InterPro : IPR015864

Name  FAD synthetase Short Name  FAD_synthase
Type  Domain 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 entry represents prokaryotic-type FAD synthetase, which occurs primarily as part of a bifunctional enzyme.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

2 Found In

Id Name Short Name Type
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain
IPR002606 Riboflavin kinase, bacterial Riboflavin_kinase_bac Family

0 Parent Features

3 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



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)