HAMAP rule MF_03178
General rule information
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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
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
case <OC:Fungi>
Gene name |
|
else case <OC:Vertebrata>
Gene name |
|
end case
Comments
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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
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case <OC:Fungi>
end case
Gene Ontology
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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.
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
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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
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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
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Size range | 575-688 amino acids |
Related rules | None |
Fusion | None |