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 08-NOV-2023, entry version 125.
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; Pseudomonadota; 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 (NADP) 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; FAD/NAD(P)-binding domain; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01424; gluta_reduc_2; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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
//
