| Description | 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 [ ] and are functionally interchangeable with ferredoxins. They have been isolated from prokaryotes, cyanobacteria, and some eukaryotic algae. Nitric oxide synthase () produces nitric oxide from L-arginine and NADPH. Nitric oxide acts as a messenger molecule in the body. The flavodoxin-like domain is an around 170-residue domain with a flavin mononucleotide (FMN)-binding site. It is involved in electron transfer reactions [, ].Structure analyses of several flavodoxin-like domains have shown that it is a wound α-β-α fold with a central 5-stranded parallel hydrophobic β-sheet flanked on either side by amphipathic α-helices [ , , ]. The FMN is positioned at the tip of the C-terminal side of the β-sheet []. The fold correlates with a highly conserved, repetitive sequence pattern in which hydrophobic residues cluster in β-strands and have a 3-4-residue periodicity in α-helices []. | Name | Flavodoxin/nitric oxide synthase |
| Short Name | Flavodoxin/NO_synth | Type | Domain |
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