ID   GSHRP_TOBAC             Reviewed;         557 AA.
AC   P80461;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 144.
DE   RecName: Full=Glutathione reductase, chloroplastic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   Flags: Precursor; Fragment;
GN   Name=GOR;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8547821; DOI=10.1007/bf00202667;
RA   Creissen G.P., Mullineaux P.M.;
RT   "Cloning and characterisation of glutathione reductase cDNAs and
RT   identification of two genes encoding the tobacco enzyme.";
RL   Planta 197:422-425(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 67-74.
RC   TISSUE=Leaf;
RA   Willows R.D., Kannangara G.C., Svendsen I.;
RL   Submitted (JUN-1995) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reduction of glutathione disulfide (GSSG) to
CC       reduced glutathione (GSH) (By similarity). Maintains high levels of GSH
CC       in the chloroplast (Probable). {ECO:0000250|UniProtKB:P06715,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + NADP(+) = glutathione disulfide + NADPH +
CC         H(+); 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         Evidence={ECO:0000250|UniProtKB:P06715};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P06715};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P06715};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06715}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250|UniProtKB:P06715}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; X76293; CAA53925.1; -; mRNA.
DR   PIR; S38908; S38908.
DR   AlphaFoldDB; P80461; -.
DR   SMR; P80461; -.
DR   STRING; 4097.P80461; -.
DR   PaxDb; 4097-P80461; -.
DR   BRENDA; 1.8.1.7; 3645.
DR   Proteomes; UP000790787; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   FunFam; 3.30.390.30:FF:000008; Glutathione reductase; 1.
DR   FunFam; 3.50.50.60:FF:000051; Glutathione reductase; 1.
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   NCBIfam; NF004776; PRK06116.1; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF9; 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   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   NADP; Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         <1..66
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           67..557
FT                   /note="Glutathione reductase, chloroplastic"
FT                   /id="PRO_0000030284"
FT   REGION          535..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        521
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00390"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         89
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P00390"
FT   BINDING         90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         184
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P00390"
FT   BINDING         200
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         263
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         266
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         283
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         289
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         347
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         388
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         396
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         426
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   BINDING         521
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   DISULFID        127..132
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P06715"
FT   NON_TER         1
SQ   SEQUENCE   557 AA;  60035 MW;  79813D1C6AA1D784 CRC64;
     ATSLSTPKLS TTLSSPTLHS LLYKHKFSLL SLSNPIKPLH FNFLTHSRST PSSLSCTRRR
     FTAPRAESSN GADAPRHYDF DLFTIGAGSG GVRASRFASN FGASVAVCEL PFSTISSDST
     GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE SCGFGWNYDV EPRFDWSTLI ANKNAELQRL
     TGIYKNILKN AGVTLIEGRG KVVDPHTVDV DGKLYSAKNI LISVGGRPFI PDIPGSEYAI
     DSDAALDLPT KPNKIAIVGG GYIALEFAGI FNGLKSEVHV FIRQKKVLRG FDEEIRDFVG
     EQMSLRGIEF HTEESPQAIV KSADGSLSLK TSRGTVEGFS HIMFATGRRP NTKNLGLETV
     GVKMTKNGAI EVDEYSRTSV PSIWAVGDVT DRINLTPVAL MEGGALAKTI FAHEPTKPDY
     RNVPAAVFSQ PPIGQVGLME EQAIKEFGDV DVYTANFRPL KATISGLPDR VFMKLIVCAK
     TSKVLGLHMC GDDAPEIVQG FAIAVKAGLT KADFDATVGI HPTSAEEFVT MRTPTRKVRS
     SPSEGKAEHD IKAAAGV
//