ID R9QAK3_JATCU Unreviewed; 212 AA.
AC R9QAK3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:AFD52631.1};
GN ORFNames=JCGZ_06589 {ECO:0000313|EMBL:KDP46078.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:AFD52631.1};
RN [1] {ECO:0000313|EMBL:AFD52631.1}
RP NUCLEOTIDE SEQUENCE.
RA Yu C., Tang J., Wang Y., Wei W., Chen F.;
RT "Molecular cloning and characterization of an Dehydroascorbate Reductase,
RT JcDHAR, from Jatropha curcas L.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDP46078.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP46078.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JF518880; AFD52631.1; -; mRNA.
DR EMBL; KK914220; KDP46078.1; -; Genomic_DNA.
DR RefSeq; NP_001295678.1; NM_001308749.1.
DR STRING; 180498.R9QAK3; -.
DR GeneID; 105634679; -.
DR KEGG; jcu:105634679; -.
DR OrthoDB; 103277at2759; -.
DR BRENDA; 1.8.5.1; 8977.
DR Proteomes; UP000027138; Unassembled WGS sequence.
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:SF2; GLUTATHIONE S-TRANSFERASE DHAR2-RELATED; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13417; GST_N_3; 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:AFD52631.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 10..88
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 66..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 212 AA; 23522 MW; F6921020E493C923 CRC64;
MALEICVKAA AGAPDVLGDC PFCQRVLLTL EEKKLTYKMH LINLSDKPQW FLEISPEGKV
PVAKIDDKWV PDSDVIVGIL EEKYPDPSLV TPPDFASVGS KIFSSFVKFL KSKDSNDESE
QALLEELKAL DEHLKAHGPF IAGEKISAVD LSLAPKLYHL DVALGHFKKW TVPENLTHFH
SYKKALFSLE SFQKTKASPE HVVAGWAPKV NA
//
