ID A0A366R7Q6_9HYPO Unreviewed; 469 AA. AC A0A366R7Q6; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 29-MAY-2024, entry version 24. DE RecName: Full=Glutathione reductase {ECO:0000256|ARBA:ARBA00017111, ECO:0000256|RuleBase:RU365016}; DE EC=1.8.1.7 {ECO:0000256|ARBA:ARBA00012607, ECO:0000256|RuleBase:RU365016}; GN ORFNames=FIESC28_08365 {ECO:0000313|EMBL:RBR13179.1}; OS Fusarium coffeatum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium incarnatum-equiseti species complex. OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR13179.1, ECO:0000313|Proteomes:UP000253153}; RN [1] {ECO:0000313|EMBL:RBR13179.1, ECO:0000313|Proteomes:UP000253153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR13179.1, RC ECO:0000313|Proteomes:UP000253153}; RA Gardiner D.M.; RT "Fusarium incarnatum-equiseti species complex species 28."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol. CC {ECO:0000256|ARBA:ARBA00003189, ECO:0000256|RuleBase:RU365016}. 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 Evidence={ECO:0000256|RuleBase:RU365016}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365016}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532, CC ECO:0000256|RuleBase:RU003691}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RBR13179.1}. 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; QKXC01000188; RBR13179.1; -; Genomic_DNA. DR AlphaFoldDB; A0A366R7Q6; -. DR OrthoDB; 5473641at2759; -. DR Proteomes; UP000253153; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. 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: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; IPR006322; Glutathione_Rdtase_euk/bac. 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; TIGR01421; gluta_reduc_1; 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 {ECO:0000256|RuleBase:RU365016}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3}; KW NADP {ECO:0000256|RuleBase:RU365016}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003691}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|RuleBase:RU003691}. FT DOMAIN 9..333 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 356..467 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" FT ACT_SITE 458 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2" FT BINDING 55 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 184..191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 277 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 318 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT DISULFID 46..51 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4" SQ SEQUENCE 469 AA; 50852 MW; D08C7015518B00CC CRC64; MAPVTKETDY LVIGGGSGGL ASARMASSKF GVKATIVENK RLGGTCVNVG CVPKKVTYNA AALAEAIHDS KAYGFSVEET APFDWSTFKT KRDAYIQRLN GIYERNLNND KVDYVHGWAR LTSKNQAEVT LDDQSKVLIN AKKILVAVGG KPTIPPEIPG AEYGTNSDGF FDISTQPKKV AIVGAGYIAV EFAGMFNALG TETHLFIRHD TFLRNFDPMI QESVTKEYER LGVKLHKRSQ ASKVEKDSNG KLTVTYKDDQ GNESVVSDVD NLIWAIGRTP ETKGIGLEEA GVKLSEKGHI VVDEYQNTAV DNIYALGDVT GEVELTPVAI AAGRRLAHRL FGGPEYSTLK LDYNNVPSVV FSHPEVGSIG LTEPEAIEKY GKDNIKVYKT SFTAMYYAMM EPEQKGPTSY KLVVTGPEEK VVGLHIMGIG SGEMLQGFGV AIKMGATKAD FDSCVAIHPT SAEELVTLK //