AdoMet_dc

• PFAM accession number: PF02675
• Interpro abstract (IPR003826):

  Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in a large number of cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein [ (PUBMED:2197977) (PUBMED:10047786) ]. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme [ (PUBMED:11526206) (PUBMED:10844697) ].

  This entry represents the prokaryotic AdoMetDC family, which includes S-adenosylmethionine decarboxylase and arginine decarboxylase proenzymes [ (PUBMED:18650422) ].

• GO process: spermidine biosynthetic process (GO:0008295)
• GO function: adenosylmethionine decarboxylase activity (GO:0004014)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AdoMet_dc