ID   GSHRC_BRARP             Reviewed;         502 AA.
AC   O04955;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glutathione reductase, cytosolic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=GR1;
OS   Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=51351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Seoul; TISSUE=Leaf;
RX   PubMed=9512665; DOI=10.1016/s0167-4781(97)00198-x;
RA   Lee H.S., Jo J.K., Son D.Y.;
RT   "Molecular cloning and characterization of the gene encoding glutathione
RT   reductase in Brassica campestris.";
RL   Biochim. Biophys. Acta 1395:309-314(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Lee H.S., Chung M.S., Jo J.K., Son D.Y.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Seoul;
RA   Lee H.S., Lee B., Won S., Jo J.K.;
RT   "Genomic cloning and its expression analysis of glutathione reductase from
RT   Brassica campestris var. Pekinensis.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC       {ECO:0000250}.
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 {ECO:0000305}.
CC   -!- INDUCTION: By paraquat and ozone. {ECO:0000269|PubMed:9512665}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF008441; AAC49980.2; -; mRNA.
DR   EMBL; AF255651; AAF67753.1; -; Genomic_DNA.
DR   PIR; T14394; T14394.
DR   RefSeq; NP_001288954.1; NM_001302025.1.
DR   AlphaFoldDB; O04955; -.
DR   SMR; O04955; -.
DR   STRING; 51351.O04955; -.
DR   PRIDE; O04955; -.
DR   GeneID; 103828679; -.
DR   KEGG; brp:103828679; -.
DR   eggNOG; KOG0405; Eukaryota.
DR   InParanoid; O04955; -.
DR   Proteomes; UP000011750; Unplaced.
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 (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase 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; -; 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   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..502
FT                   /note="Glutathione reductase, cytosolic"
FT                   /id="PRO_0000067962"
FT   ACT_SITE        475
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..76
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  54059 MW;  397D978EE114B6BE CRC64;
     MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN GAKVGICELP
     FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA RNYGWEINGN VDFNWKKLLQ
     KKTDEILRLN NIYKRLLANA AVKLYEGEGR IVGPNEVEVR QIDGTKISYT AKHILIATGS
     RAQKPNIPGH ELAITSDEAL SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL
     PLRGFDDEMR ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG
     RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP VALMEATCFA
     NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA TGDILVFTSG FNPMKNTISG
     RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE IMQGIAIALK CGATKAQFDS TVGIHPSSAE
     EFVTMRTVTR RIAYKAKPQT SL