ID A0A0E0A767_9ORYZ Unreviewed; 283 AA.
AC A0A0E0A767;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G08970.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G08970.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G08970.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00000509};
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family.
CC {ECO:0000256|ARBA:ARBA00024194}.
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DR AlphaFoldDB; A0A0E0A767; -.
DR STRING; 40148.A0A0E0A767; -.
DR EnsemblPlants; OGLUM06G08970.1; OGLUM06G08970.1; OGLUM06G08970.
DR Gramene; OGLUM06G08970.1; OGLUM06G08970.1; OGLUM06G08970.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-EC.
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 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; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT DOMAIN 70..148
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 152..283
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 283 AA; 30947 MW; 9C5E8DDF2F1E9025 CRC64;
MAVLLRTTTS ATTATSGGSS SATALLATTF RRGGRRLLLL PATRGSAPRR AALLTVRASA
EPLEVCAKAS LTVPDRLGDC PFTQRVLLTI EEKHLPYDIK LVDLANKPDW FLKISPEGKV
PIVKLEEQWV ADSDVITQAI EEKYPEPSLA TPPEKASVIL TIGNNFLYSG SKIFSTFIGF
LKSKDPNDGT EQALLSELTS FDSYLKDNGP FINGETISAA DLSLAPKLYH MEIALGHYKN
WSVPDSLSHV KKYMKTIFSM DSFVKTIALQ EDVIAGWRPK VMG
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