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P48640

- GSHRP_SOYBN

UniProt

P48640 - GSHRP_SOYBN

Protein

Glutathione reductase, chloroplastic

Gene

GR

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (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 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 sitei269 – 2691NADPBy similarity
    Binding sitei275 – 2751NADPBy similarity
    Active sitei507 – 5071Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi105 – 1139FADBy 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:GR
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Unplaced

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252ChloroplastSequence AnalysisAdd
    BLAST
    Chaini53 – 544492Glutathione reductase, chloroplasticPRO_0000030282Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi113 ↔ 118Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Gene expression databases

    GenevestigatoriP48640.

    Structurei

    3D structure databases

    ProteinModelPortaliP48640.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    KOiK00383.

    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.

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

    P48640-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSLSVSPS LSLNTLFIAK ALPLSRPSFL SLPLPKSLLS LSTRRRTFIV    50
    RAESQNGRDP VPAHYDFDLF TIGAGSGGVR ARRFAANYGA SVAICELPFS 100
    TISSETTGVG GTCVIRGCVP KKLLVYASKF SHEFEESNGF GWRYDSEPKH 150
    DWSSFIANKN AELQRLTGIY KNILNNAGVK LIEGHGKMID PHTVDVNGKL 200
    YSAKHILVAV GGRPFIPDIP GKELAIDSDA ALDLPTKPVK IAIVGGGYIA 250
    LEFAGIFNGL KSEVHVFIRQ KKVLRGFDEE IRDFVEEQMS VRGIEFHTEE 300
    SPQAITKSAD GSFSLKTNKG TVDGFSHIMF ATGRRPNTQN LGLESVGVKL 350
    AKDGAIEVDE YSQTSVYSIW AVGDVTNRIN LTPVALMEGG ALVKTLFQDN 400
    PTKPDYRAVP SAVFSQPPIG QVGLTEEQAV QQYGDIDIFT ANFRPLKATL 450
    SGLPDRVFMK LVVCAKTNEV LGLHMCGEDA PEIVQGFAVA LKARLTKADF 500
    DATVGIHPSA AEEFVTMRTP TRKIRKSESS EGKSGSQAKA AAGV 544
    Length:544
    Mass (Da):58,783
    Last modified:February 1, 1996 - v1
    Checksum:i7A71449EA21CE639
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11632 mRNA. Translation: AAA33962.1.
    PIRiT07155.
    RefSeqiNP_001238006.1. NM_001251077.1.
    UniGeneiGma.32269.

    Genome annotation databases

    GeneIDi547793.
    KEGGigmx:547793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11632 mRNA. Translation: AAA33962.1 .
    PIRi T07155.
    RefSeqi NP_001238006.1. NM_001251077.1.
    UniGenei Gma.32269.

    3D structure databases

    ProteinModelPortali P48640.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 547793.
    KEGGi gmx:547793.

    Phylogenomic databases

    KOi K00383.

    Gene expression databases

    Genevestigatori P48640.

    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. "Soybean root nodule cDNA encoding glutathione reductase."
      Tang X., Webb M.A.
      Plant Physiol. 104:1081-1082(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Root nodule.

    Entry informationi

    Entry nameiGSHRP_SOYBN
    AccessioniPrimary (citable) accession number: P48640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 104 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3