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A2XMN2

- GSTU1_ORYSI

UniProt

A2XMN2 - GSTU1_ORYSI

Protein

Probable glutathione S-transferase GSTU1

Gene

GSTU1

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (20 Mar 2007)
      Previous versions | rss
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    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

    GO - Biological processi

    1. response to cadmium ion Source: EnsemblPlants/Gramene

    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

    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 – 116
    Helixi16 – 2813
    Beta strandi33 – 364
    Helixi44 – 496
    Turni51 – 533
    Beta strandi58 – 614
    Beta strandi64 – 685
    Helixi69 – 7911
    Helixi97 – 12024
    Helixi127 – 14822
    Beta strandi154 – 1618
    Helixi164 – 1696
    Helixi170 – 1745
    Helixi176 – 1838
    Helixi187 – 1904
    Helixi192 – 20110
    Helixi205 – 2106
    Helixi214 – 22310
    Turni224 – 2263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    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

    MAEEKELVLL DFWVSPFGQR CRIAMAEKGL EFEYREEDLG NKSDLLLRSN    50
    PVHRKIPVLL HAGRPVSESL VILQYLDDAF PGTPHLLSPA NSGDADAAYA 100
    RATARFWADY VDRKLYDCGS RLWRLKGEPQ AAAGREMAEI LRTLEAELGD 150
    REFFGGGGGG RLGFVDVALV PFTAWFYSYE RCGGFSVEEV APRLAAWARR 200
    CGRIDSVAKH LPSPEKVYDF VGVLKKKYGV E 231
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF050102 mRNA. Translation: AAC05216.1.
    CM000128 Genomic DNA. Translation: EAY92092.1.
    PIRiT02765.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF050102 mRNA. Translation: AAC05216.1 .
    CM000128 Genomic DNA. Translation: EAY92092.1 .
    PIRi T02765.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OYJ X-ray 1.95 A/B/C/D 1-231 [» ]
    ProteinModelPortali A2XMN2.
    SMRi A2XMN2. Positions 2-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 39947.LOC_Os03g57200.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei A2XMN2.

    Phylogenomic databases

    eggNOGi NOG245965.
    HOGENOMi HOG000125749.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 40 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

    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