ID   GSHRC_BRARP             Reviewed;         502 AA.
AC   O04955;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Glutathione reductase, cytosolic;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
GN   Name=GR1;
OS   Brassica rapa subsp. pekinensis (Chinese cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=51351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Seoul; TISSUE=Leaf;
RX   MEDLINE=98173810; PubMed=9512665; DOI=10.1016/S0167-4781(97)00198-X;
RA   Lee H.S., Jo J.K., Son D.Y.;
RT   "Molecular cloning and characterization of the gene encoding
RT   glutathione reductase in Brassica campestris.";
RL   Biochim. Biophys. Acta 1395:309-314(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Lee H.S., Chung M.S., Jo J.K., Son D.Y.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Seoul;
RA   Lee H.S., Lee B., Won S., Jo J.K.;
RT   "Genomic cloning and its expression analysis of glutathione reductase
RT   from Brassica campestris var. Pekinensis.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       cytosol (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- INDUCTION: By paraquat and ozone.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AF008441; AAC49980.2; -; mRNA.
DR   EMBL; AF255651; AAF67753.1; -; Genomic_DNA.
DR   PIR; T14394; T14394.
DR   HSSP; Q94655; 1ONF.
DR   BRENDA; 1.8.1.7; 142183.
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; IPR000815; Hg_reductase.
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   PRINTS; PR00945; HGRDTASE.
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    502       Glutathione reductase, cytosolic.
FT                                /FTId=PRO_0000067962.
FT   NP_BIND      67     76       FAD (By similarity).
FT   ACT_SITE    475    475       Proton acceptor (By similarity).
FT   BINDING     237    237       NADP (By similarity).
FT   BINDING     243    243       NADP (By similarity).
FT   DISULFID     76     81       Redox-active (By similarity).
SQ   SEQUENCE   502 AA;  54059 MW;  397D978EE114B6BE CRC64;
     MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN GAKVGICELP
     FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA RNYGWEINGN VDFNWKKLLQ
     KKTDEILRLN NIYKRLLANA AVKLYEGEGR IVGPNEVEVR QIDGTKISYT AKHILIATGS
     RAQKPNIPGH ELAITSDEAL SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL
     PLRGFDDEMR ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG
     RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP VALMEATCFA
     NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA TGDILVFTSG FNPMKNTISG
     RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE IMQGIAIALK CGATKAQFDS TVGIHPSSAE
     EFVTMRTVTR RIAYKAKPQT SL
//