Reviewed, UniProtKB/Swiss-Prot Q9ZVQ3 (GSTZ1_ARATH)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase zeta-class 1
      Short name=AtGSTZ1
    EC=2.5.1.18
Alternative name(s):
    Maleylacetone isomerase
      Short name=MAI
    EC=5.2.1.-

Gene names

Name:	GST18
Synonyms:	GSTZ, GSTZ1
Ordered Locus Names:	At2g02390
ORF Names:	T16F16.18

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the GST superfamily. Zeta family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Isomerase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family metabolic process Inferred from electronic annotation. Source: InterPro toxin catabolic process Traceable author statement. Source: TAIR
Cellular component	cytoplasm Non-traceable author statement. Source: TAIR
Molecular function	glutathione transferase activity Inferred from electronic annotation. Source: EC isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Glutathione S-transferase zeta-class 1

PRO_0000186029

Regions

Domain

7 – 88

82

GST N-terminal

Domain

93 – 218

126

GST C-terminal

Sites

Active site

17

1

Potential

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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the glutathione S-transferase family in Arabidopsis thaliana." Wagner U., Mauch F. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 11368331] [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: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"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: 11352584] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF288182 mRNA. Translation: AAG30131.1.
AJ278293 mRNA. Translation: CAC19475.1.
AY208155 mRNA. Translation: AAO60039.1.
AC005312 Genomic DNA. Translation: AAC78521.1.
AY052332 mRNA. Translation: AAK96525.1.
AY061901 mRNA. Translation: AAL31228.1.

IPI

IPI00546895.

PIR

B84436.

RefSeq

NP_178344.1.

UniGene

At.10192

3D structure databases

PDBPDBe

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

ModBase

Search...

Proteomic databases

PRIDE

Q9ZVQ3.

Genome annotation databases

GeneID

814770.

GenomeReviews

Gene locus AT2G02390 in contig CT485783_GR.

KEGG

ath:AT2G02390.

NMPDR

fig|3702.1.peg.7836.

Organism-specific databases

TAIR

At2g02390.

Enzyme and pathway databases

BRENDA

2.5.1.18. 302.
5.2.1.2. 302.

Gene expression databases

ArrayExpress

Q9ZVQ3.

Family and domain databases

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.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01262. maiA. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

GSTZ1_ARATH

Accession

Primary (citable) accession number: Q9ZVQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)