A0A1J9PP55 · A0A1J9PP55_9EURO
- ProteinNADPH-dependent diflavin oxidoreductase 1
- GeneTAH18
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids662 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
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 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 H2O2-induced cell death.
Catalytic activity
- 2 oxidized [2Fe-2S]-[protein] + NADPH = 2 reduced [2Fe-2S]-[protein] + NADP+ + H+
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23-28 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SETGNS | ||||||
Binding site | 70-73 | FMN (UniProtKB | ChEBI) | ||||
Sequence: STTG | ||||||
Binding site | 108-117 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGDSSYPKFN | ||||||
Binding site | 143 | FMN (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 383 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 413-416 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RQFS | ||||||
Binding site | 460-463 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVCT | ||||||
Binding site | 502 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 571-572 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 577-581 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KVYVQ | ||||||
Binding site | 662 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | NADP binding | |
Molecular Function | NADPH-hemoprotein reductase activity | |
Biological Process | iron-sulfur cluster assembly |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent diflavin oxidoreductase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Ajellomycetaceae > Emergomyces
Accessions
- Primary accessionA0A1J9PP55
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Relocalizes to mitochondria after H2O2 exposure.
Keywords
- Cellular component
Interaction
Subunit
Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-161 | Flavodoxin-like | ||||
Sequence: SIILYGSETGNSQDVADELGRLTERLHFSTRVCELNAIKAESLNEYDVVIFAVSTTGQGDFPANARVFWKSLLLKKLPPTFLRGVKFALFGLGDSSYPKFNWASRKLYKRLLQLGAYELYPCGEADEQHPEGLEGTFVPWSLDLR | ||||||
Region | 190-228 | Disordered | ||||
Sequence: KHRDPSSMEGTNRYPGAGSKEQLEDARDPSYFSQDPRPI | ||||||
Domain | 229-491 | FAD-binding FR-type | ||||
Sequence: PNTVTATLAANNRLTPQTHWQDVRHLILTIPESIRYVPGDILHITPRNFAADVNSLISIMGWEKDADTPLCFVPNVQHVSASNTSSPEIPFLLNSPGFTLRNLLTDYLDIMAIPRRSFFSHIAHFSDDAMHRDRLLEFTNPEYIDEFYDYTSRPRRSILEVLHEFESVKIPWHLVCTVFPVLRGRQFSLASGGNLKTPESLPGRHATGAGTRFDLLVAIVKYQTVIKKTREGVCTRYLAVLRPGSTLKVQVQKGGLNSSMRQL |
Sequence similarities
Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
In the N-terminal section; belongs to the flavodoxin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length662
- Mass (Da)74,779
- Last updated2017-02-15 v1
- ChecksumB2F6D566E91AB8E0
Keywords
- Technical term