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Database: UniProt
Entry: D8SEW2_SELML
LinkDB: D8SEW2_SELML
Original site: D8SEW2_SELML 
ID   D8SEW2_SELML            Unreviewed;       193 AA.
AC   D8SEW2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE            EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
GN   ORFNames=SELMODRAFT_233824 {ECO:0000313|EMBL:EFJ16939.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ16939.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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; GL377616; EFJ16939.1; -; Genomic_DNA.
DR   RefSeq; XP_002981846.1; XM_002981800.1.
DR   AlphaFoldDB; D8SEW2; -.
DR   STRING; 88036.D8SEW2; -.
DR   EnsemblPlants; EFJ16939; EFJ16939; SELMODRAFT_233824.
DR   Gramene; EFJ16939; EFJ16939; SELMODRAFT_233824.
DR   KEGG; smo:SELMODRAFT_233824; -.
DR   eggNOG; KOG1422; Eukaryota.
DR   HOGENOM; CLU_011226_1_1_1; -.
DR   InParanoid; D8SEW2; -.
DR   Proteomes; UP000001514; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44420:SF5; GLUTATHIONE DEHYDROGENASE (ASCORBATE); 1.
DR   PANTHER; PTHR44420; GLUTATHIONE S-TRANSFERASE DHAR2-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 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:UP000001514}.
FT   DOMAIN          1..62
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          41..186
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   193 AA;  22382 MW;  0783FDBBA99504A6 CRC64;
     MELEEKRLPY KATYIQEGPD KPAWFMEKNP SGLMPVLRDG SEWIQDSERI FEHLEAKFPN
     PALKTPDEFK DVGSGIFPRF VEWLKSKDQA HPAKQDLIKE LLSFNQHLQK HGPYIAGEKP
     TDSDFTVAPK LRHARVALGQ IMGFAFPEKL EALHKYIELM EARPSFIHTD SPDEMIICGW
     RKKFSLPEKL DYE
//
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