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Q6HA23

- GSHR_KLULA

UniProt

Q6HA23 - GSHR_KLULA

Protein

Glutathione reductase

Gene

GLR1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.By similarity

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei473 – 4731Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 609FADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:GLR1
    Ordered Locus Names:KLLA0E24112g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome E

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Glutathione reductasePRO_0000067968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi60 ↔ 65Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ6HA23.
    SMRiQ6HA23. Positions 21-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiGTNSDGF.
    OrthoDBiEOG79W9F2.

    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.

    Q6HA23-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIRNTINRI IIRRNMSDSI RHYDYLVIGG GSGGVASSRR AASYGAKTLL    50
    IEAKAMGGTC VNKGCVPKKV MWYASDLATR IGHAHSYNLF EDLPLTKENL 100
    TFNWPEFKKK RDAYIHRLNG IYERNLTKEG VDYVYGWASF TVDGKVQVKK 150
    ADNCTETYTA DHILVATGGK PIYPAKIPGY DYGVSSDEFF ELEDQPKKVV 200
    VVGAGYIGVE IAGVFNGLGS DSHLVIRGET VLRKFDDCIQ ETVTDTYIKE 250
    GVNIHKSSNV TKVEKDESTG KLNIQLDTGK NIDNVDSLIW TIGRRSLLGL 300
    GLENIGVKLD AKEQIVVDEY QNSSVKNVYS LGDVVGKVEL TPVAIAAGRK 350
    LSNRLFGPEK FKNQKQDYEN VPSVVFSHPE AGSIGLSERE AIEKFGKDNV 400
    KVYNSKFNAM YYAMMEEKDK TPTRYKLVCT GEEEKVVGLH IIGDSSAEIL 450
    QGFGVAIKMG ATKADFDSCV AIHPTSAEEL VTLT 484
    Length:484
    Mass (Da):53,378
    Last modified:July 19, 2004 - v1
    Checksum:iCEE24F6377CC0ECB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ504414 Genomic DNA. Translation: CAD43213.1.
    CR382125 Genomic DNA. Translation: CAH00123.1.
    RefSeqiXP_455036.1. XM_455036.1.

    Genome annotation databases

    GeneIDi2894346.
    KEGGikla:KLLA0E24069g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ504414 Genomic DNA. Translation: CAD43213.1 .
    CR382125 Genomic DNA. Translation: CAH00123.1 .
    RefSeqi XP_455036.1. XM_455036.1.

    3D structure databases

    ProteinModelPortali Q6HA23.
    SMRi Q6HA23. Positions 21-483.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2894346.
    KEGGi kla:KLLA0E24069g.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi GTNSDGF.
    OrthoDBi EOG79W9F2.

    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. "Isolation and characterization of two nuclear genes encoding glutathione and thioredoxin reductases from the yeast Kluyveromyces lactis."
      Tarrio N., Diaz Prado S., Cerdan M.E., Gonzales Siso M.I.
      Biochim. Biophys. Acta 1678:170-175(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiGSHR_KLULA
    AccessioniPrimary (citable) accession number: Q6HA23
    Secondary accession number(s): Q6CM03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3