A0A7J7EYJ5 · A0A7J7EYJ5_DICBM
- ProteinNADPH-dependent diflavin oxidoreductase 1
- GeneNDOR1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids838 (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 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 CISD1 and activate this protein implicated in Fe/S cluster repair.
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 | 12-17 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SQTGTA | ||||||
Binding site | 59-62 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATTG | ||||||
Binding site | 97-106 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGDSSYAKFN | ||||||
Binding site | 132 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 350 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 382-385 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RAFS | ||||||
Binding site | 409-412 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GLCS | ||||||
Binding site | 460 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 515-516 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 521-525 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KVYVQ | ||||||
Binding site | 558 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | metal ion 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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7EYJ5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Concentrated in perinuclear structure.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 803-833 | Helical | ||||
Sequence: LALLGLLALELLGLLLIFTPLVLLGLLFMLL |
Keywords
- Cellular component
Interaction
Subunit
Interacts with CIAPIN1; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-150 | Flavodoxin-like | ||||
Sequence: LLVLFGSQTGTAQDVSDRLGREARRRRLGCLVQALDSYPVVNLINEPLVIFICATTGQGDPPDNMKNFWRFIFRKNLPSTSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGRALLPVCLGDDQHELGPDAAVDPWLHDLW | ||||||
Domain | 206-447 | FAD-binding FR-type | ||||
Sequence: LQPFLAPMVTNQRVTGPLHFQDVRLIEFDITGSGLSFAAGDVVLIQPENAAGHVQQFCQVLGLDPDQYFTLQPQEPGVPRPARLPQPCSVRHLVSRYLDIASVPRRSFFELLACLSPHELEREKLLEFSSAQGQEELCEYCSRPRRTILEVLGDFPHTAGAIPPDYLLDLIPLMRPRAFSIASSLLILVAVVQYQTRLKEPRRGLCSSWLASLDPRQGDPGTLAGPVQVPLWVRPGGLTFPE | ||||||
Domain | 664-713 | RING-type | ||||
Sequence: CPVCTEPYGPGEHRLALLNCGHGLCVGCLHRLLGTAPSADLGRVRCPLCR | ||||||
Region | 730-755 | Disordered | ||||
Sequence: XXXXDGPQRPPPPTPPTPPRRGPGPW | ||||||
Compositional bias | 735-752 | Pro residues | ||||
Sequence: GPQRPPPPTPPTPPRRGP |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length838
- Mass (Da)92,730
- Last updated2021-04-07 v1
- Checksum90B3E26540A91FF3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 735-752 | Pro residues | ||||
Sequence: GPQRPPPPTPPTPPRRGP |
Keywords
- Technical term