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HAMAP rule MF_03178

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General rule information [?]

Accession MF_03178
Dates 24-JUL-2013 (Created)
19-NOV-2022 (Last updated, Version 11)
Name NDOR1
Scope
Eukaryota
Templates Q12181 (NDOR1_YEAST); Q9UHB4 (NDOR1_HUMAN); Q6NPS8 (NDOR1_ARATH): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
NDOR1
Protein name
RecName: Full=NADPH-dependent diflavin oxidoreductase 1;
EC 1.18.1.-;
AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase;
case <OC:Fungi>
Gene name
TAH18
else case <OC:Vertebrata>
Gene name
NDOR1
end case

Comments [?]

case <OC:Fungi>
Function NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of @gn(DRE2), another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death.
Subunit Interacts with @gn(DRE2); as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
Subcellular location Cytoplasm. Mitochondrion. Note=Relocalizes to mitochondria after H(2)O(2) exposure.
else case <OC:Vertebrata>
Function NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of @gn(CIAPIN1), another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of @gn(CISD1) and activate this protein implicated in Fe/S cluster repair.
Subunit Interacts with @gn(CIAPIN1); as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
Subcellular location Cytoplasm, perinuclear region. Note=Concentrated in perinuclear structure.
else
Function NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of the anamorsin/DRE2 homolog, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins.
Subcellular location Cytoplasm.
end case
Catalytic activity RHEA:67716: NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]
PhysiologicalDirection=left-to-right (RHEA:67717)
Cofactor FAD
FMN
Similarity Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
In the N-terminal section; belongs to the flavodoxin family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Keywords [?]

case <OC:Fungi>
Mitochondrion
end case
Cytoplasm
FAD
Flavoprotein
FMN
NADP
Oxidoreductase

Gene Ontology [?]

case <OC:Fungi>
GO:0005739; Cellular component: mitochondrion.
else case <OC:Vertebrata>
GO:0048471; Cellular component: perinuclear region of cytoplasm.
end case
GO:0005737; Cellular component: cytoplasm.
GO:0050660; Molecular function: flavin adenine dinucleotide binding.
GO:0010181; Molecular function: FMN binding.
GO:0050661; Molecular function: NADP binding.
GO:0016651; Molecular function: oxidoreductase activity, acting on NAD(P)H.
GO:0016226; Biological process: iron-sulfur cluster assembly.

Cross-references [?]

PROSITE PS51384; FAD_FR; 1; trigger=PRU00716;
PS50902; FLAVODOXIN_LIKE; 1;
Pfam PF00667; FAD_binding_1; 1;
PF00258; Flavodoxin_1; 1;
PF00175; NAD_binding_1; 1;
PRINTS PR00369; FLAVODOXIN; 1;
PR00371; FPNCR; 1;

Features [?]

From: NDOR1_HUMAN (Q9UHB4)
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     6     150       Flavodoxin-like        
BINDING     12     17       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [ST]-[QE]-[ST]-G-[TN]-[AS]  
BINDING     59     62       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [AS]-T-x-G  
BINDING     97     106       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [LIVC]-G-D-[ST]-[ST]-Y-x-[KR]-[FY]-[NC]  
BINDING     382     385       /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692     R-x-[FY]-S  
BINDING     416     419       /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692     G-[LIV]-[CL]-[ST]  
BINDING     515     516       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     S-R  
BINDING     521     525       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     x(2)-Y-V-Q  
BINDING     132     132       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [DE]  
BINDING     350     350       /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692     R  
BINDING     460     460       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     T  
BINDING (Optional)     558     558       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     D  
BINDING     596     596       /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692     W  

Additional information [?]

Size range 575-688 amino acids
Related rules None
Fusion None


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