UniProt functional annotation for P16083

UniProt code: P16083.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
 
Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. {ECO:0000269|PubMed:18254726}.
 
Catalytic activity: Reaction=1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone + H(+) = a quinol + beta-nicotinamide D-riboside; Xref=Rhea:RHEA:12364, ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:24646, ChEBI:CHEBI:55458, ChEBI:CHEBI:132124; EC=1.10.5.1; Evidence={ECO:0000269|PubMed:18579530};
Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
Cofactor: Name=FAD; Xref=ChEBI:CHEBI:57692;
Activity regulation: Inhibited by melatonin, resveratrol and 5- hydroxytryptamine. {ECO:0000269|PubMed:18254726}.
Biophysicochemical properties: Kinetic parameters: KM=28 uM for NRH {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528}; KM=11.6 uM for menadione {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528}; KM=252 uM for NADH {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528};
Subunit: Homodimer. {ECO:0000269|PubMed:15350128, ECO:0000269|PubMed:16129418, ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722}.
Subcellular location: Cytoplasm.
Miscellaneous: Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.
Similarity: Belongs to the NAD(P)H dehydrogenase (quinone) family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.