NDOR1

NADPH dependent diflavin oxidoreductase 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4H2D​
Identifiers
Symbols	NDOR1 ; NR1; bA350O14.9
External IDs	OMIM: 606073 MGI: 1926047 HomoloGene: 7144 GeneCards: NDOR1 Gene
EC number	1.6.-.-
Gene ontology Molecular function • NADPH-hemoprotein reductase activity • iron ion binding • protein binding • FMN binding • oxidoreductase activity • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen • flavin adenine dinucleotide binding • NADP binding Cellular component • nucleus • cytoplasm • cytosol • intermediate filament cytoskeleton • perinuclear region of cytoplasm Biological process • cell death • iron-sulfur cluster assembly • cellular response to menadione • small molecule metabolic process • oxidation-reduction process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27158	78797
Ensembl	ENSG00000188566	ENSMUSG00000006471
UniProt	Q9UHB4	A2AI05
RefSeq (mRNA)	NM_001144026	NM_001082476
RefSeq (protein)	NP_001137498	NP_001075945
Location (UCSC)	Chr 9: 137.21 – 137.22 Mb	Chr 2: 25.24 – 25.26 Mb
PubMed search

NADPH-dependent diflavin oxidoreductase 1 is an enzyme that in humans is encoded by the NDOR1 gene.^[1][2][3]

References

1. Paine MJ, Garner AP, Powell D, Sibbald J, Sales M, Pratt N, Smith T, Tew DG, Wolf CR (Feb 2000). "Cloning and characterization of a novel human dual flavin reductase". J Biol Chem 275 (2): 1471–8. doi:10.1074/jbc.275.2.1471. PMID 10625700.
2. Finn RD, Basran J, Roitel O, Wolf CR, Munro AW, Paine MJ, Scrutton NS (Mar 2003). "Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1". Eur J Biochem 270 (6): 1164–75. doi:10.1046/j.1432-1033.2003.03474.x. PMID 12631275.
3. "Entrez Gene: NDOR1 NADPH dependent diflavin oxidoreductase 1".

Further reading

• Kwasnicka DA, Krakowiak A, Thacker C, et al. (2003). "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1.". J. Biol. Chem. 278 (40): 39051–8. doi:10.1074/jbc.M306355200. PMC 2556063. PMID 12871939.
• Olteanu H, Banerjee R (2003). "Redundancy in the pathway for redox regulation of mammalian methionine synthase: reductive activation by the dual flavoprotein, novel reductase 1.". J. Biol. Chem. 278 (40): 38310–4. doi:10.1074/jbc.M306282200. PMID 12871938.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995). "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.". Science 269 (5231): 1737–40. doi:10.1126/science.7569905. PMID 7569905.