Flavodoxin/nitric oxide synthase
IPR008254
Definition
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:1.14.13.39]) 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 [[cite:PMID:8160268], [cite:PMID:7756978]]. 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 [[cite:PMID:9237990], [cite:PMID:10048323], [cite:PMID:10610791]]. The FMN is positioned at the tip of the C-terminal side of the β-sheet PMID:9237990. 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 PMID:7756978.
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...