ID A0A0D2GTB0_9EURO Unreviewed; 645 AA. AC A0A0D2GTB0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 24-JAN-2024, entry version 36. 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: NADPH-dependent reductase which is a central component of the CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to CC the [2Fe-2S] cluster of DRE2, another key component of the CIA CC machinery. In turn, this reduced cluster provides electrons for CC assembly of cytosolic iron-sulfur cluster proteins. Positively controls CC H(2)O(2)-induced cell death. {ECO:0000256|HAMAP-Rule:MF_03178}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 CC reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA- CC COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000256|HAMAP-Rule:MF_03178}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA- CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:60344; EC=1.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00036596}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|HAMAP-Rule:MF_03178}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00001917, CC ECO:0000256|HAMAP-Rule:MF_03178}; CC -!- SUBUNIT: Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe- CC S) protein assembly (CIA) machinery. {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 AlphaFoldDB; A0A0D2GTB0; -. DR STRING; 1442368.A0A0D2GTB0; -. DR GeneID; 25309906; -. DR VEuPathDB; FungiDB:Z517_10416; -. DR HOGENOM; CLU_001570_17_6_1; -. DR OrthoDB; 276396at2759; -. 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; 3.40.50.360; -; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. 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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03178}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03178}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_03178}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03178}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03178}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03178}; 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 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 residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 16..21 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 63..66 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 101..110 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 136 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 369 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 399..402 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 438..441 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 481 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 542..543 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 548..552 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178" FT BINDING 645 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" 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 //