ID   GSHRC_ORYSJ             Reviewed;         496 AA.
AC   P48642; Q6K3E8; Q8GRV3; Q9ZNS8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Glutathione reductase, cytosolic;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
GN   Name=GRC2; Synonyms=RGRC2;
GN   OrderedLocusNames=Os02g0813500, LOC_Os02g56850;
GN   ORFNames=OJ1293_E04.4-1, OSJNBa0053L11.26-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=99159219; PubMed=10050312;
RA   Kaminaka H., Morita S., Nakajima M., Masumura T., Tanaka K.;
RT   "Gene cloning and expression of cytosolic glutathione reductase in
RT   rice (Oryza sativa L.).";
RL   Plant Cell Physiol. 39:1269-1280(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RG   The international rice genome sequencing project (IRGSP) consortium;
RT   "Oryza sativa nipponbare chromosome 2 genomic DNA sequence.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 355-413.
RX   MEDLINE=22286393; PubMed=12399401;
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
CC       cytosol.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
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.
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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; 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; NP_001048485.1; -.
DR   UniGene; Os.4154; -.
DR   HSSP; P39040; 1FEC.
DR   GeneID; 4331112; -.
DR   KEGG; osa:4331112; -.
DR   Gramene; P48642; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:InterPro.
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   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006324; Glut_reduct_pln.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR001864; Trypnth_redctse.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00470; TRYPANRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01424; gluta_reduc_2; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    496       Glutathione reductase, cytosolic.
FT                                /FTId=PRO_0000067963.
FT   NP_BIND      61     70       FAD (By similarity).
FT   ACT_SITE    469    469       Proton acceptor (By similarity).
FT   BINDING     231    231       NADP (By similarity).
FT   BINDING     237    237       NADP (By similarity).
FT   DISULFID     70     75       Redox-active (By similarity).
FT   CONFLICT     31     31       G -> V (in Ref. 1; BAA11214).
FT   CONFLICT     48     48       V -> F (in Ref. 1; BAA11214).
FT   CONFLICT     97     97       F -> L (in Ref. 1; BAA11214).
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
//