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P80461

- GSHRP_TOBAC

UniProt

P80461 - GSHRP_TOBAC

Protein

Glutathione reductase, chloroplastic

Gene

GOR

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the chloroplast.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei283 – 2831NADPBy similarity
    Binding sitei289 – 2891NADPBy similarity
    Active sitei521 – 5211Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi118 – 12710FADBy 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, chloroplastic (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:GOR
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei‹1 – 66›66Chloroplast1 PublicationAdd
    BLAST
    Chaini67 – 557491Glutathione reductase, chloroplasticPRO_0000030284Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi127 ↔ 132Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP80461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    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: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80461-1 [UniParc]FASTAAdd to Basket

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    ATSLSTPKLS TTLSSPTLHS LLYKHKFSLL SLSNPIKPLH FNFLTHSRST    50
    PSSLSCTRRR FTAPRAESSN GADAPRHYDF DLFTIGAGSG GVRASRFASN 100
    FGASVAVCEL PFSTISSDST GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE 150
    SCGFGWNYDV EPRFDWSTLI ANKNAELQRL TGIYKNILKN AGVTLIEGRG 200
    KVVDPHTVDV DGKLYSAKNI LISVGGRPFI PDIPGSEYAI DSDAALDLPT 250
    KPNKIAIVGG GYIALEFAGI FNGLKSEVHV FIRQKKVLRG FDEEIRDFVG 300
    EQMSLRGIEF HTEESPQAIV KSADGSLSLK TSRGTVEGFS HIMFATGRRP 350
    NTKNLGLETV GVKMTKNGAI EVDEYSRTSV PSIWAVGDVT DRINLTPVAL 400
    MEGGALAKTI FAHEPTKPDY RNVPAAVFSQ PPIGQVGLME EQAIKEFGDV 450
    DVYTANFRPL KATISGLPDR VFMKLIVCAK TSKVLGLHMC GDDAPEIVQG 500
    FAIAVKAGLT KADFDATVGI HPTSAEEFVT MRTPTRKVRS SPSEGKAEHD 550
    IKAAAGV 557
    Length:557
    Mass (Da):60,035
    Last modified:October 1, 1996 - v1
    Checksum:i79813D1C6AA1D784
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76293 mRNA. Translation: CAA53925.1.
    PIRiS38908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76293 mRNA. Translation: CAA53925.1 .
    PIRi S38908.

    3D structure databases

    ProteinModelPortali P80461.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme."
      Creissen G.P., Mullineaux P.M.
      Planta 197:422-425(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Willows R.D., Kannangara G.C., Svendsen I.
      Submitted (JUN-1995) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 67-74.
      Tissue: Leaf.

    Entry informationi

    Entry nameiGSHRP_TOBAC
    AccessioniPrimary (citable) accession number: P80461
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 94 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3