ID   GSHRP_SPIOL             Reviewed;         489 AA.
AC   Q43154;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Glutathione reductase, chloroplastic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   Flags: Precursor; Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. New Asia; TISSUE=Leaf;
RA   Aono M., Fujiyama K., Sano T., Tanaka K.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       chloroplast.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D37870; BAA07108.1; -; mRNA.
DR   PIR; T09151; T09151.
DR   AlphaFoldDB; Q43154; -.
DR   SMR; Q43154; -.
DR   BRENDA; 1.8.1.7; 5812.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006324; GSHR.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01424; gluta_reduc_2; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Plastid; Redox-active center; Transit peptide.
FT   TRANSIT         <1..2
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           3..489
FT                   /note="Glutathione reductase, chloroplastic"
FT                   /id="PRO_0000030283"
FT   ACT_SITE        462
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         54..63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   489 AA;  52611 MW;  970FC5B079A72CCD CRC64;
     EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP ISSEVIGGVG
     GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF NWKKLLQKKT DEIIRLNNIY
     KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD GTKLSYSAKH ILIATGSRAQ RPNIPGQELA
     ITSDEALSLE EFPKRVVILG GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV
     ARNLEGRGVN VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL
     GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV FGGQNSKPDY
     SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP MKNTISGRQE KTIMKLVVDA
     ETDKVLGASM CGPDAAEIMQ GIAIALKFGA TKAQFDSTVG IHPSAAEEFV TMREPSRRVP
     GAGKPKTNL