.1.2. 399.

Gene expression databases

ArrayExpress

Q9ZVQ3.

Genevestigator

Q9ZVQ3.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
[Graphical view]

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR01262. maiA. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9ZVQ3.

Entry information

Entry name

GSTZ1_ARATH

Accession

Primary (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 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program