ID A0A022QZU0_ERYGU Unreviewed; 212 AA.
AC A0A022QZU0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
GN ORFNames=MIMGU_mgv1a013716mg {ECO:0000313|EMBL:EYU33189.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU33189.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU33189.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(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; KI630787; EYU33189.1; -; Genomic_DNA.
DR RefSeq; XP_012842503.1; XM_012987049.1.
DR AlphaFoldDB; A0A022QZU0; -.
DR STRING; 4155.A0A022QZU0; -.
DR GeneID; 105962725; -.
DR KEGG; egt:105962725; -.
DR eggNOG; KOG1422; Eukaryota.
DR OMA; CHQIFMI; -.
DR OrthoDB; 103277at2759; -.
DR PhylomeDB; A0A022QZU0; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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; 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; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
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; 23576 MW; FEBA7F3EC75D10D5 CRC64;
MAVEICVKAA AGAPDILGDC PFSQRVQLTL EEKKVHYKLH LINTDDKPQW FLEVNPEGKV
PVIKFDDKWI ADSDVIVGII EEKYPNPSLS PPTEVSSVGS KVFPSFVKFL KSKDSTDGSE
QALIDELKAL DEHLSTKGPY VNGENICAVD LSLAPKLYHL DVALGHFKKW SVPESLTHVH
NYMKLLFSRE SFQKTKAAKE FVIAGWAPKV NA
//
