A2XMN2 (GSTU1_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable glutathione S-transferase GSTU1
EC=2.5.1.18

Gene names

Name:	GSTU1
Synonyms:	GST1
ORF Names:	OsI_013325

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Sequence similarities	Belongs to the GST superfamily. Tau family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
Gene Ontology (GO)
Biological_process	cellular response to water deprivation Inferred from electronic annotation. Source: EnsemblPlants/Gramene glutathione metabolic process Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to cadmium ion Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to cold Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to herbicide Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to karrikin Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to oxidative stress Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	apoplast Inferred from electronic annotation. Source: EnsemblPlants/Gramene chloroplast stroma Inferred from electronic annotation. Source: EnsemblPlants/Gramene plasma membrane Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	glutathione binding Inferred from electronic annotation. Source: EnsemblPlants/Gramene 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 – 231	231	Probable glutathione S-transferase GSTU1		PRO_0000295653
Regions
	Domain	5 – 84	80	GST N-terminal
	Domain	97 – 220	124	GST C-terminal
	Region	68 – 69	2	Glutathione binding By similarity
Sites
	Binding site	15	1	Glutathione By similarity
	Binding site	42	1	Glutathione By similarity
	Binding site	56	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Experimental info
	Sequence conflict	88	1	S → P in AAC05216. Ref.1
	Sequence conflict	90	1	A → G in AAC05216. Ref.1
	Sequence conflict	99	1	Y → F in AAC05216. Ref.1
	Sequence conflict	130	1	Q → H in AAC05216. Ref.1
	Sequence conflict	175 – 179	5	WFYSY → CSTAT in AAC05216. Ref.1
	Sequence conflict	201	1	C → R in AAC05216. Ref.1
	Sequence conflict	208	1	A → V in AAC05216. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A2XMN2 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 42C953E8F540DAB0	FASTA	231	25,832
	10 20 30 40 50 60 MAEEKELVLL DFWVSPFGQR CRIAMAEKGL EFEYREEDLG NKSDLLLRSN PVHRKIPVLL 70 80 90 100 110 120 HAGRPVSESL VILQYLDDAF PGTPHLLSPA NSGDADAAYA RATARFWADY VDRKLYDCGS 130 140 150 160 170 180 RLWRLKGEPQ AAAGREMAEI LRTLEAELGD REFFGGGGGG RLGFVDVALV PFTAWFYSYE 190 200 210 220 230 RCGGFSVEEV APRLAAWARR CGRIDSVAKH LPSPEKVYDF VGVLKKKYGV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of rice glutathione S-transferase." Yun C.-H., Lee M.C., Park J.H., Eun M.Y. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Milyang 23.
[2]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.
[3]	"Organisation and structural evolution of the rice glutathione S-transferase gene family." Soranzo N., Sari Gorla M., Mizzi L., De Toma G., Frova C. Mol. Genet. Genomics 271:511-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF050102 mRNA. Translation: AAC05216.1. CM000128 Genomic DNA. Translation: EAY92092.1.
PIR	T02765.
3D structure databases
ProteinModelPortal	A2XMN2.
SMR	A2XMN2. Positions 2-230.
ModBase	Search...
Protein-protein interaction databases
STRING	39947.LOC_Os03g57200.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	A2XMN2.
Phylogenomic databases
eggNOG	NOG245965.
HOGENOM	HOG000125749.
Gene expression databases
ArrayExpress	A2XMN2.
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]
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

GSTU1_ORYSI

Accession

Primary (citable) accession number: A2XMN2
Secondary accession number(s): O65032

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	March 20, 2007
Last modified:	April 3, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program