Pyridoxamine 5'-phosphate oxidase, putative (IPR011576)

Short name: Pyridox_Oxase_put

Overlapping homologous superfamilies

Domain relationships



Pyridoxamine 5'-phosphate oxidase (PNPOx; EC: is a FMN flavoprotein that catalyses the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This reaction serves as the terminal step in the de novo biosynthesis of PLP in Escherichia coli and as a part of the salvage pathway of this coenzyme in both E. coli and mammalian cells [PMID: 12686112, PMID: 12824491]. The binding sites for FMN and for substrate have been highly conserved throughout evolution.

This entry represents a domain with putative PNPOx (Pyridoxamine 5'-phosphate oxidase) function. The domain was initially predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both PF01243 and PF10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown [PMID: 26327315].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.