ID A0A0D2GTB0_9EURO Unreviewed; 645 AA. AC A0A0D2GTB0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 26-FEB-2020, entry version 27. 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; 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., Nusbaum C., RA 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 chain CC functioning in an early step of cytosolic Fe-S biogenesis. Transfers CC electrons from NADPH to the Fe-S cluster of DRE2. Positively controls CC H(2)O(2)-induced cell death. {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03178}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-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 to CC 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. {ECO:0000256|HAMAP- CC 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 of CC 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 HOGENOM; CLU_001570_17_6_1; -. 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 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 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT DOMAIN 215..466 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT NP_BIND 16..21 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 63..66 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 101..110 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 399..402 FT /note="FAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 438..441 FT /note="FAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 542..543 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT NP_BIND 548..552 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT REGION 187..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 601..622 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 198..220 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 136 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 369 FT /note="FAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 481 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 645 FT /note="FAD" FT /evidence="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 //