ID A0A0D2GTB0_9EURO Unreviewed; 645 AA. AC A0A0D2GTB0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 16-SEP-2015, entry version 4. DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000256|HAMAP-Rule:MF_03178}; DE EC=1.6.-.- {ECO:0000256|HAMAP-Rule:MF_03178}; DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03178}; GN Name=TAH18 {ECO:0000256|HAMAP-Rule:MF_03178}; GN ORFNames=Z517_10416 {ECO:0000313|EMBL:KIW75674.1}; OS Fonsecaea pedrosoi CBS 271.37. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; OC Fonsecaea. OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW75674.1}; RN [1] {ECO:0000313|EMBL:KIW75674.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75674.1}; RG The Broad Institute Genomics Platform; RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M., RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein CC assembly (CIA) machinery. Required for the maturation of CC extramitochondrial Fe-S proteins. Part of an electron transfer CC chain functioning in an early step of cytosolic Fe-S biogenesis. CC Transfers electrons from NADPH to the Fe-S cluster of DRE2. CC Positively controls H(2)O(2)-induced cell death. CC {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03178}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03178}; CC -!- SUBUNIT: Interacts with DRE2. {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}. CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}. Note=Relocalizes CC to mitochondria after H(2)O(2) exposure. {ECO:0000256|HAMAP- CC Rule:MF_03178}. CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase CC NDOR1 family. {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. {ECO:0000256|HAMAP- CC Rule:MF_03178}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC {ECO:0000256|HAMAP-Rule:MF_03178}. 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; KN846975; KIW75674.1; -; Genomic_DNA. DR EnsemblFungi; KIW75674; KIW75674; Z517_10416. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_03178; NDOR1; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR028879; NDOR1. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}; KW FAD {ECO:0000256|HAMAP-Rule:MF_03178}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_03178}; KW FMN {ECO:0000256|HAMAP-Rule:MF_03178}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}; KW NADP {ECO:0000256|HAMAP-Rule:MF_03178}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03178}. FT DOMAIN 10 154 Flavodoxin-like. {ECO:0000256|HAMAP-Rule: FT MF_03178}. FT DOMAIN 215 466 FAD-binding FR-type. {ECO:0000256|HAMAP- FT Rule:MF_03178}. FT NP_BIND 16 20 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 98 129 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 250 261 FAD. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 396 406 FAD. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 570 586 NADP. {ECO:0000256|HAMAP-Rule:MF_03178}. SQ SEQUENCE 645 AA; 71903 MW; E1FDC21ABF5579FA CRC64; MTEQGRDRSA LVLYGTETGT AQDLAEEVGR TLERLHFRTD VLGLDAATHG LLHQYTLTVF VVATTGQGDF PENARRFWTG LLRKKLAATT LAGVDYALAG LGDTSYPKFN WAARKLDKRL RQLGASPLVE PCEADEQGDE GTDGAFLSWI QLFRETVLNT FPLADGQDPI PNDVLLPTKW RLERASEHPA ASGASSIADG NHRPSSTTTG PNAPPNSFSV SLECNQRVTP LDHWQDVRFM SLKTSAKISY MPGDALAISP QNIAEDVESL ITRMGWQRVA DVPIRLVSTR RSTSATTLAG LASDAIFRRA RLTLRALLTE YLDINAIPRR SFFGCIANYT SNDMHKERLL EFTDPQYLDE YYDYATRPRR SILEILQEFD SVHLPWEEVT SIFPAMRPRQ FSIASGGLLK STEDRATKFE LLVAIVKYRT VIKRIREGVC TRYLAQLPAG TTLQVSLKTE GRFSRAGELA DQSHILVGAG TGIAPLRALI HEKAMQDQVS GPTALFFGCR NARSDYFFRD EWTALQTKDH PTAGLEVITA FSRDQTSKVY VQDRMRQRSR LICQFLRDKA ATVIVCGSSG QMPKAVRQAL VDALVQQGKS TENEDKAVSG QGMVPVEEEP IQTEEDAEKY LARLEKVGRY KQETW //