ID A0A0E0NQ22_ORYRU Unreviewed; 555 AA.
AC A0A0E0NQ22;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glutathione reductase {ECO:0000256|RuleBase:RU365040};
DE Short=GRase {ECO:0000256|RuleBase:RU365040};
DE EC=1.8.1.7 {ECO:0000256|RuleBase:RU365040};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI03G04410.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI03G04410.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Maintains high levels of reduced glutathione.
CC {ECO:0000256|RuleBase:RU365040}.
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 Evidence={ECO:0000256|ARBA:ARBA00000669,
CC ECO:0000256|RuleBase:RU365040};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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; A0A0E0NQ22; -.
DR STRING; 4529.A0A0E0NQ22; -.
DR EnsemblPlants; ORUFI03G04410.1; ORUFI03G04410.1; ORUFI03G04410.
DR Gramene; ORUFI03G04410.1; ORUFI03G04410.1; ORUFI03G04410.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_3_1; -.
DR OMA; MSKHYDY; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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: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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW NADP {ECO:0000256|RuleBase:RU365040};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000008022}.
FT DOMAIN 79..402
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 422..530
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 520
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 199
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 258..265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 387
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 126..131
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 555 AA; 60260 MW; E1B474C2C5CEA7CA CRC64;
MATTATLPFS CSSTLQTLTR TIPLRLRLHR RRFLHHLPSL SALPRLPLPR PPLLPHARRQ
VSASAAPNGA SSEGEYDYDL FTIGAGSGGV RASRFASTLY GARAAVCEMP FATVASDDLG
GVGGTCVLRG CVPKKLLVYG SKYSHEFEES HGFGWVYETD PKHDWNTLIA NKNTELQRLV
GIYKNILNNS GVTLIEGRGK IVDPHTVSVD GKLYTARNIL IAVGGRPSMP NIPGIEHVID
SDAALDLPSK PEKIAIVGGG YIALEFAGIF NGLKSEVHVF IRQKKVLRGF DEEVRDFIAE
QMSLRGITFH TEQSPQAITK SNDGLLSLKT NKETIGGFSH VMFATGRKPN TKNLGLEEVG
VKLDKNGAIM VDEYSRTSVD SIWAVGDVTD RVNLTPVALM EGGAFAKTVF GDEPTKPDYR
AVPSAVFSQP PIGQVGLTEE QAIEEYGDVD IYTANFRPLR ATLSGLPDRI FMKLIVCATT
NKVVGVHMCG EDAPEIIQGV AIAVKAGLTK QDFDATIGIH PTSAEEFVTM RNATRKVRRS
TTDEVESKDK VVTQN
//
