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HAMAP rule MF_03178

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_03178
Accession MF_03178
Dates 24-JUL-2013 (Created)
03-SEP-2024 (Last updated, Version 13)
Name NDOR1
Scope(s) Eukaryota
Template(s) Q12181; Q9UHB4; Q6NPS8; [ Recover all ]
Triggered by HAMAP; MF_03178 (Get profile general information and statistics)

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 Name=TAH18;
else case <OC:Vertebrata>
Gene name Name=NDOR1;
end case

Comments [?]

case <OC:Fungi>
FUNCTIONNADPH-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.
SUBUNITInteracts with @gn(DRE2); as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
SUBCELLULAR LOCATIONCytoplasm. Mitochondrion. Note=Relocalizes to mitochondria after H(2)O(2) exposure.
else case <OC:Vertebrata>
FUNCTIONNADPH-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.
SUBUNITInteracts with @gn(CIAPIN1); as part of the cytosolic iron- sulfur (Fe-S) protein assembly (CIA) machinery.
SUBCELLULAR LOCATIONCytoplasm, perinuclear region. Note=Concentrated in perinuclear structure.
else
FUNCTIONNADPH-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 LOCATIONCytoplasm.
end case
CATALYTIC ACTIVITY Reaction=2 oxidized [2Fe-2S]-[protein] + NADPH = 2 reduced [2Fe-2S]- [protein] + NADP(+) + H(+); 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;
SIMILARITYBelongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
SIMILARITYIn the N-terminal section; belongs to the flavodoxin family.
SIMILARITYIn 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 <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 [?]

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 [?]

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 [?]

Size range 575-688 amino acids
Related rules None
Fusion Nter: None Cter: None



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