ID   GSHRP_SOYBN             Reviewed;         544 AA.
AC   P48640;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Glutathione reductase, chloroplastic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   Flags: Precursor;
GN   Name=GR;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=8165247; DOI=10.1104/pp.104.3.1081;
RA   Tang X., Webb M.A.;
RT   "Soybean root nodule cDNA encoding glutathione reductase.";
RL   Plant Physiol. 104:1081-1082(1994).
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 {ECO:0000305}.
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; L11632; AAA33962.1; -; mRNA.
DR   PIR; T07155; T07155.
DR   RefSeq; NP_001238006.1; NM_001251077.1.
DR   AlphaFoldDB; P48640; -.
DR   SMR; P48640; -.
DR   STRING; 3847.P48640; -.
DR   PaxDb; 3847-GLYMA02G16010-3; -.
DR   GeneID; 547793; -.
DR   KEGG; gmx:547793; -.
DR   eggNOG; KOG0405; Eukaryota.
DR   InParanoid; P48640; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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:SF2; 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   Chloroplast; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Plastid; Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..544
FT                   /note="Glutathione reductase, chloroplastic"
FT                   /id="PRO_0000030282"
FT   REGION          519..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        507
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..118
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  58783 MW;  7A71449EA21CE639 CRC64;
     MATSLSVSPS LSLNTLFIAK ALPLSRPSFL SLPLPKSLLS LSTRRRTFIV RAESQNGRDP
     VPAHYDFDLF TIGAGSGGVR ARRFAANYGA SVAICELPFS TISSETTGVG GTCVIRGCVP
     KKLLVYASKF SHEFEESNGF GWRYDSEPKH DWSSFIANKN AELQRLTGIY KNILNNAGVK
     LIEGHGKMID PHTVDVNGKL YSAKHILVAV GGRPFIPDIP GKELAIDSDA ALDLPTKPVK
     IAIVGGGYIA LEFAGIFNGL KSEVHVFIRQ KKVLRGFDEE IRDFVEEQMS VRGIEFHTEE
     SPQAITKSAD GSFSLKTNKG TVDGFSHIMF ATGRRPNTQN LGLESVGVKL AKDGAIEVDE
     YSQTSVYSIW AVGDVTNRIN LTPVALMEGG ALVKTLFQDN PTKPDYRAVP SAVFSQPPIG
     QVGLTEEQAV QQYGDIDIFT ANFRPLKATL SGLPDRVFMK LVVCAKTNEV LGLHMCGEDA
     PEIVQGFAVA LKARLTKADF DATVGIHPSA AEEFVTMRTP TRKIRKSESS EGKSGSQAKA
     AAGV
//