ID   GSHR_BURCE     STANDARD;      PRT;   449 AA.
AC   P48639;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Glutathione reductase (EC 1.8.1.7) (GR) (GRase).
GN   Name=gor;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AC1100;
RX   MEDLINE=95266809; PubMed=7538273;
RA   Daubaras D.L., Hershberger C.D., Kitano K., Chakrabarty A.M.;
RT   "Sequence analysis of a gene cluster involved in metabolism of 2,4,5-
RT   trichlorophenoxyacetic acid by Burkholderia cepacia AC1100.";
RL   Appl. Environ. Microbiol. 61:1279-1289(1995).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- PATHWAY: 2,4,5-trichlorophenoxyacetic acid degradation.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U19883; AAC43334.1; -.
DR   PIR; I40178; I40178.
DR   HSSP; Q94655; 1ONF.
DR   InterPro; IPR001327; FAD_pyr_redox.
DR   InterPro; IPR006324; Glut_reduct_2.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR001100; Pyr_redox.
DR   InterPro; IPR004099; Pyr_redox_dim.
DR   Pfam; PF00070; Pyr_redox; 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.
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
FT   NP_BIND      35     43       FAD (ADP part) (By similarity).
FT   DISULFID     43     48       Redox-active (By similarity).
FT   ACT_SITE    435    435       Proton acceptor (By similarity).
SQ   SEQUENCE   449 AA;  47541 MW;  402FCC6E7A8D6720 CRC64;
     MQKYDFDLFV IGAGSGGVRA ARIAAGHGAK VAIAEEYRFG GTCVIRGCVP KKLLMYASQY
     GQGFEDAAGF GWHSAATSHS WTSLIAAKDA EIARLEGVYQ RLIENANVEI FKGRAQIAGP
     NRVTVTGASV SARTILIATG ARPVMPPVAG ANLMITSDDV FDLPVGPPRI AIIGGGYIAC
     EFAGIFNGLG RHVVQLHRGS QVLRGFDDEL REHLGDELKK SGIDLRLGVD VVAVERQRGA
     LSVQLTTGDA MEVDAVMAAT GRLPNTWGLG LETVDVGLDQ NGAIKVDEYS RTSSPGIYAV
     GDVTNRLNLT PVAIHEGHAF ADTVFGGKAL PTEHENVPFA VFSQPQAASV GLSEAQARDR
     YSNVEIYGSA FRPMRAALSG RDEKALVKLV VNGSNDRVVG AHIVGADAAE IIQGIAVAIK
     ARATKADFDA TLGVHPTLAE EFVTLRNRR
//