The domain within your query sequence starts at position 13 and ends at position 350; the E-value for the FMN_dh domain shown below is 1.8e-127.



PFAM accession number:PF01070
Interpro abstract (IPR000262):

A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown [ (PUBMED:2324094) (PUBMED:2271624) (PUBMED:1939137) ] to be structurally related. These enzymes are:

  • Lactate dehydrogenase ( EC ), which consists of a dehydrogenase domain and a haem-binding domain called cytochrome b2 and which catalyses the conversion of lactate into pyruvate.
  • Glycolate oxidase ( EC ) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyses the conversion of glycolate and oxygen to glyoxylate and hydrogen peroxide.
  • Long chain alpha-hydroxy acid oxidase from rat ( EC ), a peroxisomal enzyme.
  • Lactate 2-monooxygenase ( EC ) (lactate oxidase) from Mycobacterium smegmatis, which catalyses the conversion of lactate and oxygen to acetate, carbon dioxide and water.
  • (S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyses the reduction of (S)-mandelate to benzoylformate.

The first step in the reaction mechanism of these enzymes is the abstraction of the proton from the alpha-carbon of the substrate producing a carbanion which can subsequently attach to the N5 atom of FMN. A conserved histidine has been shown [ (PUBMED:2644287) ] to be involved in the removal of the proton. The region around this active site residue is highly conserved and contains an arginine residue which is involved in substrate binding.

GO function:oxidoreductase activity (GO:0016491)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FMN_dh