Q9ZRT5 (GSTT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase T1
Short name=AtGSTT1
EC=2.5.1.18

Alternative name(s):
GST class-theta member 1
Glutathione S-transferase 10

Gene names

Name:	GSTT1
Synonyms:	GST10
Ordered Locus Names:	At5g41210
ORF Names:	MEE6.28

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	245 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrobenzyl chloride (pNBC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. Ref.5
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Nucleus Ref.6.
Sequence similarities	Belongs to the GST superfamily. Theta family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Detoxification
Cellular component	Nucleus
Molecular function	Oxidoreductase Peroxidase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to toxin Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.5. Source: TAIR
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from direct assay PubMed 17951448. Source: TAIR
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 245	245	Glutathione S-transferase T1		PRO_0000413574
Regions
	Domain	2 – 83	82	GST N-terminal
	Domain	90 – 233	144	GST C-terminal
	Region	12 – 13	2	Glutathione binding By similarity
	Region	41 – 42	2	Glutathione binding By similarity
	Region	54 – 55	2	Glutathione binding By similarity
	Region	67 – 68	2	Glutathione binding By similarity
	Motif	243 – 245	3	Microbody targeting signal Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9ZRT5 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6F16FE1399E793B7	FASTA	245	27,653
	10 20 30 40 50 60 MMKLKVYADR MSQPSRAVII FCKVNGIQFD EVLISLAKRQ QLSPEFKDIN PLGKVPAIVD 70 80 90 100 110 120 GRLKLFESHA ILIYLSSAFP SVADHWYPND LSKRAKIHSV LDWHHTNLRR GAAGYVLNSV 130 140 150 160 170 180 LGPALGLPLN PKAAAEAEQL LTKSLSTLET FWLKGNAKFL LGSNQPSIAD LSLVCELMQL 190 200 210 220 230 240 QVLDDKDRLR LLSTHKKVEQ WIENTKKATM PHFDETHEIL FKVKEGFQKR REMGTLSKPG LQSKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and cloning of AtGST 10, members of a novel type of plant glutathione transferases." Dixon D.P., Cole D.J., Edwards R. Plant Gene Register PGR99-053 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones." Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"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: FUNCTION, GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia.
[6]	"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily." Dixon D.P., Hawkins T., Hussey P.J., Edwards R. J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ131580 mRNA. Translation: CAA10457.1. AB010072 Genomic DNA. Translation: BAB09723.1. CP002688 Genomic DNA. Translation: AED94654.1. AY054659 mRNA. Translation: AAK96850.1. AY072466 mRNA. Translation: AAL66881.1.
IPI	IPI00546678.
PIR	T51594.
RefSeq	NP_198937.1. NM_123486.3.
UniGene	At.24905.
3D structure databases
HSSP	HSSP built from PDB template 1LJR based on UniProtKB P30712.
ProteinModelPortal	Q9ZRT5.
SMR	Q9ZRT5. Positions 2-202.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ZRT5. 1 interaction.
STRING	3702.AT5G41210.1-P.
Proteomic databases
PaxDb	Q9ZRT5.
PRIDE	Q9ZRT5.
Protocols and materials databases
DNASU	834123.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G41210.1; AT5G41210.1; AT5G41210.
GeneID	834123.
KEGG	ath:AT5G41210.
Organism-specific databases
TAIR	At5g41210.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000125747.
InParanoid	Q9ZRT5.
KO	K00799.
OMA	IMQLEIL.
PhylomeDB	Q9ZRT5.
ProtClustDB	CLSN2914818.
Gene expression databases
Genevestigator	Q9ZRT5.
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. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF02798. GST_N. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTT1_ARATH

Accession

Primary (citable) accession number: Q9ZRT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program