ID   GSHRP_SPIOL             Reviewed;         489 AA.
AC   Q43154;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Glutathione reductase, chloroplastic;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
DE   Flags: Precursor; Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. New Asia; TISSUE=Leaf;
RA   Aono M., Fujiyama K., Sano T., Tanaka K.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       chloroplast.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; D37870; BAA07108.1; -; mRNA.
DR   PIR; T09151; T09151.
DR   HSSP; Q94655; 1ONF.
DR   BRENDA; 1.8.1.7; 286.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
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   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   Chloroplast; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Plastid; Redox-active center; Transit peptide.
FT   TRANSIT      <1      2       Chloroplast (Potential).
FT   CHAIN         3    489       Glutathione reductase, chloroplastic.
FT                                /FTId=PRO_0000030283.
FT   NP_BIND      54     63       FAD (By similarity).
FT   ACT_SITE    462    462       Proton acceptor (By similarity).
FT   BINDING     224    224       NADP (By similarity).
FT   BINDING     230    230       NADP (By similarity).
FT   DISULFID     63     68       Redox-active (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   489 AA;  52611 MW;  970FC5B079A72CCD CRC64;
     EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP ISSEVIGGVG
     GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF NWKKLLQKKT DEIIRLNNIY
     KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD GTKLSYSAKH ILIATGSRAQ RPNIPGQELA
     ITSDEALSLE EFPKRVVILG GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV
     ARNLEGRGVN VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL
     GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV FGGQNSKPDY
     SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP MKNTISGRQE KTIMKLVVDA
     ETDKVLGASM CGPDAAEIMQ GIAIALKFGA TKAQFDSTVG IHPSAAEEFV TMREPSRRVP
     GAGKPKTNL
//