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P48641

- GSHRC_ARATH

UniProt

P48641 - GSHRC_ARATH

Protein

Glutathione reductase, cytosolic

Gene

At3g24170

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei234 – 2341NADPBy similarity
    Binding sitei240 – 2401NADPBy similarity
    Active sitei472 – 4721Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi64 – 7310FADBy 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

    Enzyme and pathway databases

    BioCyciARA:AT3G24170-MONOMER.
    ARA:GQT-556-MONOMER.
    ARA:GQT-557-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase, cytosolic (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Alternative name(s):
    OBP29
    Gene namesi
    Ordered Locus Names:At3g24170
    ORF Names:MUJ8.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G24170.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. peroxisome Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Glutathione reductase, cytosolicPRO_0000067961Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi73 ↔ 78Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP48641.
    PRIDEiP48641.

    Expressioni

    Gene expression databases

    ArrayExpressiP48641.
    GenevestigatoriP48641.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-60756N.

    Structurei

    3D structure databases

    ProteinModelPortaliP48641.
    SMRiP48641. Positions 24-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    InParanoidiP48641.
    KOiK00383.
    OMAiDAKNYGW.
    PhylomeDBiP48641.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    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.
    TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48641-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARKMLVDGE IDKVAADEAN ATHYDFDLFV IGAGSGGVRA ARFSANHGAK    50
    VGICELPFHP ISSEEIGGVG GTCVIRGCVP KKILVYGATY GGELEDAKNY 100
    GWEINEKVDF TWKKLLQKKT DEILRLNNIY KRLLANAAVK LYEGEGRVVG 150
    PNEVEVRQID GTKISYTAKH ILIATGSRAQ KPNIPGHELA ITSDEALSLE 200
    EFPKRAIVLG GGYIAVEFAS IWRGMGATVD LFFRKELPLR GFDDEMRALV 250
    ARNLEGRGVN LHPQTSLTQL TKTDQGIKVI SSHGEEFVAD VVLFATGRSP 300
    NTKRLNLEAV GVELDQAGAV KVDEYSRTNI PSIWAVGDAT NRINLTPVAL 350
    MEATCFANTA FGGKPTKAEY SNVACAVFCI PPLAVVGLSE EEAVEQATGD 400
    ILVFTSGFNP MKNTISGRQE KTLMKLIVDE KSDKVIGASM CGPDAAEIMQ 450
    GIAIALKCGA TKAQFDSTVG IHPSSAEEFV TMRSVTRRIA HKPKPKTNL 499
    Length:499
    Mass (Da):53,871
    Last modified:February 1, 1996 - v1
    Checksum:iD6B29E8B5B867186
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621T → A in AAK25938. (PubMed:14593172)Curated
    Sequence conflicti162 – 1621T → A in AAK64087. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37697 mRNA. Translation: AAB67841.1.
    AB028621 Genomic DNA. Translation: BAB01358.1.
    CP002686 Genomic DNA. Translation: AEE76865.1.
    CP002686 Genomic DNA. Translation: AEE76866.1.
    CP002686 Genomic DNA. Translation: AEE76867.1.
    AF360228 mRNA. Translation: AAK25938.1.
    AY040029 mRNA. Translation: AAK64087.1.
    AY140042 mRNA. Translation: AAM98183.1.
    AY142628 mRNA. Translation: AAN13086.1.
    BT008870 mRNA. Translation: AAP68309.1.
    RefSeqiNP_001030756.2. NM_001035679.2.
    NP_001118688.1. NM_001125216.1.
    NP_189059.1. NM_113322.4.
    UniGeneiAt.24980.

    Genome annotation databases

    EnsemblPlantsiAT3G24170.1; AT3G24170.1; AT3G24170.
    AT3G24170.2; AT3G24170.2; AT3G24170.
    AT3G24170.3; AT3G24170.3; AT3G24170.
    GeneIDi822003.
    KEGGiath:AT3G24170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37697 mRNA. Translation: AAB67841.1 .
    AB028621 Genomic DNA. Translation: BAB01358.1 .
    CP002686 Genomic DNA. Translation: AEE76865.1 .
    CP002686 Genomic DNA. Translation: AEE76866.1 .
    CP002686 Genomic DNA. Translation: AEE76867.1 .
    AF360228 mRNA. Translation: AAK25938.1 .
    AY040029 mRNA. Translation: AAK64087.1 .
    AY140042 mRNA. Translation: AAM98183.1 .
    AY142628 mRNA. Translation: AAN13086.1 .
    BT008870 mRNA. Translation: AAP68309.1 .
    RefSeqi NP_001030756.2. NM_001035679.2.
    NP_001118688.1. NM_001125216.1.
    NP_189059.1. NM_113322.4.
    UniGenei At.24980.

    3D structure databases

    ProteinModelPortali P48641.
    SMRi P48641. Positions 24-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60756N.

    Proteomic databases

    PaxDbi P48641.
    PRIDEi P48641.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G24170.1 ; AT3G24170.1 ; AT3G24170 .
    AT3G24170.2 ; AT3G24170.2 ; AT3G24170 .
    AT3G24170.3 ; AT3G24170.3 ; AT3G24170 .
    GeneIDi 822003.
    KEGGi ath:AT3G24170.

    Organism-specific databases

    TAIRi AT3G24170.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    InParanoidi P48641.
    KOi K00383.
    OMAi DAKNYGW.
    PhylomeDBi P48641.

    Enzyme and pathway databases

    BioCyci ARA:AT3G24170-MONOMER.
    ARA:GQT-556-MONOMER.
    ARA:GQT-557-MONOMER.

    Gene expression databases

    ArrayExpressi P48641.
    Genevestigatori P48641.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    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 TIGR01424. gluta_reduc_2. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An Arabidopsis cDNA homologous to glutathione reductase."
      Loebler M.
      Plant Gene Register PGR96-053
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiGSHRC_ARATH
    AccessioniPrimary (citable) accession number: P48641
    Secondary accession number(s): Q2V3T0, Q94BM6, Q9C5I4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3