ID   GSHRP_ARATH             Reviewed;         565 AA.
AC   P42770;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 73.
DE   RecName: Full=Glutathione reductase, chloroplastic;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2360;
DE   Flags: Precursor;
GN   Name=EMB2360; OrderedLocusNames=At3g54660; ORFNames=T5N23_20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Columbia;
RA   Kubo A., Sano T., Saji H., Tanaka K., Kondo N., Tanaka K.;
RT   "Primary structure and properties of glutathione reductase from
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 34:1259-1266(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Columbia;
RA   Kubo A.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
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 (Potential).
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; D14049; BAA03137.1; -; mRNA.
DR   EMBL; D89620; BAA19653.1; -; Genomic_DNA.
DR   EMBL; AL138650; CAB77586.1; -; Genomic_DNA.
DR   PIR; T47625; T47625.
DR   RefSeq; NP_191026.1; -.
DR   UniGene; At.21776; -.
DR   HSSP; P06715; 1GER.
DR   GeneID; 824631; -.
DR   GenomeReviews; BA000014_GR; AT3G54660.
DR   KEGG; ath:AT3G54660; -.
DR   GeneFarm; 2285; 251.
DR   TAIR; At3g54660; -.
DR   ArrayExpress; P42770; -.
DR   GermOnline; AT3G54660; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; 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; Complete proteome; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Plastid; Redox-active center; Transit peptide.
FT   TRANSIT       1     74       Chloroplast (Potential).
FT   CHAIN        75    565       Glutathione reductase, chloroplastic.
FT                                /FTId=PRO_0000030280.
FT   NP_BIND     126    135       FAD (By similarity).
FT   ACT_SITE    529    529       Proton acceptor (By similarity).
FT   BINDING     291    291       NADP (By similarity).
FT   BINDING     297    297       NADP (By similarity).
FT   DISULFID    135    140       Redox-active (By similarity).
SQ   SEQUENCE   565 AA;  60852 MW;  29C2CD0E68ED4E4A CRC64;
     MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY SLRPRIALLS
     NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV RASRFATSFG ASAAVCELPF
     STISSDTAGG VGGTCVLRGC VPKKLLVYAS KYSHEFEDSH GFGWKYETEP SHDWTTLIAN
     KNAELQRLTG IYKNILSKAN VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD
     IPGKEFAIDS DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD
     EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV MFATGRKPNT
     KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR INLTPVALME GGALAKTLFQ
     NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF
     MKLIVCANTN KVLGVHMCGE DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR
     APTRKFRKDS SEGKASPEAK TAAGV
//