ID   DHAR3_ARATH             Reviewed;         258 AA.
AC   Q8LE52; Q67XJ9; Q680W2; Q8VZA3; Q9FE30; Q9LFE6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Glutathione S-transferase DHAR3, chloroplastic;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:12077129};
DE   AltName: Full=Chloride intracellular channel homolog 3;
DE            Short=CLIC homolog 3;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase 3 {ECO:0000303|PubMed:12077129};
DE            Short=AtDHAR3 {ECO:0000303|PubMed:12077129};
DE            Short=ChlDHAR;
DE            Short=GSH-dependent dehydroascorbate reductase 3;
DE            EC=1.8.5.1 {ECO:0000269|PubMed:12077129};
DE   Flags: Precursor;
GN   Name=DHAR3; OrderedLocusNames=At5g16710; ORFNames=F5E19.50;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-258.
RC   STRAIN=cv. Columbia;
RX   PubMed=11148269; DOI=10.1093/pcp/pcd035;
RA   Shimaoka T., Yokota A., Miyake C.;
RT   "Purification and characterization of chloroplast dehydroascorbate
RT   reductase from spinach leaves.";
RL   Plant Cell Physiol. 41:1110-1118(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-258.
RA   Creissen G.;
RT   "Cloning of a chloroplast dehydroascorbate reductase from Arabidopsis
RT   thaliana.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   GENE FAMILY, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND GLUTATHIONYLATION AT CYS-52.
RX   PubMed=12077129; DOI=10.1074/jbc.m202919200;
RA   Dixon D.P., Davis B.G., Edwards R.;
RT   "Functional divergence in the glutathione transferase superfamily in
RT   plants. Identification of two classes with putative functions in redox
RT   homeostasis in Arabidopsis thaliana.";
RL   J. Biol. Chem. 277:30859-30869(2002).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH TRX3.
RX   PubMed=15352244; DOI=10.1002/pmic.200400805;
RA   Marchand C., Le Marechal P., Meyer Y., Miginiac-Maslow M.,
RA   Issakidis-Bourguet E., Decottignies P.;
RT   "New targets of Arabidopsis thioredoxins revealed by proteomic analysis.";
RL   Proteomics 4:2696-2706(2004).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA   van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT   proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19174456; DOI=10.1093/jxb/ern365;
RA   Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT   "Enzyme activities and subcellular localization of members of the
RT   Arabidopsis glutathione transferase superfamily.";
RL   J. Exp. Bot. 60:1207-1218(2009).
CC   -!- FUNCTION: Displays a dual function. As a soluble protein, exhibits
CC       glutathione-dependent thiol transferase and dehydroascorbate (DHA)
CC       reductase activities (PubMed:12077129). Key component of the ascorbate
CC       recycling system. Involved in the redox homeostasis, especially in
CC       scavenging of ROS under oxidative stresses (By similarity).
CC       {ECO:0000250|UniProtKB:Q9FWR4, ECO:0000269|PubMed:12077129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:12077129};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000269|PubMed:12077129};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for DHA (at pH 6.5 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:12077129};
CC         KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:12077129};
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with TRX3.
CC       {ECO:0000250|UniProtKB:Q9FWR4, ECO:0000269|PubMed:15352244}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:19174456}.
CC   -!- PTM: Partial S-glutathionylation and intramolecular disulfide bond
CC       formation between Cys-66 and Cys-69 in the presence of oxidized
CC       glutathione (GSSG). Could be reduced by TRX-dependent process.
CC       {ECO:0000269|PubMed:12077129}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01835.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At5g16710 and At5g16715.; Evidence={ECO:0000305};
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DR   EMBL; AL391147; CAC01835.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92328.1; -; Genomic_DNA.
DR   EMBL; AK118603; BAC43202.1; -; mRNA.
DR   EMBL; AY065124; AAL38300.1; -; mRNA.
DR   EMBL; BT001185; AAN65072.1; -; mRNA.
DR   EMBL; AK175537; BAD43300.1; -; mRNA.
DR   EMBL; AK175755; BAD43518.1; -; mRNA.
DR   EMBL; AK175798; BAD43561.1; -; mRNA.
DR   EMBL; AK176039; BAD43802.1; -; mRNA.
DR   EMBL; AK176071; BAD43834.1; -; mRNA.
