DHAR2_ORYSJ
ID DHAR2_ORYSJ Reviewed; 272 AA.
AC Q67UK9; B9FSC5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable glutathione S-transferase DHAR2, chloroplastic {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000305};
DE AltName: Full=GSH-dependent dehydroascorbate reductase 2 {ECO:0000305};
DE Short=OsDHAR2 {ECO:0000303|PubMed:20109239};
DE EC=1.8.5.1 {ECO:0000305};
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=DHAR2 {ECO:0000303|PubMed:20109239};
GN OrderedLocusNames=Os06g0232600 {ECO:0000312|EMBL:BAF19142.1},
GN LOC_Os06g12630 {ECO:0000305};
GN ORFNames=OsJ_20706 {ECO:0000312|EMBL:EEE65386.1},
GN P0479H10.23 {ECO:0000312|EMBL:BAD38160.1};
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
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 [6]
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 [7]
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).
CC -!- FUNCTION: Involved in ascorbate homeostasis. Maintains redox pools of
CC ascorbate by recycling dihydroascorbate (DHA) to ascorbate. Involved in
CC scavenging reactive oxygen species (ROS) under oxidative stresses.
CC {ECO:0000250|UniProtKB:Q65XA0}.
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:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q65XA0}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Down-regulated during senescence.
CC {ECO:0000269|PubMed:25546583}.
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
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DR EMBL; AP005522; BAD38160.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19142.1; -; Genomic_DNA.
DR EMBL; AK106013; BAG97507.1; -; mRNA.
DR EMBL; AP014962; BAS96927.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65386.1; -; Genomic_DNA.
DR RefSeq; XP_015641035.1; XM_015785549.1.
DR AlphaFoldDB; Q67UK9; -.
DR SMR; Q67UK9; -.
DR STRING; 4530.OS06T0232600-01; -.
DR PaxDb; Q67UK9; -.
DR PRIDE; Q67UK9; -.
DR EnsemblPlants; Os06t0232600-01; Os06t0232600-01; Os06g0232600.
DR GeneID; 4340581; -.
DR Gramene; Os06t0232600-01; Os06t0232600-01; Os06g0232600.
DR KEGG; osa:4340581; -.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR InParanoid; Q67UK9; -.
DR OMA; IHTCPED; -.
DR OrthoDB; 974249at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140547; P:acquisition of seed longevity; IEA:EnsemblPlants.
DR GO; GO:0033355; P:ascorbate glutathione cycle; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chloroplast; Detoxification; Oxidoreductase; Plastid; Reference proteome;
KW Stress response; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..272
FT /note="Probable glutathione S-transferase DHAR2,
FT chloroplastic"
FT /id="PRO_0000441987"
FT DOMAIN 70..148
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 126..272
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 68
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 79
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 79
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 107
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 120
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 133
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 219
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 266
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 269
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT CONFLICT 17
FT /note="G -> C (in Ref. 4; EEE65386)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="T -> K (in Ref. 4; EEE65386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29682 MW; BDA3E8836B403C51 CRC64;
MAVLLRTTTS ATTATSGGSS SATALLATTF RRGGRRLLLL PATRGSAPRR AALLTARASA
EPLEVCAKAS LTVPDRLGDC PFTQRVLLTI EEKHLPYDIK LVDLANKPDW FLKISPEGKV
PIVKLEEQWV ADSDVITQAI EEKYPEPSLA TPPEKASVGS KIFSTFIGFL KSKDPNDGTE
QALLSELTSF DSYLKDNGPF INGETISAAD LSLAPKLYHM EIALGHYKNW SVPDSLSHVK
KYMKTIFSMD SFVKTIALQE DVIAGWRPKV MG
