A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer.
Biosynthesis of flavin adenine dinucleotides in most prokaryotes is catalyzed by a family of bifunctional flavin adenine dinucleotide (FAD) synthetases. These enzymes carry out the dual functions of phosphorylation of flavin mononucleotide (FMN) and its subsequent adenylylation to generate FAD. Using various sequence analysis methods, a new domain has been identified in the N-terminal region that is well conserved in all the bacterial FAD synthetases. We also identify remote similarity of this domain to the nucleotidyl transferases and, hence, this domain is suggested to be invloved in the adenylylation reaction of FAD synthetases.
Krupa
Ananth
A
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Sandhya
Kumaraswamy
K
Srinivasan
Narayanaswamy
N
Jonnalagadda
Sobhanaditya
S
D000595:Amino Acid Sequence; D002384:Catalysis; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism*; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D009711:Nucleotides; D009713:Nucleotidyltransferases; C020143:FMN adenylyltransferase