ID A0A0D2GTB0_9EURO Unreviewed; 645 AA. AC A0A0D2GTB0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 31-JUL-2019, entry version 25. DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000256|HAMAP-Rule:MF_03178}; DE EC=1.18.1.- {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, ECO:0000313|Proteomes:UP000053029}; RN [1] {ECO:0000313|EMBL:KIW75674.1, ECO:0000313|Proteomes:UP000053029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75674.1, RC ECO:0000313|Proteomes:UP000053029}; 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: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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 RefSeq; XP_013279482.1; XM_013424028.1. DR EnsemblFungi; KIW75674; KIW75674; Z517_10416. DR GeneID; 25309906; -. DR EuPathDB; FungiDB:Z517_10416; -. DR OrthoDB; 318396at2759; -. DR Proteomes; UP000053029; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.40.50.80; -; 1. DR HAMAP; MF_03178; NDOR1; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. 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; SSF52343; SSF52343; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053029}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000053029}. FT DOMAIN 10 154 Flavodoxin-like. {ECO:0000259|PROSITE: FT PS50902}. FT DOMAIN 215 466 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. FT NP_BIND 16 21 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 63 66 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 101 110 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 399 402 FAD. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 438 441 FAD. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 542 543 NADP. {ECO:0000256|HAMAP-Rule:MF_03178}. FT NP_BIND 548 552 NADP. {ECO:0000256|HAMAP-Rule:MF_03178}. FT REGION 187 220 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 601 622 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 198 220 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT BINDING 136 136 FMN. {ECO:0000256|HAMAP-Rule:MF_03178}. FT BINDING 369 369 FAD. {ECO:0000256|HAMAP-Rule:MF_03178}. FT BINDING 481 481 NADP. {ECO:0000256|HAMAP-Rule:MF_03178}. FT BINDING 645 645 FAD. {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 //