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(s) |
Eukaryota |
Template(s) | Q12181 (NDOR1_YEAST); Q9UHB4 (NDOR1_HUMAN); Q6NPS8 (NDOR1_ARATH); [ Recover all ] |
Triggered by |
HAMAP; MF_03178 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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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 | Name=TAH18; |
else case <OC:Vertebrata> | |
Gene name | Name=NDOR1; |
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 | Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA- COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717; |
COFACTOR | Name=FAD; Xref=ChEBI:CHEBI:57692; |
COFACTOR | Name=FMN; Xref=ChEBI:CHEBI:58210; |
SIMILARITY | Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family. |
SIMILARITY | In the N-terminal section; belongs to the flavodoxin family. |
SIMILARITY | In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. |
Keywords
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case <OC:Fungi> | |
Mitochondrion | |
end case | |
Cytoplasm | |
FAD | |
Flavoprotein | |
FMN | |
NADP | |
Oxidoreductase |
Gene Ontology
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case <OCellular component:Fungi> | |
GO:0005739; Cellular component:mitochondrion | |
else case <OCellular component: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
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PROSITE | PS51384; FAD_FR; 1; |
PROSITE | PS50902; FLAVODOXIN_LIKE; 1; |
Pfam | PF00667; FAD_binding_1; 1; |
Pfam | PF00258; Flavodoxin_1; 1; |
Pfam | PF00175; NAD_binding_1; 1; |
PRINTS | PR00369; FLAVODOXIN; 1; |
PRINTS | PR00371; FPNCR; 1; |
Features
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From: NDOR1_HUMAN (Q9UHB4) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | 6 | 150 | /note="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 | 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 | Nter: None Cter: None |