Flavodoxin/nitric oxide synthase (IPR008254)

Short name: Flavodoxin/NO_synth

Overlapping homologous superfamilies

Domain relationships


The flavodoxin-like domain is an around 170-residue domain with a flavin mononucleotide (FMN)-binding site. It is involved in electron transfer reactions [PMID: 8160268, PMID: 7756978].

Structure analyses of several flavodoxin-like domains have shown that it is a wound alpha-beta-alpha fold with a central 5-stranded parallel hydrophobic beta-sheet flanked on either side by amphipathic alpha-helices [PMID: 9237990, PMID: 10048323, PMID: 10610791]. The FMN is positioned at the tip of the C-terminal side of the beta-sheet [PMID: 9237990]. The fold correlates with a highly conserved, repetitive sequence pattern in which hydrophobic residues cluster in beta-strands and have a 3-4-residue periodicity in alpha-helices [PMID: 7756978].

This domain is found in a number of proteins including flavodoxin and nitric-oxide synthase. Flavodoxins are electron-transfer proteins that function in various electron transport systems. They bind one FMN molecule, which serves as a redox-active prosthetic group [PMID: 2597140] and are functionally interchangeable with ferredoxins. They have been isolated from prokaryotes, cyanobacteria, and some eukaryotic algae. Nitric oxide synthase (EC: produces nitric oxide from L-arginie and NADPH. Nitric oxide acts as a messenger molecule in the body.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0010181 FMN binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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