ID   GSHR_ANASP              Reviewed;         459 AA.
AC   P48638;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   16-DEC-2008, entry version 66.
DE   RecName: Full=Glutathione reductase;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
GN   Name=gor; OrderedLocusNames=all4968;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96032718; PubMed=7559423; DOI=10.1074/jbc.270.39.23143;
RA   Jiang F., Hellman U., Sroga G.E., Bergman B., Mannervik B.;
RT   "Cloning, sequencing, and regulation of the glutathione reductase gene
RT   from the cyanobacterium Anabaena PCC 7120.";
RL   J. Biol. Chem. 270:22882-22889(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       cytosol.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X89712; CAA61856.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB76667.1; -; Genomic_DNA.
DR   PIR; AH2426; AH2426.
DR   PIR; I39477; I39477.
DR   RefSeq; NP_489008.1; -.
DR   HSSP; Q94655; 1ONF.
DR   GeneID; 1108569; -.
DR   GenomeReviews; BA000019_GR; all4968.
DR   KEGG; ana:all4968; -.
DR   NMPDR; fig|103690.1.peg.5275; -.
DR   HOGENOM; P48638; -.
DR   BioCyc; NSP103690:ALL4968-MON; -.
DR   GO; GO:0005737; C:cytoplasm; 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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    459       Glutathione reductase.
FT                                /FTId=PRO_0000067973.
FT   NP_BIND      34     42       FAD (By similarity).
FT   ACT_SITE    448    448       Proton acceptor (By similarity).
FT   DISULFID     42     47       Redox-active (By similarity).
FT   CONFLICT    234    234       E -> Q (in Ref. 1; CAA61856).
FT   CONFLICT    340    340       R -> L (in Ref. 1; CAA61856).
FT   CONFLICT    361    361       V -> L (in Ref. 1; CAA61856).
FT   CONFLICT    372    372       L -> H (in Ref. 1; CAA61856).
FT   CONFLICT    381    383       RTR -> AP (in Ref. 1; CAA61856).
SQ   SEQUENCE   459 AA;  49478 MW;  29C1F06CE2195888 CRC64;
     MTFDYDLFVI GAGSGGLAAS KRAASYGAKV AIAENDLVGG TCVIRGCVPK KLMVYGSHFP
     ALFEDAAGYG WQVGKAELNW EHFITSIDKE VRRLSQLHIS FLEKAGVELI SGRATLVDNH
     TVEVGERKFT ADKILIAVGG RPIKPELPGM EYGITSNEIF HLKTQPKHIA IIGSGYIGTE
     FAGIMRGLGS QVTQITRGDK ILKGFDEDIR TEIQEGMTNH GIRIIPKNVV TAIEQVPEGL
     KISLSGEDQE PIIADVFLVA TGRVPNVDGL GLENAGVDVV DSSIEGPGYS TMNAIAVNEY
     SQTSQPNIYA VGDVTDRLNL TPVAIGEGRA FADSEFGNNR REFSHETIAT AVFSNPQAST
     VGLTEAEARA KLGDDAVTIY RTRFRPMYHS FTGKQERIMM KLVVDTKTDK VLGAHMVGEN
     AAEIIQGVAI AVKMGATKKD FDATVGIHPS SAEEFVTMR
//