ID   A0A0E0M7N5_ORYPU        Unreviewed;       506 AA.
AC   A0A0E0M7N5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glutathione-disulfide reductase {ECO:0008006|Google:ProtNLM};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G08600.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G08600.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G08600.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   AlphaFoldDB; A0A0E0M7N5; -.
DR   STRING; 4537.A0A0E0M7N5; -.
DR   EnsemblPlants; OPUNC10G08600.1; OPUNC10G08600.1; OPUNC10G08600.
DR   Gramene; OPUNC10G08600.1; OPUNC10G08600.1; OPUNC10G08600.
DR   eggNOG; KOG0405; Eukaryota.
DR   HOGENOM; CLU_016755_2_1_1; -.
DR   OMA; CFDYVKP; -.
DR   Proteomes; UP000026962; Chromosome 10.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
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   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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT   DOMAIN          26..313
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          333..441
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   REGION          445..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  54643 MW;  1CF4C7B3E3D291D8 CRC64;
     MRASRVAASL YGARAAVCEM PFATVASDSL GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE
     NHGFGWRYGT EPKHNWSTLM TNKNLELQRL VGVQTNMLKN SGVTIIEGRG KVVDPHTVSV
     DGKLYTAKNI LVAVGGRPSM PDIPGIVHVI DSDAALDLPS RPEKIAIVGG GYIALEFAGI
     FNGLKSGVHV FIRQKKVLRG FDEEVRDFVA DQMSLRGITF HAEETPQAVT KSDDGLLTLK
     TNKGSINGFS HVMFATGRKP NTKNLGLEEV GVKMDKHGAI VVDEFSRTSV DSIWAVGDVT
     NRVNLTPVAL MEGGALARTI FGNEPTKPDY SAVPSAVFSQ PPIGQVGLTE EKAIEKYGDV
     DIYISNFRPL RATLSGLPDR VYMKVIVCAN TNKVLGVHMC GEDAPEIIQG IAIAVKAGLT
     KQNFDATIGV HPSTAEELVT MRSPTRKVRR DAADEAKMKD EATSQSVLQS DQSISNRGNN
     RQVSVFQAAP EKSNPRLQPV KNGDEL
//