HMM Summary Page: TIGR04539

FunctiontRNA-dependent cyclodipeptide synthase
Trusted Cutoff45.00
Domain Trusted Cutoff45.00
Noise Cutoff34.00
Domain Noise Cutoff34.00
Isology Typesubfamily
HMM Length220
AuthorHaft DH
Entry DateJun 4 2014 4:58PM
Last ModifiedSep 16 2014 4:02PM
CommentMembers of this family take two aminoacylated tRNA molecules and produce a cyclic dipeptide with two peptide bonds. This enzyme therefore produces a type of nonribosomal peptide, but by a mechanism entirely different from the typical non-ribosomal peptide synthase (NRPS) that relies on adenylation to activate amino acids. Three characterized members of this family are the cyclodityrosine synthase of Mycobacterium tuberculosis (an essential gene), a cyclo(L-Phe-L-Leu) synthase from Streptomyces noursei involved in natural product biosynthesis, and cyclodileucine synthase YvmC from Bacillus licheniformis. Many cyclodipeptide synthases are found next to a cytochrome P450 that further modifies the product.
ReferencesRN [1] RM PMID:20852636 RT The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. RA Vetting MW, Hegde SS, Blanchard JS RL Nat Chem Biol. 2010 Nov;6(11):797-9. doi: 10.1038/nchembio.440. RN [2] RM PMID:21325056 RT Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog. RA Bonnefond L, Arai T, Sakaguchi Y, Suzuki T, Ishitani R, Nureki O RL Proc Natl Acad Sci U S A. 2011 Mar 8;108(10):3912-7. doi:10.1073/pnas.1019480108. RN [3] RM PMID:21296757 RT Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis. RA Sauguet L, Moutiez M, Li Y, Belin P, Seguin J, Le Du MH, Thai R, Masson C, Fonvielle M, Pernodet JL, Charbonnier JB, Gondry M RL Nucleic Acids Res. 2011 May;39(10):4475-89. doi: 10.1093/nar/gkr027.