ID   GSHRC_ORYSJ             Reviewed;         496 AA.
AC   P48642; A0A0P0VR51; Q0DWI9; Q6K3E8; Q8GRV3; Q9ZNS8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Glutathione reductase, cytosolic;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=GRC2; Synonyms=RGRC2;
GN   OrderedLocusNames=Os02g0813500 {ECO:0000312|EMBL:BAF10399.1},
GN   LOC_Os02g56850 {ECO:0000305};
GN   ORFNames=OJ1293_E04.4-1, OsJ_08842 {ECO:0000312|EMBL:EAZ25050.1},
GN   OSJNBa0053L11.26-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=10050312; DOI=10.1093/oxfordjournals.pcp.a029330;
RA   Kaminaka H., Morita S., Nakajima M., Masumura T., Tanaka K.;
RT   "Gene cloning and expression of cytosolic glutathione reductase in rice
RT   (Oryza sativa L.).";
RL   Plant Cell Physiol. 39:1269-1280(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 355-413.
RX   PubMed=12399401; DOI=10.1093/genetics/162.2.941;
RA   Olsen K.M., Purugganan M.D.;
RT   "Molecular evidence on the origin and evolution of glutinous rice.";
RL   Genetics 162:941-950(2002).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
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.
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; D78136; BAA11214.1; -; mRNA.
DR   EMBL; D85751; BAA36283.1; -; mRNA.
DR   EMBL; AB009592; BAA37092.1; -; Genomic_DNA.
DR   EMBL; AP004120; BAD21653.1; -; Genomic_DNA.
DR   EMBL; AP005691; BAD22392.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF10399.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS81540.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ25050.1; -; Genomic_DNA.
DR   EMBL; AY136760; AAN15933.1; -; Genomic_DNA.
DR   EMBL; AY136761; AAN15934.1; -; Genomic_DNA.
DR   EMBL; AY136762; AAN15935.1; -; Genomic_DNA.
DR   EMBL; AY136763; AAN15936.1; -; Genomic_DNA.
DR   EMBL; AY136764; AAN15937.1; -; Genomic_DNA.
DR   EMBL; AY136765; AAN15938.1; -; Genomic_DNA.
DR   EMBL; AY136766; AAN15939.1; -; Genomic_DNA.
DR   PIR; T03766; T03766.
DR   RefSeq; XP_015626808.1; XM_015771322.1.
DR   RefSeq; XP_015626809.1; XM_015771323.1.
DR   AlphaFoldDB; P48642; -.
DR   SMR; P48642; -.
DR   STRING; 39947.P48642; -.
DR   PaxDb; 39947-P48642; -.
DR   EnsemblPlants; Os02t0813500-01; Os02t0813500-01; Os02g0813500.
DR   GeneID; 4331112; -.
DR   Gramene; Os02t0813500-01; Os02t0813500-01; Os02g0813500.
DR   KEGG; osa:4331112; -.
DR   eggNOG; KOG0405; Eukaryota.
DR   HOGENOM; CLU_016755_2_1_1; -.
DR   InParanoid; P48642; -.
DR   OMA; VHIIHHN; -.
DR   OrthoDB; 5473641at2759; -.
DR   BRENDA; 1.8.1.7; 4460.
DR   PlantReactome; R-OSA-1119298; Glutathione redox reactions II.
DR   PlantReactome; R-OSA-1119437; Glutathione redox reactions I.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; P48642; baseline and differential.
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:SF4; 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.
DR   Genevisible; P48642; OS.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..496
FT                   /note="Glutathione reductase, cytosolic"
FT                   /id="PRO_0000067963"
FT   ACT_SITE        469
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..70
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..75
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        31
FT                   /note="G -> V (in Ref. 1; BAA11214)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="V -> F (in Ref. 1; BAA11214)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="F -> L (in Ref. 1; BAA11214)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  53507 MW;  A27FEE5D847F97F6 CRC64;
     MARKMLKDEE VEVAVTDGGS YDYDLFVIGA GSGGVRGSRT SASFGAKVAI CELPFHPISS
     DWQGGHGGTC VIRGCVPKKI LVYGSSFRGE FEDAKNFGWE INGDINFNWK RLLENKTQEI
     VRLNGVYQRI LGNSGVTMIE GAGSLVDAHT VEVTKPDGSK QRYTAKHILI ATGSRAQRVN
     IPGKELAITS DEALSLEELP KRAVILGGGY IAVEFASIWK GMGAHVDLFY RKELPLRGFD
     DEMRTVVASN LEGRGIRLHP GTNLSELSKT ADGIKVVTDK GEEIIADVVL FATGRTPNSQ
     RLNLEAAGVE VDNIGAIKVD DYSRTSVPNI WAVGDVTNRI NLTPVALMEA TCFSKTVFGG
     QPTKPDYRDV PCAVFSIPPL SVVGLSEQQA LEEAKSDVLV YTSSFNPMKN SISKRQEKTV
     MKLVVDSETD KVLGASMCGP DAPEIIQGMA VALKCGATKA TFDSTVGIHP SAAEEFVTMR
     TLTRRVSPSS KPKTNL
//