Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminal (IPR019576)

Short name: Pyridoxamine_oxidase_dimer_C

Overlapping homologous superfamilies

Domain relationships



Pyridoxamine 5'-phosphate oxidase (EC: is an enzyme that is involved in the de novo synthesis of pyridoxine (vitamin B6) and pyridoxal phosphate. It oxidizes pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P. The enzyme requires the presence of flavin mononucleotide (FMN) as a cofactor, although there is some evidence that coenzyme F420 may perform this role in some species [PMID: 20675471].

The sequences of the enzyme from bacterial (genes pdxH or fprA) [PMID: 1356963] and fungal (gene PDX3) [PMID: 7896706] sources show that this protein has been highly conserved throughout evolution. PdxH is evolutionary related [PMID: 8586283] to one of the enzymes in the phenazine biosynthesis protein pathway, phzD (also known as phzG).

This entry represents one of the two dimerisation regions of the protein, located at the edge of the dimer interface, at the C terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule [PMID: 10903950]. To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both PF01243 and PF10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity [PMID: 26327315].

Contributing signatures

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