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Database: UniProt
Entry: Q0ZNW5_MALDO
LinkDB: Q0ZNW5_MALDO
Original site: Q0ZNW5_MALDO 
ID   Q0ZNW5_MALDO            Unreviewed;       213 AA.
AC   Q0ZNW5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE            EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
GN   Name=DHAR {ECO:0000313|EMBL:ABG49123.1};
GN   ORFNames=DVH24_023159 {ECO:0000313|EMBL:RXI09015.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:ABG49123.1};
RN   [1] {ECO:0000313|EMBL:ABG49123.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ma F.W., Zhang Y.Z., Zhang J.K., Liang D.;
RT   "Molecular cloning of glutathione-dependent dehydroascorbate reductase gene
RT   of Royal Gala.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RXI09015.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXI09015.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; DQ322706; ABG49123.1; -; mRNA.
DR   EMBL; RDQH01000327; RXI09015.1; -; Genomic_DNA.
DR   RefSeq; NP_001281055.1; NM_001294126.1.
DR   AlphaFoldDB; Q0ZNW5; -.
DR   STRING; 3750.Q0ZNW5; -.
DR   EnsemblPlants; mRNA:MD01G0094700; mRNA:MD01G0094700; MD01G0094700.
DR   GeneID; 103433463; -.
DR   Gramene; mRNA:MD01G0094700; mRNA:MD01G0094700; MD01G0094700.
DR   KEGG; mdm:103433463; -.
DR   OrthoDB; 103277at2759; -.
DR   Proteomes; UP000290289; Chromosome 1.
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: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:SF6; REDUCTASE, PUTATIVE-RELATED; 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   2: Evidence at transcript level;
KW   Oxidoreductase {ECO:0000313|EMBL:ABG49123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          10..88
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          66..213
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   213 AA;  23520 MW;  6CC6CBD1D464E0DE CRC64;
     MALEVAAKAA AGAPDLLGDC PFCQRVTLTL EEKKVPYKLH LINLSDKPKW FTEVNPEGKV
     PVVKFDDKWV PDSDVIVGII EEKYPEPSLK TPPEFASVGS KILGSFVTFL KSKDPGDGSE
     QALLTELKAL DEHLKAHGPY IAGEKVTAAD LSLAPKLYHL KVALGHFKKW TVPADLAHYH
     KYTELLFSRE SFVKTAPADE KYVIAGWEPK VNP
//
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