ID   GSHRC_PEA               Reviewed;         498 AA.
AC   Q43621;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Glutathione reductase, cytosolic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   AltName: Full=GOR2;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Birte; TISSUE=Leaf;
RX   PubMed=9349285; DOI=10.1023/a:1005858120232;
RA   Stevens R.G., Greissen G.P., Mullineaux P.M.;
RT   "Cloning and characterisation of a cytosolic glutathione reductase cDNA
RT   from pea (Pisum sativum L.) and its expression in response to stress.";
RL   Plant Mol. Biol. 35:641-654(1997).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC       May play a role in the restoration of the post-stress redox state of
CC       the cytosolic glutathione pool.
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: Cytoplasm.
CC   -!- INDUCTION: Increased expression in the recovery (post-stress) phases of
CC       both drought and chilling.
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; X98274; CAA66924.1; -; mRNA.
DR   PIR; T06442; T06442.
DR   AlphaFoldDB; Q43621; -.
DR   SMR; Q43621; -.
DR   EnsemblPlants; Psat1g098440.1; Psat1g098440.1.cds; Psat1g098440.
DR   EnsemblPlants; Psat1g098440.2; Psat1g098440.2.cds; Psat1g098440.
DR   Gramene; Psat1g098440.1; Psat1g098440.1.cds; Psat1g098440.
DR   Gramene; Psat1g098440.2; Psat1g098440.2.cds; Psat1g098440.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) 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; FAD/NAD(P)-binding domain; 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; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01424; gluta_reduc_2; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF4; GLUTATHIONE REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..498
FT                   /note="Glutathione reductase, cytosolic"
FT                   /id="PRO_0000067964"
FT   ACT_SITE        471
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..77
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  53897 MW;  19AD08959764C6D0 CRC64;
     MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV GICELPFHPI
     SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG WELNENVDFN WKKLLQKKTD
     EINRLNGIYK RLLSNAGVKL FEGEGKIASP NEVEVTQLDG TKLSYSAKHI LIATGSRAQR
     PNIPGQELGI TSDEALSLEE FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG
     FDDEMRAVVA RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN
     SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM EASLFAKTVF
     GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV LIFTSTFNPM KNTISGRQEK
     TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT
     MRSETRRVTG GVKPKTNL
//