DHAR1_ORYSJ
ID DHAR1_ORYSJ Reviewed; 213 AA.
AC Q65XA0; Q84UH5; Q9MB31;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable glutathione S-transferase DHAR1, cytosolic {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000305};
DE AltName: Full=GSH-dependent dehydroascorbate reductase 1 {ECO:0000303|PubMed:10648822};
DE Short=OsDHAR1 {ECO:0000303|PubMed:20109239};
DE EC=1.8.5.1 {ECO:0000269|PubMed:19011360};
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase 1 {ECO:0000305};
GN Name=DHAR1 {ECO:0000303|PubMed:20109239};
GN Synonyms=DHAR {ECO:0000303|PubMed:12624189};
GN OrderedLocusNames=Os05g0116100 {ECO:0000312|EMBL:BAF16384.1},
GN LOC_Os05g02530 {ECO:0000305};
GN ORFNames=OJ1654_B10.18 {ECO:0000312|EMBL:AAU44087.1},
GN P0496H07.8 {ECO:0000312|EMBL:AAV44199.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-15; 84-100 AND 128-147,
RP AND INDUCTION BY HEAT SHOCK.
RC STRAIN=cv. Nipponbare;
RX PubMed=10648822; DOI=10.1016/s0014-5793(99)01768-8;
RA Urano J., Nakagawa T., Maki Y., Masumura T., Tanaka K., Murata N.,
RA Ushimaru T.;
RT "Molecular cloning and characterization of a rice dehydroascorbate
RT reductase.";
RL FEBS Lett. 466:107-111(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12624189; DOI=10.1073/pnas.0635176100;
RA Chen Z., Young T.E., Ling J., Chang S.C., Gallie D.R.;
RT "Increasing vitamin C content of plants through enhanced ascorbate
RT recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3525-3530(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19011360;
RA Shin S.Y., Kim I.S., Kim Y.H., Park H.M., Lee J.Y., Kang H.G., Yoon H.S.;
RT "Scavenging reactive oxygen species by rice dehydroascorbate reductase
RT alleviates oxidative stresses in Escherichia coli.";
RL Mol. Cells 26:616-620(2008).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20109239; DOI=10.1186/1471-2164-11-73;
RA Jain M., Ghanashyam C., Bhattacharjee A.;
RT "Comprehensive expression analysis suggests overlapping and specific roles
RT of rice glutathione S-transferase genes during development and stress
RT responses.";
RL BMC Genomics 11:73-73(2010).
RN [10]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=23519921; DOI=10.1007/s00425-013-1862-8;
RA Kim Y.S., Kim I.S., Bae M.J., Choe Y.H., Kim Y.H., Park H.M., Kang H.G.,
RA Yoon H.S.;
RT "Homologous expression of cytosolic dehydroascorbate reductase increases
RT grain yield and biomass under paddy field conditions in transgenic rice
RT (Oryza sativa L. japonica).";
RL Planta 237:1613-1625(2013).
RN [11]
RP INDUCTION.
RX PubMed=25546583; DOI=10.1016/j.jplph.2014.09.020;
RA Li Z., Su D., Lei B., Wang F., Geng W., Pan G., Cheng F.;
RT "Transcriptional profile of genes involved in ascorbate glutathione cycle
RT in senescing leaves for an early senescence leaf (esl) rice mutant.";
RL J. Plant Physiol. 176:1-15(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH ASCORBATE AND
RP GLUTATHIONE, FUNCTION, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF LYS-8;
RP CYS-20 AND LYS-47.
RX PubMed=26775680; DOI=10.1038/srep19498;
RA Do H., Kim I.S., Jeon B.W., Lee C.W., Park A.K., Wi A.R., Shin S.C.,
RA Park H., Kim Y.S., Yoon H.S., Kim H.W., Lee J.H.;
RT "Structural understanding of the recycling of oxidized ascorbate by
RT dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica.";
RL Sci. Rep. 6:19498-19498(2016).
CC -!- FUNCTION: Involved in ascorbate homeostasis. Maintains redox pools of
CC ascorbate by recycling dihydroascorbate (DHA) to ascorbate (Probable).
CC Involved in scavenging reactive oxygen species (ROS) under oxidative
CC stresses. Possesses dehydroascorbate reductase (DHAR) activity in vitro
CC (PubMed:19011360). May function via a ping-pong reaction mechanism with
CC an electron transfer at the active site (PubMed:26775680). Possesses
CC chaperone-like activity in vitro (PubMed:26775680).
