ID Q4VDN7_SOLLC Unreviewed; 268 AA.
AC Q4VDN7;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
GN Name=DHAR2 {ECO:0000313|EMBL:AAY47049.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EMBL:AAY47049.1};
RN [1] {ECO:0000313|EMBL:AAY47049.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AAY47049.1};
RX AGRICOLA=IND43764163;
RA Zou L., Li H., Ouyang B., Zhang J., Ye Z.;
RT "Cloning and mapping of genes involved in tomato ascorbic acid biosynthesis
RT and metabolism.";
RL Plant Sci. 170:120-127(2006).
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; AY971874; AAY47049.1; -; mRNA.
DR AlphaFoldDB; Q4VDN7; -.
DR SMR; Q4VDN7; -.
DR BRENDA; 1.8.5.1; 3101.
DR ExpressionAtlas; Q4VDN7; baseline and differential.
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; 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; 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; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000313|EMBL:AAY47049.1}.
FT DOMAIN 66..144
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
SQ SEQUENCE 268 AA; 29932 MW; 98AA8A5B38E20A10 CRC64;
MSTAKITPSA ASFATSIKHL AGIQLPRRQS TIFTSNSTKF RAPRRGFTVS MAASIETPLE
VCVKQSITTP NKLGDCPFTQ RVLLTLEEKH LPYDMKFVDL SNKPDWFLKI SPEGKVPLIK
LDEKWVPDSD VISQALEEKF PKPPLTTPPE KASVGSKIFP KFVAFLKSKD SGDGTEQALL
DELTAFNDYL KENGPFINGN EVSAADLSLG PKLYHLEIAL GNYKNWSIPD SLSYMKSYMK
SIFSRESFIH TRALKEDVIE GWRPKVMG
//
