Protein Family Models

This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 (Swiss:Q9X9W3) is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue. [1]. 12625841. New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3. (from Pfam)

Date:

2024-10-16

This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin [1]. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalysed by SnaA, SnaB heterodimer [2]. This flavin reductase region characterised by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain [1]. [1]. 7665509. Cloning and analysis of structural genes from Streptomyces pristinaespiralis encoding enzymes involved in the conversion of pristinamycin IIB to pristinamycin IIA (PIIA): PIIA synthase and NADH:riboflavin 5'-phosphate oxidoreductase. Blanc V, Lagneaux D, Didier P, Gil P, Lacroix P, Crouzet J;. J Bacteriol 1995;177:5206-5214. [2]. 9287340. An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning, analysis, and overexpression. Parry RJ, Li W;. J Biol Chem 1997;272:23303-23311. (from Pfam)

Date:

2024-10-16