Reviewed, UniProtKB/Swiss-Prot P42760 (GSTF1_ARATH)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase 1
    EC=2.5.1.18
Alternative name(s):
    GST class-phi member 1

Gene names

Name:	GST1
Synonyms:	ERD11
Ordered Locus Names:	At1g02930
ORF Names:	F22D16.7

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	208 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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm Probable.
Induction	By dehydration stress.
Sequence similarities	Belongs to the GST superfamily. Phi family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Stress response
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 oxidative stress Inferred from direct assay. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR response to water deprivation Ref.1 Inferred from expression pattern. Source: TAIR toxin catabolic process Traceable author statement. Source: TAIR
Cellular component	cell wall Inferred from direct assay. Source: TAIR mitochondrion 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 – 208	208	Glutathione S-transferase 1		PRO_0000185846
Regions
	Domain	2 – 83	82	GST N-terminal
	Domain	89 – 208	120	GST C-terminal
Experimental info
	Sequence conflict	12	1	S → F in BAA04553. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42760-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 113CED008A11902F	FASTA	208	23,486
	10 20 30 40 50 60 MAGIKVFGHP ASTATRRVLI ALHEKNVDFE FVHVELKDGE HKKEPFILRN PFGKVPAFED 70 80 90 100 110 120 GDFKIFESRA ITQYIAHEFS DKGNNLLSTG KDMAIIAMGI EIESHEFDPV GSKLVWEQVL 130 140 150 160 170 180 KPLYGMTTDK TVVEEEEAKL AKVLDVYEHR LGESKYLASD HFTLVDLHTI PVIQYLLGTP 190 200 TKKLFDERPH VSAWVADITS RPSAQKVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible genes that encode putative glutathione S-transferases in Arabidopsis thaliana L." Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K. FEBS Lett. 335:189-192(1993) [PubMed: 8253194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Characterization of a glutathione S-transferase gene ATGST1 in Arabidopsis thaliana." Yang K.Y., Kim E.Y., Kim K.S., Choi S.N., Guh J.O., Kim K.C., Cho B.-H. Plant Cell Rep. 17:700-704(1999) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[3]	Yu G.-L., Ausubel F.M. Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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.
[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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D17672 mRNA. Translation: BAA04553.1. Y11727 Genomic DNA. Translation: CAA72413.1. L12057 Genomic RNA. No translation available. AC009525 Genomic DNA. Translation: AAF02873.1. AY050332 mRNA. Translation: AAK91349.1. AY097392 mRNA. Translation: AAM19908.1.
IPI	IPI00548409.
PIR	G86159. S39541.
RefSeq	NP_171792.1.
UniGene	At.20350 At.23846
3D structure databases
HSSP	HSSP built from PDB template 1GNW based on UniProtKB P46422.
SMR	P42760. Positions 3-207.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	P42760.
Proteomic databases
PRIDE	P42760.
Genome annotation databases
GeneID	839515.
GenomeReviews	Gene locus AT1G02930 in contig CT485782_GR.
KEGG	ath:AT1G02930.
NMPDR	fig|3702.1.peg.423.
Organism-specific databases
TAIR	At1g02930.
Phylogenomic databases
OMA	P42760. ARYIATK.
Enzyme and pathway databases
BRENDA	2.5.1.18. 302.
Gene expression databases
ArrayExpress	P42760.
GermOnline	AT1G02930. 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

GSTF1_ARATH

Accession

Primary (citable) accession number: P42760

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)