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Protein

Glutathione S-transferase DHAR3, chloroplastic

Gene

DHAR3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Kineticsi

  1. KM=0.50 mM for DHA (at pH 6.5 and 30 degrees Celsius)1 Publication
  2. KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei66By similarity1

    GO - Molecular functioni

    GO - Biological processi

    • glutathione metabolic process Source: GO_Central
    • protein glutathionylation Source: TAIR
    • response to cytokinin Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Detoxification

    Enzyme and pathway databases

    BioCyciARA:AT5G16710-MONOMER.
    SABIO-RKQ8LE52.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase DHAR3, chloroplastic (EC:2.5.1.18)
    Alternative name(s):
    Chloride intracellular channel homolog 3
    Short name:
    CLIC homolog 3
    Glutathione-dependent dehydroascorbate reductase 3
    Short name:
    AtDHAR3
    Short name:
    ChlDHAR
    Short name:
    GSH-dependent dehydroascorbate reductase 3
    Gene namesi
    Name:DHAR3
    Ordered Locus Names:At5g16710
    ORF Names:F5E19.50
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G16710.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast envelope Source: TAIR
    • chloroplast stroma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 42ChloroplastSequence analysisAdd BLAST42
    ChainiPRO_000039548343 – 258Glutathione S-transferase DHAR3, chloroplasticAdd BLAST216

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei52S-glutathionyl cysteine1 Publication1
    Disulfide bondi66 ↔ 69In soluble form

    Post-translational modificationi

    Partial S-glutathionylation and intramolecular disulfide bond formation between Cys-66 and Cys-69 in the presence of oxidized glutathione (GSSG). Could be reduced by TRX-dependent process.1 Publication

    Keywords - PTMi

    Disulfide bond, Glutathionylation

    Proteomic databases

    PaxDbiQ8LE52.
    PRIDEiQ8LE52.

    PTM databases

    iPTMnetiQ8LE52.

    Expressioni

    Gene expression databases

    GenevisibleiQ8LE52. AT.

    Interactioni

    Subunit structurei

    Monomer (By similarity). Interacts with TRX3.By similarity1 Publication

    Protein-protein interaction databases

    IntActiQ8LE52. 1 interactor.
    STRINGi3702.AT5G16710.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8LE52.
    SMRiQ8LE52.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini56 – 129GST N-terminalAdd BLAST74
    Domaini130 – 258GST C-terminalAdd BLAST129

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni66 – 67Glutathione bindingBy similarity2
    Regioni92 – 93Glutathione bindingBy similarity2
    Regioni105 – 106Glutathione bindingBy similarity2
    Regioni118 – 119Glutathione bindingBy similarity2

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi66 – 71Glutathione-bindingSequence analysis6

    Sequence similaritiesi

    Belongs to the GST superfamily. DHAR family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410INGY. Eukaryota.
    ENOG4110FKA. LUCA.
    HOGENOMiHOG000272670.
    InParanoidiQ8LE52.
    OMAiSYMKSIF.
    OrthoDBiEOG09360IQR.
    PhylomeDBiQ8LE52.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8LE52-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MISLRFQPST TAGVLSASVS RAGFIKRCGS TKPGRVGRFV TMATAASPLE
    60 70 80 90 100
    ICVKASITTP NKLGDCPFCQ KVLLTMEEKN VPYDMKMVDL SNKPEWFLKI
    110 120 130 140 150
    SPEGKVPVVK FDEKWVPDSD VITQALEEKY PEPPLATPPE KASVGSKIFS
    160 170 180 190 200
    TFVGFLKSKD SGDGTEQVLL DELTTFNDYI KDNGPFINGE KISAADLSLA
    210 220 230 240 250
    PKLYHMKIAL GHYKNWSVPD SLPFVKSYME NVFSRESFTN TRAETEDVIA

    GWRPKVMG
    Length:258
    Mass (Da):28,514
    Last modified:October 1, 2002 - v1
    Checksum:i35AC1A8EFDD3E77C
    GO