CC {ECO:0000269|PubMed:19011360, ECO:0000269|PubMed:26775680,
CC ECO:0000305|PubMed:23519921}.
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; Evidence={ECO:0000305};
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:19011360};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26775680}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- INDUCTION: Induced by heat shock (PubMed:10648822). Down-regulated
CC during senescence (PubMed:25546583). {ECO:0000269|PubMed:10648822,
CC ECO:0000269|PubMed:25546583}.
CC -!- BIOTECHNOLOGY: Overexpression of DHAR1 improve ascorbate pool and redox
CC homeostasis, and enhances grain yield and biomass in paddy field
CC conditions. {ECO:0000269|PubMed:23519921}.
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
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DR EMBL; AB037970; BAA90672.1; -; mRNA.
DR EMBL; AY074786; AAL71856.1; -; mRNA.
DR EMBL; AC108504; AAU44087.1; -; Genomic_DNA.
DR EMBL; AC078977; AAV44199.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16384.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS91971.1; -; Genomic_DNA.
DR EMBL; AK061836; BAG88138.1; -; mRNA.
DR EMBL; AK070895; BAG92197.1; -; mRNA.
DR PDB; 5D9T; X-ray; 1.90 A; A=1-213.
DR PDB; 5D9V; X-ray; 1.69 A; A=1-213.
DR PDB; 5D9W; X-ray; 1.69 A; A=1-213.
DR PDB; 5D9X; X-ray; 1.68 A; A=1-213.
DR PDBsum; 5D9T; -.
DR PDBsum; 5D9V; -.
DR PDBsum; 5D9W; -.
DR PDBsum; 5D9X; -.
DR AlphaFoldDB; Q65XA0; -.
DR SMR; Q65XA0; -.
DR STRING; 4530.OS05T0116100-01; -.
DR PaxDb; Q65XA0; -.
DR PRIDE; Q65XA0; -.
DR EnsemblPlants; Os05t0116100-01; Os05t0116100-01; Os05g0116100.
DR Gramene; Os05t0116100-01; Os05t0116100-01; Os05g0116100.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR InParanoid; Q65XA0; -.
DR OMA; CHQIFMI; -.
DR BRENDA; 1.8.5.1; 8948.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033355; P:ascorbate glutathione cycle; IDA:UniProtKB.
DR GO; GO:0098869; P:cellular oxidant detoxification; IDA:UniProtKB.
DR GO; GO:0010731; P:protein glutathionylation; IBA:GO_Central.
DR InterPro; IPR044627; DHAR1/2/3/4.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
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 3D-structure; Cytoplasm; Detoxification; Direct protein sequencing;
KW Oxidoreductase; Reference proteome; Stress response; Transferase.
FT CHAIN 1..213
FT /note="Probable glutathione S-transferase DHAR1, cytosolic"
FT /id="PRO_0000441986"
FT DOMAIN 10..89
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 73..213
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:26775680"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9X"
FT BINDING 8
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9W"
FT BINDING 19
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9X"
FT BINDING 19
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9W"
FT BINDING 47
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 74
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 160
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9X"
FT BINDING 207
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9X"
FT BINDING 210
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:26775680,
FT ECO:0007744|PDB:5D9W"
FT MUTAGEN 8
FT /note="K->A: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:26775680"
FT MUTAGEN 20
FT /note="C->A,S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26775680"
FT MUTAGEN 47
FT /note="K->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:26775680"
FT CONFLICT 47
FT /note="K -> N (in Ref. 1; BAA90672)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5D9W"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5D9X"
FT TURN 97..102
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:5D9X"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5D9W"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5D9X"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:5D9X"
SQ SEQUENCE 213 AA; 23570 MW; A15733211C901E39 CRC64;
MGVEVCVKAA VGHPDTLGDC PFSQRVLLTL EEKKVPYEMK LIDVQNKPDW FLKISPEGKV
PVFNGGDGKW IPDSDVITQV IEEKYPTPSL VTPPEYASVG SKIFSCFTTF LKSKDPNDGS
EKALLTELQA LEEHLKAHGP FINGQNISAA DLSLAPKLYH LQVALEHFKG WKIPEDLTNV
HAYTEALFSR ESFIKTKAAK EHLIAGWAPK VNA
