ID   GSHRC_PEA               Reviewed;         498 AA.
AC   Q43621;
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, cytosolic;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
DE   AltName: Full=GOR2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Birte; TISSUE=Leaf;
RX   MEDLINE=98009998; PubMed=9349285; DOI=10.1023/A:1005858120232;
RA   Stevens R.G., Greissen G.P., Mullineaux P.M.;
RT   "Cloning and characterisation of a cytosolic glutathione reductase
RT   cDNA from pea (Pisum sativum L.) and its expression in response to
RT   stress.";
RL   Plant Mol. Biol. 35:641-654(1997).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       cytosol. May play a role in the restoration of the post-stress
CC       redox state of the cytosolic glutathione pool.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Increased expression in the recovery (post-stress)
CC       phases of both drought and chilling.
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; X98274; CAA66924.1; -; mRNA.
DR   PIR; T06442; T06442.
DR   HSSP; Q94655; 1ONF.
DR   BRENDA; 1.8.1.7; 287.
DR   GO; GO:0005737; C:cytoplasm; 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   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    498       Glutathione reductase, cytosolic.
FT                                /FTId=PRO_0000067964.
FT   NP_BIND      63     72       FAD (By similarity).
FT   ACT_SITE    471    471       Proton acceptor (By similarity).
FT   BINDING     233    233       NADP (By similarity).
FT   BINDING     239    239       NADP (By similarity).
FT   DISULFID     72     77       Redox-active (By similarity).
SQ   SEQUENCE   498 AA;  53897 MW;  19AD08959764C6D0 CRC64;
     MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV GICELPFHPI
     SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG WELNENVDFN WKKLLQKKTD
     EINRLNGIYK RLLSNAGVKL FEGEGKIASP NEVEVTQLDG TKLSYSAKHI LIATGSRAQR
     PNIPGQELGI TSDEALSLEE FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG
     FDDEMRAVVA RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN
     SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM EASLFAKTVF
     GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV LIFTSTFNPM KNTISGRQEK
     TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT
     MRSETRRVTG GVKPKTNL
//