DR   EMBL; AK176708; BAD44471.1; -; mRNA.
DR   EMBL; AK176820; BAD44583.1; -; mRNA.
DR   EMBL; AK176870; BAD44633.1; -; mRNA.
DR   EMBL; AY085616; AAM62837.1; -; mRNA.
DR   EMBL; AF195887; AAG24946.1; -; mRNA.
DR   EMBL; AF301597; AAG40196.1; -; mRNA.
DR   PIR; T51503; T51503.
DR   RefSeq; NP_568336.1; NM_121676.4.
DR   AlphaFoldDB; Q8LE52; -.
DR   SMR; Q8LE52; -.
DR   BioGRID; 16808; 1.
DR   IntAct; Q8LE52; 1.
DR   STRING; 3702.Q8LE52; -.
DR   iPTMnet; Q8LE52; -.
DR   MetOSite; Q8LE52; -.
DR   PaxDb; 3702-AT5G16710-1; -.
DR   ProteomicsDB; 224057; -.
DR   EnsemblPlants; AT5G16710.1; AT5G16710.1; AT5G16710.
DR   GeneID; 831532; -.
DR   Gramene; AT5G16710.1; AT5G16710.1; AT5G16710.
DR   KEGG; ath:AT5G16710; -.
DR   Araport; AT5G16710; -.
DR   TAIR; AT5G16710; DHAR3.
DR   eggNOG; KOG1422; Eukaryota.
DR   HOGENOM; CLU_011226_1_0_1; -.
DR   InParanoid; Q8LE52; -.
DR   OMA; SYMKSIF; -.
DR   OrthoDB; 103277at2759; -.
DR   PhylomeDB; Q8LE52; -.
DR   BioCyc; ARA:AT5G16710-MONOMER; -.
DR   SABIO-RK; Q8LE52; -.
DR   PRO; PR:Q8LE52; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LE52; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140547; P:acquisition of seed longevity; IGI:TAIR.
DR   GO; GO:0033355; P:ascorbate glutathione cycle; IEA:InterPro.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IGI:TAIR.
DR   GO; GO:0010731; P:protein glutathionylation; IDA:TAIR.
DR   CDD; cd03201; GST_C_DHAR; 1.
DR   CDD; cd00570; GST_N_family; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR044627; DHAR1/2/3/4.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44420; GLUTATHIONE S-TRANSFERASE DHAR2-RELATED; 1.
DR   PANTHER; PTHR44420:SF1; GLUTATHIONE S-TRANSFERASE DHAR3, CHLOROPLASTIC; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; Q8LE52; AT.
PE   1: Evidence at protein level;
KW   Chloroplast; Detoxification; Disulfide bond; Glutathionylation;
KW   Oxidoreductase; Plastid; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..258
FT                   /note="Glutathione S-transferase DHAR3, chloroplastic"
FT                   /id="PRO_0000395483"
FT   DOMAIN          56..129
FT                   /note="GST N-terminal"
FT   DOMAIN          130..258
FT                   /note="GST C-terminal"
FT   MOTIF           66..71
FT                   /note="Glutathione-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         54
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         65
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         65
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         93
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT   BINDING         106
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT   BINDING         119
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT   BINDING         205
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         252
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   BINDING         255
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT   MOD_RES         52
FT                   /note="S-glutathionyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:12077129"
FT   DISULFID        66..69
FT                   /note="In soluble form"
FT   CONFLICT        65
FT                   /note="D -> Y (in Ref. 4; AAL38300/AAN65072)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="N -> D (in Ref. 5; BAD43518)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  28514 MW;  35AC1A8EFDD3E77C CRC64;
     MISLRFQPST TAGVLSASVS RAGFIKRCGS TKPGRVGRFV TMATAASPLE ICVKASITTP
     NKLGDCPFCQ KVLLTMEEKN VPYDMKMVDL SNKPEWFLKI SPEGKVPVVK FDEKWVPDSD
     VITQALEEKY PEPPLATPPE KASVGSKIFS TFVGFLKSKD SGDGTEQVLL DELTTFNDYI
     KDNGPFINGE KISAADLSLA PKLYHMKIAL GHYKNWSVPD SLPFVKSYME NVFSRESFTN
     TRAETEDVIA GWRPKVMG
//