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Q8T137

- GSHR_DICDI

UniProt

Q8T137 - GSHR_DICDI

Protein

Glutathione reductase

Gene

gsr

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.1 Publication

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei454 – 4541Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 509FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. glutathione binding Source: dictyBase
    3. glutathione-disulfide reductase activity Source: dictyBase
    4. NADP binding Source: dictyBase

    GO - Biological processi

    1. cell redox homeostasis Source: dictyBase
    2. culmination involved in sorocarp development Source: dictyBase
    3. glutathione metabolic process Source: dictyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_176495. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:gsr
    ORF Names:DDB_G0272754
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0272754. gsr.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. intracellular Source: dictyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Glutathione reductasePRO_0000327610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 55Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ8T137.

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0231410.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8T137.
    SMRiQ8T137. Positions 6-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    KOiK00383.
    OMAiTERYEAT.
    PhylomeDBiQ8T137.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8T137-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSTNHFTYL VLGAGSGGIA SARRAAKHLN AKGNGDRIGI VEVTRPGGTC    50
    VNVGCVPKKV MWNTSFIKEM INAAPSYGFD FGGQQVKFNW PTIKKARDEY 100
    IKRLNGIYDS NLAKDNIVRI NGYGRFSGPK EIQVNGANGE KYTADHILIA 150
    AGGRPTVPDV PGKELGITSD GFFELEDLPK STLVVGAGYI AVELAGVLHS 200
    LGSETTMVIR QKQFLRTFDE MLHTTLLKQM TDDGVKFVTE ASIKSLERDV 250
    DGKRIIATTN AGVKLPPVEC VIWAIGRVPN TDDLGIDKAG IQLTEQSGFI 300
    KVDEFQNTNV PGVHAVGDIC GNFLLTPVAI AAGRRLSERL FNGKSDLKFE 350
    YENVATVVFS HPPIGTVGLT EQEAITKYGT ENIKCYNTSF INMFYSVQVH 400
    KVRTSMKLVC LGKEEKVIGL HIIGDGCDEI IQGFAVAVKM GCTKWDLDNT 450
    CAIHPTSAEE LVTMV 465
    Length:465
    Mass (Da):50,483
    Last modified:June 1, 2003 - v2
    Checksum:iE89CAF09AEA6A771
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000008 Genomic DNA. Translation: EAL71014.1.
    RefSeqiXP_644939.1. XM_639847.1.

    Genome annotation databases

    EnsemblProtistsiDDB0231410; DDB0231410; DDB_G0272754.
    GeneIDi8618618.
    KEGGiddi:DDB_G0272754.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000008 Genomic DNA. Translation: EAL71014.1 .
    RefSeqi XP_644939.1. XM_639847.1.

    3D structure databases

    ProteinModelPortali Q8T137.
    SMRi Q8T137. Positions 6-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0231410.

    Proteomic databases

    PRIDEi Q8T137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0231410 ; DDB0231410 ; DDB_G0272754 .
    GeneIDi 8618618.
    KEGGi ddi:DDB_G0272754.

    Organism-specific databases

    dictyBasei DDB_G0272754. gsr.

    Phylogenomic databases

    eggNOGi COG1249.
    KOi K00383.
    OMAi TERYEAT.
    PhylomeDBi Q8T137.

    Enzyme and pathway databases

    Reactomei REACT_176495. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    PROi Q8T137.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01421. gluta_reduc_1. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Reduced glutathione levels affect the culmination and cell fate decision in Dictyostelium discoideum."
      Choi C.-H., Kim B.-J., Jeong S.-Y., Lee C.-H., Kim J.-S., Park S.-J., Yim H.-S., Kang S.-O.
      Dev. Biol. 295:523-533(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiGSHR_DICDI
    AccessioniPrimary (citable) accession number: Q8T137
    Secondary accession number(s): Q558X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3