ID H6S166_THECC Unreviewed; 212 AA.
AC H6S166;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
GN ORFNames=TCM_042968 {ECO:0000313|EMBL:EOY18362.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:ADW84692.1};
RN [1] {ECO:0000313|EMBL:ADW84692.1}
RP NUCLEOTIDE SEQUENCE.
RA Dias C.V., Mendes J.S., Carvalho A., Pirovani C.P., Gesteira A.S.,
RA Micheli F., Gramacho K.P., Hammerstone J., Mazzafera P., Cascardo J.C.M.;
RT "A dual role for calcium oxalate in Theobroma cacao tissues infected by the
RT hemibiotrophic fungus Moniliophthora perniciosa.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EOY18362.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; GU570573; ADW84692.1; -; mRNA.
DR EMBL; CM001888; EOY18362.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY18363.1; -; Genomic_DNA.
DR AlphaFoldDB; H6S166; -.
DR STRING; 3641.H6S166; -.
DR EnsemblPlants; EOY18362; EOY18362; TCM_042968.
DR EnsemblPlants; EOY18363; EOY18363; TCM_042968.
DR Gramene; EOY18362; EOY18362; TCM_042968.
DR Gramene; EOY18363; EOY18363; TCM_042968.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR InParanoid; H6S166; -.
DR OMA; TYVHNYM; -.
DR Proteomes; UP000026915; Chromosome 10.
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: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:SF2; GLUTATHIONE S-TRANSFERASE DHAR2-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; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000313|EMBL:ADW84692.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 10..88
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
SQ SEQUENCE 212 AA; 23482 MW; 42CC26BCAC15C11A CRC64;
MALEICVKAA AGAPDVLGDC PFCQRVVLTL EEKKVPYKMH LVNLSDKPRW FLEISPEGKV
PVVKFDDKWV PDSDVIVGIL EEKYPEPSLK TPPEFASVGS KIFGTFITFL KSRDANDGSE
QALLNELKAL DEHLKGQGPF IAGEKITAID LSLGPKLYHL EIALGHFKKW TIPESLTCVH
GYLKLIFSQE SFVKTSVAKE FVITGWAPKV NA
//
