InterPro : IPR012183

Name  FAD synthetase, molybdopterin binding Short Name  FAD_synth_Mopterin-bd
Type  Family Description  Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (), which converts it into FMN, and FAD synthetase (), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme [], the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family []. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases [].This group represents a predicted FAD synthetase with a molybdopterin binding domain. It requires magnesium as a cofactor and is highly specific for ATP as a phosphate donor []. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates []. This entry includes the eukaryotic enzymes.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

3 Contains

Id Name Short Name Type
IPR001453 Molybdopterin binding domain Mopterin-bd_dom Domain
IPR002500 Phosphoadenosine phosphosulphate reductase PAPS_reduct Domain
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Krupa A A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. 2003 Trends Biochem Sci 28 9-12
Karthikeyan S Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. 2003 Biochemistry 42 12532-8
Galluccio M Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase. 2007 Protein Expr Purif 52 175-81
Brizio C Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase. 2006 Biochem Biophys Res Commun 344 1008-16
Sandoval FJ An FMN hydrolase is fused to a riboflavin kinase homolog in plants. 2005 J Biol Chem 280 38337-45

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)