Domain

FAD synthetase (IPR015864)

Short name: FAD_synthase

Domain relationships

None.

Description

Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (EC:2.7.1.26), which converts it into FMN, and FAD synthetase (EC:2.7.7.2), 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 [PMID: 14580199], the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family [PMID: 17049878]. 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 [PMID: 12517446].

This entry represents prokaryotic-type FAD synthetase, which occurs primarily as part of a bifunctional enzyme.

GO terms

Biological Process

GO:0009231 riboflavin biosynthetic process

Molecular Function

GO:0003919 FMN adenylyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam