Pyridoxamine 5'-phosphate oxidase-like, FMN-binding domain (IPR011576)

Short name: Pyridox_Oxase_FMN-bd

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 the FMN-binding domain present in pyridoxamine 5'-phosphate oxidases, as well as in a number of proteins that have not been demonstrated to have enzymatic activity. The FMN-binding domain has a structure consisting of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. PNPOx has a different dimerisation mode than that found in flavin reductases, which also carry an FMN-binding domain with a similar topology.

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0010181 FMN binding
GO:0004733 pyridoxamine-phosphate oxidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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