Reviewed, UniProtKB/Swiss-Prot Q9SRY5 (GST11_ARATH)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase 11
    EC=2.5.1.18
Alternative name(s):
    GST class-phi

Gene names

Name:	GST11
Ordered Locus Names:	At1g02920
ORF Names:	F22D16.8

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	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. In plants, may have a detoxification role against certain herbicides By similarity.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the GST superfamily. Phi family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from expression pattern. Source: TAIR response to cadmium ion Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR toxin catabolic process Ref.2 Traceable author statement. Source: TAIR
Cellular component	nucleus Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	copper ion binding Inferred from direct assay. Source: TAIR glutathione binding Inferred from direct assay. Source: TAIR glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	Glutathione S-transferase 11		PRO_0000185852
Regions
	Domain	2 – 83	82	GST N-terminal
	Domain	90 – 209	120	GST C-terminal
	Compositional bias	135 – 138	4	Poly-Glu
Experimental info
	Sequence conflict	187	1	D → A Ref.1
	Sequence conflict	187	1	D → A Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SRY5-1 [UniParc]. Last modified February 5, 2008. Version 3. Checksum: FD2CC0FD28A31ACC	FASTA	209	23,598
	10 20 30 40 50 60 MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED 70 80 90 100 110 120 GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV 130 140 150 160 170 180 LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT 190 200 PTKKLFDERP HVSAWVADIT SRPSAKKVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel glutathione S-transferase gene in Arabidopsis thaliana." Yang K.Y., Kim C.S., Kim K.C., Cho B.-H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"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: 12090627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y14251 Genomic DNA. Translation: CAA74639.1. AF288177 mRNA. Translation: AAG30126.1. AC009525 Genomic DNA. Translation: AAF02874.1. AY062642 mRNA. Translation: AAL32720.1. AY093281 mRNA. Translation: AAM13280.1.
IPI	IPI00530258.
PIR	F86159.
RefSeq	NP_171791.1.
UniGene	At.20350 At.23846 At.71571
3D structure databases
HSSP	HSSP built from PDB template 1GNW based on UniProtKB P46422.
SMR	Q9SRY5. Positions 3-208.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	Q9SRY5.
Proteomic databases
PRIDE	Q9SRY5.
Genome annotation databases
GeneID	839295.
GenomeReviews	Gene locus AT1G02920 in contig CT485782_GR.
KEGG	ath:AT1G02920.
Organism-specific databases
TAIR	At1g02920.
Phylogenomic databases
OMA	Q9SRY5. DIAGIAM.
Enzyme and pathway databases
BRENDA	2.5.1.18. 302.
Gene expression databases
GermOnline	AT1G02920. Arabidopsis thaliana.
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. 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]
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GST11_ARATH

Accession

Primary (citable) accession number: Q9SRY5
Secondary accession number(s): O23720, Q541C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 5, 2008
Last modified:	May 5, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)