HMM Summary Page: TIGR04479

Functionradical SAM P-methyltransferase, PhpK family
Gene SymbolphpK
Trusted Cutoff600.00
Domain Trusted Cutoff600.00
Noise Cutoff400.00
Domain Noise Cutoff400.00
Isology Typesubfamily
EC Number2.1.-.-
HMM Length504
AuthorHaft DH
Entry DateSep 9 2013 12:15PM
Last ModifiedSep 9 2013 12:15PM
CommentCharacterized members of this family are B12-binding domain/radical SAM domain enzymes that use methylcobalamin as a methyl donor to methylate a phosphorous atom during the biosynthesis of natural products such as bialaphos and phosalacine. These syntheses create an extremely rare C-P-C bond. All members of the seed alignment derive from genomic regions that include a non-ribosomal peptide synthase. Note that a single organism, Pelosinus fermentans JBW45 from Cr(VI)-contaminated groundwater, has eight additional homologs of unknown function that score between trusted and noise cutoffs of this model.
ReferencesRN [1] RM PMID:21950770 RT In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea. RA Werner WJ, Allen KD, Hu K, Helms GL, Chen BS, Wang SC RL Biochemistry. 2011 Oct 25;50(42):8986-8. doi: 10.1021/bi201220r. RN [2] RM PMID:7789803 RT Sequence of a P-methyltransferase-encoding gene isolated from a bialaphos-producing Streptomyces hygroscopicus. RA Hidaka T, Hidaka M, Kuzuyama T, Seto H RL Gene. 1995 May 26;158(1):149-50.