ID A9NS07_PICSI Unreviewed; 284 AA.
AC A9NS07;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=glutathione dehydrogenase (ascorbate) {ECO:0000256|ARBA:ARBA00012436};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABK23418.1};
RN [1] {ECO:0000313|EMBL:ABK23418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Green portion of the leader tissue
RC {ECO:0000313|EMBL:ABK23418.1};
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
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; EF084088; ABK23418.1; -; mRNA.
DR AlphaFoldDB; A9NS07; -.
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; 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 2: Evidence at transcript level;
FT DOMAIN 81..159
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 137..284
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 284 AA; 31805 MW; B557481CC26EF233 CRC64;
MLGKAPTLGV ASTSSLTVAK NLRCDSLESL VLYRRAFNCG LLTQLFGERG VRSRVLLQKR
KIASTRIVSM AEALDVCVKA ATGVPDKLGD CPFSQRVLLT LEEKQVPYNT KLIDTSNKPD
WFLQISPEGK VPVLKIDDKW VPDSDVITQI LEEKYPEPPL ATPPEKATVG SKIFSTFIPF
LKSKDPNDGT EQALLNELRA LDEHLKDNGP FINGEKISAV DISLAPKLYH LKVALGHFKK
WSVPEELTYV RDYMETLFSR ESFLRTSPPD EQYIIASWFP KVNP
//
