A0A3M2SBR5 · A0A3M2SBR5_9HYPO
- ProteinNADPH-dependent diflavin oxidoreductase 1
- GeneTAH18
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids603 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- NADPH + 2 oxidized [2Fe-2S]-[protein] = H+ + NADP+ + 2 reduced [2Fe-2S]-[protein]
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14-19 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SETGNA | ||||||
Binding site | 61-64 | FMN (UniProtKB | ChEBI) | ||||
Sequence: STTG | ||||||
Binding site | 99-108 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGDSTYLKFN | ||||||
Binding site | 134 | FMN (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 358 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 388-391 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RDFS | ||||||
Binding site | 429-432 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GLCS | ||||||
Binding site | 472 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 528-529 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 534-538 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KIYVQ | ||||||
Binding site | 598 | 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 > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium solani species complex
Accessions
- Primary accessionA0A3M2SBR5
Proteomes
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-152 | Flavodoxin-like | ||||
Sequence: VLILYGSETGNAQDMAEELGRVCQRLHFKSRVEELDAVDLNALLQHRFVIFVISTTGQGDMPHNSLLFWKRLLRKKLPPGCLSSVQYTTFGLGDSTYLKFNWAARKLNRRLEQLGATTFIESFEADEQFPDGIDGSFVRWSETLS | ||||||
Domain | 210-465 | FAD-binding FR-type | ||||
Sequence: PNGWTATLADNVRFTPETHWQDVRLVSFDIPKRDGVKLQCNPGDCLTIYPKNFPQDAQKLITLMGWDDIADKPLDLSLCDSLPQNLYIDPKCTLREIILNNIDFTAIPRRSFLKSMSYFSTNPGHKERLLEFTMTEYLDEYFDYATRSRRSILEVLEEFTSVKLPAERVLDIFPLIRGRDFSIANGGMKLKHPTNEDITRVELLVALVKYRTILRKPRQGLCSRYLENLPAGSSLTVTHKPVLSPIHGPQNAQRPL |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length603
- Mass (Da)68,516
- Last updated2019-02-13 v1
- Checksum09010F4B17C23C75
Keywords
- Technical term