ID   GSHRP_PEA               Reviewed;         552 AA.
AC   P27456;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 70.
DE   RecName: Full=Glutathione reductase, chloroplastic/mitochondrial;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
DE   AltName: Full=GOR1;
DE   Flags: Precursor;
GN   Name=GR; Synonyms=GOR1;
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   TISSUE=Leaf;
RX   MEDLINE=93272041; PubMed=1303792;
RA   Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.M.;
RT   "Molecular characterization of glutathione reductase cDNAs from pea
RT   (Pisum sativum L.).";
RL   Plant J. 2:129-131(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Birte;
RX   MEDLINE=97060759; PubMed=8904805; DOI=10.1007/BF00208308;
RA   Mullineaux P.M., Enard C., Hellens R., Creissen G.;
RT   "Characterisation of a glutathione reductase gene and its genetic
RT   locus from pea (Pisum sativum L.).";
RL   Planta 200:186-194(1996).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=95400335; PubMed=7670502;
RA   Creissen G.P., Reynolds H., Xue Y., Mullineaux P.M.;
RT   "Simultaneous targeting of pea glutathione reductase and of a
RT   bacterial fusion protein to chloroplasts and mitochondria in
RT   transgenic tobacco.";
RL   Plant J. 8:167-175(1995).
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. Mitochondrion.
CC       Note=The majority of the protein is found in chloroplast, with
CC       only 3% in mitochondria.
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; X60373; CAA42921.1; ALT_INIT; mRNA.
DR   EMBL; X90996; CAA62482.1; -; Genomic_DNA.
DR   PIR; S18973; S18973.
DR   HSSP; Q94655; 1ONF.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   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   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; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase;
KW   Plastid; Redox-active center; Transit peptide.
FT   TRANSIT       1     60       Chloroplast and mitochondrion
FT                                (Potential).
FT   CHAIN        61    552       Glutathione reductase,
FT                                chloroplastic/mitochondrial.
FT                                /FTId=PRO_0000030281.
FT   NP_BIND     112    121       FAD (By similarity).
FT   ACT_SITE    515    515       Proton acceptor (By similarity).
FT   BINDING     277    277       NADP (By similarity).
FT   BINDING     283    283       NADP (By similarity).
FT   DISULFID    121    126       Redox-active (By similarity).
SQ   SEQUENCE   552 AA;  59108 MW;  690D1058AE4168BC CRC64;
     MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS PPHRTFAVRA
     ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA VCELPFSTIS SDTTGGVGGT
     CVIRGCVPKK LLVYASKFSH EFEESNGFGW RYDSEPKHDW SSLIANKNAE LQRLTGIYKN
     TLKNAGVKLI EGRGKIVDAH TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL
     DLPSKPQKIA IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR
     GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG LESVGVKVAK
     DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL AKTLFQNEPT KPDYRAIPSA
     VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN FRPMKATLSG LPDRVFMKLI VSAETNVVLG
     LHMCGEDAAE IAQGFAVGIK AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG
     KSDSKAKAVA GS
//