GSHRC_ORYSJ
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 03-AUG-2022, entry version 156.
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; 4530.OS02T0813500-01; -.
DR PaxDb; P48642; -.
DR PRIDE; 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; CFDYVKP; -.
DR OrthoDB; 581771at2759; -.
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 Genevisible; P48642; OS.
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..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