Protein Family Models

Family member FomD is a protein encoded in the fosfomycin biosynthesis gene cluster [1,2], which hydrolyses (S)-HPP-CMP to give (S)-HPP and CMP in the presence of Mn2 or Co2 [2]. FomD also hydrolyses cytidylyl 2-hydroxyethylphosphonate (HEP-CMP), which is a biosynthetic intermediate before C-methylation. FomD structure revealed that it has a beta-barrel fold consisting of a large twisted antiparallel beta-sheet, a key feature of DUF402-containing proteins. The function of this domain is unknown. It has a Tyr residue which activates a water molecule to promote nucleophilic attack on the phosphorus atom of the phosphonate moiety [2]. This domain has also been found in Ntdp (nucleoside tri- and diphosphatase, also known as Sa1684) from Staphylococcus aureus [3]. [1]. 7500951. Cloning and nucleotide sequence of fosfomycin biosynthetic genes. of Streptomyces wedmorensis.. Hidaka T, Goda M, Kuzuyama T, Takei N, Hidaka M, Seto H;. Mol Gen Genet 1995;249:274-280.. [2]. 30010320. Biochemical and Structural Analysis of FomD That Catalyzes the. Hydrolysis of Cytidylyl ( S)-2-Hydroxypropylphosphonate in. Fosfomycin Biosynthesis.. Sato S, Miyanaga A, Kim SY, Kuzuyama T, Kudo F, Eguchi T;. Biochemistry. 2018;57:4858-4866.. [3]. 33955674. The structural mechanism for the nucleoside tri- and diphosphate. hydrolysis activity of Ntdp from Staphylococcus aureus.. Wang Z, Shen H, He B, Teng M, Guo Q, Li X;. FEBS J. 2021;288:6019-6034. (from Pfam)

Date:

2024-08-14

uncharacterized DUF402 domain-containing protein similar to Bacillus subtilis YgaC

Date:

2017-11-08

Date:

2020-10-26