AC MF_03178; DC Protein; auto TR HAMAP; MF_03178; -; 1; level=0 XX Names: NDOR1 XX ID NDOR1 DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1; DE EC=1.18.1.-; DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase; case GN Name=TAH18; else case GN Name=NDOR1; end case XX case 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 @gn(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. CC -!- SUBUNIT: Interacts with @gn(DRE2); as part of the cytosolic iron-sulfur CC (Fe-S) protein assembly (CIA) machinery. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Relocalizes to CC mitochondria after H(2)O(2) exposure. else case 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 @gn(CIAPIN1), another key component of the CIA CC machinery. In turn, this reduced cluster provides electrons for CC assembly of cytosolic iron-sulfur cluster proteins. It can also reduce CC the [2Fe-2S] cluster of @gn(CISD1) and activate this protein implicated CC in Fe/S cluster repair. CC -!- SUBUNIT: Interacts with @gn(CIAPIN1); as part of the cytosolic iron- CC sulfur (Fe-S) protein assembly (CIA) machinery. CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=Concentrated CC in perinuclear structure. else 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 the anamorsin/DRE2 homolog, another key CC component of the CIA machinery. In turn, this reduced cluster provides CC electrons for assembly of cytosolic iron-sulfur cluster proteins. CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case 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; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase CC NDOR1 family. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. XX DR PROSITE; PS51384; FAD_FR; 1; trigger=yes DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1; trigger=no DR Pfam; PF00667; FAD_binding_1; 1; trigger=no DR Pfam; PF00258; Flavodoxin_1; 1; trigger=no DR Pfam; PF00175; NAD_binding_1; 1; trigger=no DR PRINTS; PR00369; FLAVODOXIN; 1; trigger=no DR PRINTS; PR00371; FPNCR; 1; trigger=no XX case KW Mitochondrion end case KW Cytoplasm KW FAD KW Flavoprotein KW FMN KW NADP KW Oxidoreductase XX case GO GO:0005739; C:mitochondrion else case GO GO:0048471; C:perinuclear region of cytoplasm end case GO GO:0005737; C:cytoplasm GO GO:0050660; F:flavin adenine dinucleotide binding GO GO:0010181; F:FMN binding GO GO:0050661; F:NADP binding GO GO:0016651; F:oxidoreductase activity, acting on NAD(P)H GO GO:0016226; P:iron-sulfur cluster assembly XX FT From: NDOR1_HUMAN (Q9UHB4) FT DOMAIN 6..150 FT /note="Flavodoxin-like" FT BINDING 12..17 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [ST]-[QE]-[ST]-G-[TN]-[AS] FT BINDING 59..62 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [AS]-T-x-G FT BINDING 97..106 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [LIVC]-G-D-[ST]-[ST]-Y-x-[KR]-[FY]-[NC] FT BINDING 382..385 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: R-x-[FY]-S FT BINDING 416..419 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: G-[LIV]-[CL]-[ST] FT BINDING 515..516 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Condition: S-R FT BINDING 521..525 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Condition: x(2)-Y-V-Q FT BINDING 132 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [DE] FT BINDING 350 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: R FT BINDING 460 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Condition: T FT BINDING 558 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Optional; Condition: D FT BINDING 596 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: W XX Size: 575-688; Related: None; Template: Q12181; Q9UHB4; Q6NPS8; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.11 2022/11/19 //