ID A0A366R7Q6_9HYPO Unreviewed; 469 AA. AC A0A366R7Q6; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 18-SEP-2019, entry version 8. DE RecName: Full=Glutathione reductase {ECO:0000256|RuleBase:RU365016}; DE EC=1.8.1.7 {ECO:0000256|RuleBase:RU365016}; GN ORFNames=FIESC28_08365 {ECO:0000313|EMBL:RBR13179.1}; OS Fusarium coffeatum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium; 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 CC cytosol. {ECO:0000256|RuleBase:RU365016}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + CC NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, CC 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|RuleBase:RU003691}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000253153; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase 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: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; IPR006322; Glutathione_Rdtase_euk/bac. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR PANTHER; PTHR42737; PTHR42737; 1. 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; TIGR01421; gluta_reduc_1; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000253153}; KW Cytoplasm {ECO:0000256|RuleBase:RU365016}; KW FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003691}; KW Flavoprotein {ECO:0000256|RuleBase:RU003691}; KW NAD {ECO:0000256|PIRSR:PIRSR000350-3}; KW NADP {ECO:0000256|RuleBase:RU365016}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003691}; KW Redox-active center {ECO:0000256|RuleBase:RU003691}; KW Reference proteome {ECO:0000313|Proteomes:UP000253153}. FT DOMAIN 9 333 Pyr_redox_2. {ECO:0000259|Pfam:PF07992}. FT DOMAIN 356 467 Pyr_redox_dim. {ECO:0000259|Pfam: FT PF02852}. FT NP_BIND 184 191 NAD. {ECO:0000256|PIRSR:PIRSR000350-3}. FT ACT_SITE 458 458 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000350-2}. FT BINDING 55 55 FAD. {ECO:0000256|PIRSR:PIRSR000350-3}. FT BINDING 277 277 NAD; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000350-3}. FT BINDING 318 318 FAD. {ECO:0000256|PIRSR:PIRSR000350-3}. FT DISULFID 46 51 Redox-active. {ECO:0000256|PIRSR: FT 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 //