DHAR3_ARATH
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 03-AUG-2022, entry version 144.
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=0.50 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.AT5G16710.1; -.
DR iPTMnet; Q8LE52; -.
DR MetOSite; Q8LE52; -.
DR PaxDb; Q8LE52; -.
DR PRIDE; Q8LE52; -.
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; locus:2149015; AT5G16710.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR InParanoid; Q8LE52; -.
DR OMA; IHTCPED; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q8LE52; -.
DR BioCyc; ARA:AT5G16710-MON; -.
DR SABIO-RK; Q8LE52; -.
DR PRO; PR:Q8LE52; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LE52; baseline and differential.
DR Genevisible; Q8LE52; AT.
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 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; PTHR44420; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
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
