ID   GSHR_HAEIN              Reviewed;         456 AA.
AC   P43783;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 68.
DE   RecName: Full=Glutathione reductase;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
GN   Name=gor; OrderedLocusNames=HI0161;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RA   Barcak G.J., Heimer S.R.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- 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; U20229; AAA62137.1; -; Genomic_DNA.
DR   EMBL; L42023; AAC21833.1; -; Genomic_DNA.
DR   PIR; A64052; A64052.
DR   RefSeq; NP_438331.1; -.
DR   HSSP; P00390; 1ALG.
DR   SMR; P43783; 2-456.
DR   GeneID; 951071; -.
DR   GenomeReviews; L42023_GR; HI0161.
DR   KEGG; hin:HI0161; -.
DR   NMPDR; fig|71421.1.peg.152; -.
DR   TIGR; HI0161; -.
DR   HOGENOM; P43783; -.
DR   BioCyc; HINF71421:HI_0161-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR006322; Glut_reduct_1.
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; TIGR01421; gluta_reduc_1; 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    456       Glutathione reductase.
FT                                /FTId=PRO_0000067976.
FT   NP_BIND      34     42       FAD (By similarity).
FT   ACT_SITE    445    445       Proton acceptor (By similarity).
FT   DISULFID     42     47       Redox-active (By similarity).
SQ   SEQUENCE   456 AA;  49329 MW;  846988C215FE949A CRC64;
     MTKHYDYIAI GGGSGGIASL NRAASYGKKC AIIEAKHLGG TCVNVGCVPK KVMFYGAHIA
     EAINNYAPDY GFDVEVKKFD FSKLIESRQA YISRIHTSYN NVLAKNNIDV INGFGKFVDA
     HTIEVTLADG TKEQVTADHI LIATGGRPYR PNIKGQEYGI DSDGFFALTE LPKRAAVIGA
     GYIAVELSGV LNSLGVETHL LVRRHAPMRN QDPLIVETLV EVLAQDGIQL HTNSTPSEIV
     KNADGSLTVR CDGQSDVTVD CVIWAAGRVP TTDKIGLENA GVETNEHGYV KVDKYQNTNV
     KGIYAVGDII ENGIELTPVA VAAGRRLSER LFNNKPTEYL DYSLVPTVVF SHPPIGTVGL
     TEPQAIEQYG AENVKVYKSS FTAMYTAVTQ HRQPCKMKLV CVGKDEKVVG LHGIGFGVDE
     MIQGFAVAIK MGATKADFDN TVAIHPTGSE EFVTMR
//