Premium
Co‐evolution of HAD phosphatase and hotdog‐fold thioesterase domain function in the menaquinone‐pathway fusion proteins BF1314 and PG1653
Author(s) -
Wang Min,
Song Feng,
Wu Rui,
Allen Karen N.,
Mariano Patrick S.,
Dunaway-Mariano Debra
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.009
Subject(s) - thioesterase , chemistry , phosphatase , fold (higher order function) , fusion protein , fusion , function (biology) , biochemistry , microbiology and biotechnology , biology , enzyme , biosynthesis , gene , computer science , recombinant dna , linguistics , philosophy , programming language
The function of a Bacteroidetes menaquinone biosynthetic pathway fusion protein comprised of an N‐terminal haloacid dehalogenase (HAD) family domain and a C‐terminal hotdog‐fold family domain is described. Whereas the thioesterase domain efficiently catalyzes 1,4‐dihydroxynapthoyl‐CoA hydrolysis, an intermediate step in the menaquinone pathway, the HAD domain is devoid of catalytic activity. In some Bacteroidetes a homologous, catalytically active 1,4‐dihydroxynapthoyl‐CoA thioesterase replaces the fusion protein. Following the gene fusion event, sequence divergence resulted in a HAD domain that functions solely as the oligomerization domain of an otherwise inactive thioesterase domain.