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 04-NOV-2026, entry version 132. 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; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; OC 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 -!- FUNCTION: Catalyzes the reduction of glutathione disulfide (GSSG) to CC reduced glutathione (GSH). Constitutes the major mechanism to maintain CC a high GSH:GSSG ratio in the cytosol. {ECO:0000250|UniProtKB:P06715}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + NADPH + CC H(+); 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 Evidence={ECO:0000250|UniProtKB:P06715}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P06715}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P06715}; CC -!- PATHWAY: Xenobiotic degradation; (2,4,5-trichlorophenoxy)acetate CC degradation. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06715}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06715}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000250|UniProtKB:P06715}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; ISS:UniProtKB. 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:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. 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 NCBIfam; NF004776; gorA; 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|UniProtKB:P06715" FT BINDING 15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 15 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P00390" FT BINDING 16 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 35 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 42 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 43 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 99 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P00390" FT BINDING 115 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 175 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 178 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 181 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 198 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 204 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 261 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 302 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 310 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 340 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P06715" FT BINDING 435 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P06715" FT DISULFID 43..48 FT /note="Redox-active" FT /evidence="ECO:0000250|UniProtKB:P06715" 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 //