Protein Domain : S-adenosylmethionine decarboxylase, core IPR016067

Type  Homologous_superfamily
Description  S-adenosylmethionine decarboxylase (AdoMetDC) [ ] catalyzes the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine.The catalytic mechanism of AdoMetDC involves a covalently-bound pyruvoyl group. This group is post-translationally generated by a self-catalyzed intramolecular proteolytic cleavage reaction between a glutamate and a serine. This cleavage generates two chains, beta (N-terminal) and alpha (C-terminal). The N-terminal serine residue of the alpha chain is then converted by nonhydrolytic serinolysis into a pyruvyol group.
Short Name  S-AdoMet_deCO2ase_core

0 Child Features

2 Gene Families

458 Genes

2 Ontology Annotations

0 Parent Features

14 Publications

USDA
InterMine logo
The Legume Information System (LIS) is a research project of the USDA-ARS:Corn Insects and Crop Genetics Research in Ames, IA.
LegumeMine || ArachisMine | CicerMine | GlycineMine | LensMine | LupinusMine | PhaseolusMine | VignaMine | MedicagoMine
InterMine © 2002 - 2022 Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, United Kingdom