Aminomethyltransferase-like (IPR028896)

Short name: GCST/YgfZ/DmdA

Overlapping homologous superfamilies

Family relationships


Dimethlysulfonioproprionate (DMS) is catabolised in marine bacterioplankton through a pathway in which the initial step involves demethylation to methylmercaptopropionate (MMPA), which is then further catabolised to methane thiol and acetate. The enzyme responsible for the first step is dimethylsulfonioproprionate demethylase DmdA [PMID: 21562561, PMID: 21886640].

The overall fold of DmdA is not similar to other enzymes that typically utilise the cofactor tetrahydrofolate (THF). Instead DmdA has a triple domain structure similar to that observed for the glycine cleavage T protein [PMID: 22162093]. Glycine cleavage T protein is an aminomethyltransferase EC: which is part of the glycine cleavage complex responsible for the reversible oxidation of glycine [PMID: 20375021].

This entry also includes YgfZ, which is a folate-binding protein [PMID: 15489424] involved in regulating the level of ATP-dnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication [PMID: 16359333].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.