1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR029063 | Domain | S-adenosyl-L-methionine-dependent methyltransferase |
| Type: | Domain | Name: | Polyamine biosynthesis domain |
| Description: | The nearly ubiquitous polyamines (putrescine, spermidine and spermine) are polycationic mediators of cell proliferation and differentiation whosefunctions likely provide both stability and neutralisation for nucleic acids. The following polyamine biosynthetic enzymes are evolutionary related andcontain a polyamine biosynthesis (PABS) domain []:Spermidine synthase () (putrescine aminopropyltransferase). It catalyses the last step in the biosynthesis of spermidine from arginine and methionine; the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor.Spermine synthase () (spermidine aminopropyltransferase). It converts spermidine into spermine using decarboxylated S-adenosylmethionine as the cofactor.Putrescine N-methyltransferase (). It catalyses a step in the biosynthesis of nicotine in plants; the methylation of putrescine to N-methylputrescine using S-adenosylmethionine as the cofactor.The PABS domain consists of two subdomains: an N-terminal subdomain composed of six beta-strands, and a Rossmann-like C-terminal subdomain. The larger C-terminal catalytic core subdomain consists of aseven-stranded beta-sheet flanked by nine alpha helices. This subdomain resembles a topology observed in a number of nucleotide and dinucleotide-binding enzymes, and in S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases (MTases) [].This entry represents the PABS domain that includes the two subdomains. | Short Name: | PABS |
| DB identifier | Type | Name |
|---|---|---|
| IPR029063 | Domain | S-adenosyl-L-methionine-dependent methyltransferase |
