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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei66 – 661By similarity

    GO - Molecular functioni

    GO - Biological processi

    • oxidation-reduction process Source: GOC
    • protein glutathionylation Source: TAIR
    • response to cytokinin Source: TAIR
    • response to toxic substance Source: UniProtKB-KW
    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
    ProteomesiUP000006548 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)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4242ChloroplastSequence AnalysisAdd
    BLAST
    Chaini43 – 258216Glutathione S-transferase DHAR3, chloroplasticPRO_0000395483Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521S-glutathionyl cysteine1 Publication
    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.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiQ8LE52. 1 interaction.
    STRINGi3702.AT5G16710.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8LE52.
    SMRiQ8LE52. Positions 64-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 12974GST N-terminalAdd
    BLAST
    Domaini130 – 258129GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 672Glutathione bindingBy similarity
    Regioni92 – 932Glutathione bindingBy similarity
    Regioni105 – 1062Glutathione bindingBy similarity
    Regioni118 – 1192Glutathione bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi66 – 716Glutathione-bindingSequence Analysis

    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

    eggNOGiCOG0625.
    HOGENOMiHOG000272670.
    InParanoidiQ8LE52.
    OMAiHLPYDMK.
    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 CAC01835.1 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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651D → Y in AAL38300 (PubMed:14593172).Curated
    Sequence conflicti65 – 651D → Y in AAN65072 (PubMed:14593172).Curated
    Sequence conflicti231 – 2311N → D in BAD43518 (Ref. 5) Curated

    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_121676.3.
    UniGeneiAt.16881.

    Genome annotation databases

    EnsemblPlantsiAT5G16710.1; AT5G16710.1; AT5G16710.
    GeneIDi831532.
    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_121676.3.
    UniGeneiAt.16881.

    3D structure databases

    ProteinModelPortaliQ8LE52.
    SMRiQ8LE52. Positions 64-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8LE52. 1 interaction.
    STRINGi3702.AT5G16710.1.

    Proteomic databases

    PaxDbiQ8LE52.
    PRIDEiQ8LE52.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT5G16710.

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000272670.
    InParanoidiQ8LE52.
    OMAiHLPYDMK.
    PhylomeDBiQ8LE52.

    Enzyme and pathway databases

    BioCyciARA:AT5G16710-MONOMER.
    SABIO-RKQ8LE52.

    Miscellaneous databases

    PROiQ8LE52.

    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      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.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Purification and characterization of chloroplast dehydroascorbate reductase from spinach leaves."
      Shimaoka T., Yokota A., Miyake C.
      Plant Cell Physiol. 41:1110-1118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-258.
      Strain: cv. Columbia.
    8. "Cloning of a chloroplast dehydroascorbate reductase from Arabidopsis thaliana."
      Creissen G.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-258.
    9. "Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana."
      Dixon D.P., Davis B.G., Edwards R.
      J. Biol. Chem. 277:30859-30869(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, GLUTATHIONYLATION AT CYS-52.
    10. "Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
      Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
      J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
      Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
      Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TRX3.
    13. Cited for: SUBCELLULAR LOCATION.
    14. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
      Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
      PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
      Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
      J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    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: June 24, 2015
    This is version 105 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

    External Data

    Dasty 3

    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 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.