ID   GSHR_BURCE              Reviewed;         449 AA.
AC   P48639;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=gor;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AC1100;
RX   PubMed=7538273; DOI=10.1128/aem.61.4.1279-1289.1995;
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:
CC       Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- PATHWAY: Xenobiotic degradation; (2,4,5-trichlorophenoxy)acetate
CC       degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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. {ECO:0000305}.
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DR   EMBL; U19883; AAC43334.1; -; Genomic_DNA.
DR   PIR; I40178; I40178.
DR   AlphaFoldDB; P48639; -.
DR   SMR; P48639; -.
DR   UniPathway; UPA00686; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0046228; P:2,4,5-trichlorophenoxyacetic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006324; GSHR.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01424; gluta_reduc_2; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..449
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067974"
FT   ACT_SITE        435
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
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