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Protein

Probable glutathione S-transferase GSTU1

Gene

GSTU1

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151GlutathioneBy similarity
Binding sitei42 – 421GlutathioneBy similarity
Binding sitei56 – 561Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glutathione S-transferase GSTU1 (EC:2.5.1.18)
Gene namesi
Name:GSTU1
Synonyms:GST1
ORF Names:OsI_013325
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
ProteomesiUP000007015: Chromosome 3

Organism-specific databases

GrameneiA2XMN2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Probable glutathione S-transferase GSTU1PRO_0000295653Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi39947.LOC_Os03g57200.1.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi16 – 2813Combined sources
Beta strandi33 – 364Combined sources
Helixi44 – 496Combined sources
Turni51 – 533Combined sources
Beta strandi58 – 614Combined sources
Beta strandi64 – 685Combined sources
Helixi69 – 7911Combined sources
Helixi97 – 12024Combined sources
Helixi127 – 14822Combined sources
Beta strandi154 – 1618Combined sources
Helixi164 – 1696Combined sources
Helixi170 – 1745Combined sources
Helixi176 – 1838Combined sources
Helixi187 – 1904Combined sources
Helixi192 – 20110Combined sources
Helixi205 – 2106Combined sources
Helixi214 – 22310Combined sources
Turni224 – 2263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYJX-ray1.95A/B/C/D1-231[»]
ProteinModelPortaliA2XMN2.
SMRiA2XMN2. Positions 2-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 8480GST N-terminalAdd
BLAST
Domaini97 – 220124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 692Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Tau family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG245965.
HOGENOMiHOG000125749.
OMAiKGEPQAQ.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2XMN2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEEKELVLL DFWVSPFGQR CRIAMAEKGL EFEYREEDLG NKSDLLLRSN
60 70 80 90 100
PVHRKIPVLL HAGRPVSESL VILQYLDDAF PGTPHLLSPA NSGDADAAYA
110 120 130 140 150
RATARFWADY VDRKLYDCGS RLWRLKGEPQ AAAGREMAEI LRTLEAELGD
160 170 180 190 200
REFFGGGGGG RLGFVDVALV PFTAWFYSYE RCGGFSVEEV APRLAAWARR
210 220 230
CGRIDSVAKH LPSPEKVYDF VGVLKKKYGV E
Length:231
Mass (Da):25,832
Last modified:March 20, 2007 - v1
Checksum:i42C953E8F540DAB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881S → P in AAC05216. 1 PublicationCurated
Sequence conflicti90 – 901A → G in AAC05216. 1 PublicationCurated
Sequence conflicti99 – 991Y → F in AAC05216. 1 PublicationCurated
Sequence conflicti130 – 1301Q → H in AAC05216. 1 PublicationCurated
Sequence conflicti175 – 1795WFYSY → CSTAT in AAC05216. 1 PublicationCurated
Sequence conflicti201 – 2011C → R in AAC05216. 1 PublicationCurated
Sequence conflicti208 – 2081A → V in AAC05216. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050102 mRNA. Translation: AAC05216.1.
CM000128 Genomic DNA. Translation: EAY92092.1.
PIRiT02765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050102 mRNA. Translation: AAC05216.1.
CM000128 Genomic DNA. Translation: EAY92092.1.
PIRiT02765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYJX-ray1.95A/B/C/D1-231[»]
ProteinModelPortaliA2XMN2.
SMRiA2XMN2. Positions 2-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os03g57200.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiA2XMN2.

Phylogenomic databases

eggNOGiNOG245965.
HOGENOMiHOG000125749.
OMAiKGEPQAQ.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGSTU1_ORYSI
AccessioniPrimary (citable) accession number: A2XMN2
Secondary accession number(s): O65032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: March 20, 2007
Last modified: January 7, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.