    Sequence cautioni

    The sequence CAC01835 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At5g16710 and At5g16715.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti65D → Y in AAL38300 (PubMed:14593172).Curated1
    Sequence conflicti65D → Y in AAN65072 (PubMed:14593172).Curated1
    Sequence conflicti231N → D in BAD43518 (Ref. 5) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL391147 Genomic DNA. Translation: CAC01835.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED92328.1.
    AK118603 mRNA. Translation: BAC43202.1.
    AY065124 mRNA. Translation: AAL38300.1.
    BT001185 mRNA. Translation: AAN65072.1.
    AK175537 mRNA. Translation: BAD43300.1.
    AK175755 mRNA. Translation: BAD43518.1.
    AK175798 mRNA. Translation: BAD43561.1.
    AK176039 mRNA. Translation: BAD43802.1.
    AK176071 mRNA. Translation: BAD43834.1.
    AK176708 mRNA. Translation: BAD44471.1.
    AK176820 mRNA. Translation: BAD44583.1.
    AK176870 mRNA. Translation: BAD44633.1.
    AY085616 mRNA. Translation: AAM62837.1.
    AF195887 mRNA. Translation: AAG24946.1.
    AF301597 mRNA. Translation: AAG40196.1.
    PIRiT51503.
    RefSeqiNP_568336.1. NM_121676.4.
    UniGeneiAt.16881.

    Genome annotation databases

    EnsemblPlantsiAT5G16710.1; AT5G16710.1; AT5G16710.
    GeneIDi831532.
    GrameneiAT5G16710.1; AT5G16710.1; AT5G16710.
    KEGGiath:AT5G16710.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL391147 Genomic DNA. Translation: CAC01835.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED92328.1.
    AK118603 mRNA. Translation: BAC43202.1.
    AY065124 mRNA. Translation: AAL38300.1.
    BT001185 mRNA. Translation: AAN65072.1.
    AK175537 mRNA. Translation: BAD43300.1.
    AK175755 mRNA. Translation: BAD43518.1.
    AK175798 mRNA. Translation: BAD43561.1.
    AK176039 mRNA. Translation: BAD43802.1.
    AK176071 mRNA. Translation: BAD43834.1.
    AK176708 mRNA. Translation: BAD44471.1.
    AK176820 mRNA. Translation: BAD44583.1.
    AK176870 mRNA. Translation: BAD44633.1.
    AY085616 mRNA. Translation: AAM62837.1.
    AF195887 mRNA. Translation: AAG24946.1.
    AF301597 mRNA. Translation: AAG40196.1.
    PIRiT51503.
    RefSeqiNP_568336.1. NM_121676.4.
    UniGeneiAt.16881.

    3D structure databases

    ProteinModelPortaliQ8LE52.
    SMRiQ8LE52.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8LE52. 1 interactor.
    STRINGi3702.AT5G16710.1.

    PTM databases

    iPTMnetiQ8LE52.

    Proteomic databases

    PaxDbiQ8LE52.
    PRIDEiQ8LE52.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G16710.1; AT5G16710.1; AT5G16710.
    GeneIDi831532.
    GrameneiAT5G16710.1; AT5G16710.1; AT5G16710.
    KEGGiath:AT5G16710.

    Organism-specific databases

    TAIRiAT5G16710.

    Phylogenomic databases

    eggNOGiENOG410INGY. Eukaryota.
    ENOG4110FKA. LUCA.
    HOGENOMiHOG000272670.
    InParanoidiQ8LE52.
    OMAiSYMKSIF.
    OrthoDBiEOG09360IQR.
    PhylomeDBiQ8LE52.

    Enzyme and pathway databases

    BioCyciARA:AT5G16710-MONOMER.
    SABIO-RKQ8LE52.

    Miscellaneous databases

    PROiQ8LE52.

    Gene expression databases

    GenevisibleiQ8LE52. AT.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHAR3_ARATH
    AccessioniPrimary (citable) accession number: Q8LE52
    Secondary accession number(s): Q67XJ9
    , Q680W2, Q8VZA3, Q9FE30, Q9LFE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: October 1, 2002
    Last modified: November 30, 2016
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.