Cobalamin-independent methionine synthase MetE, N-terminal (IPR013215)

Short name: Cbl-indep_Met_Synth_N

Overlapping homologous superfamilies

Domain relationships



Cobalamin-independent methionine synthase, MetE, catalyses the synthesis of the amino acid methionine by the transfer of a methyl group from methyltetrahydrofolate to homocysteine [PMID: 15326182]. The N-terminal and C-terminal domains of MetE together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilise a loop from the C-terminal domain.

GO terms

Biological Process

GO:0008652 cellular amino acid biosynthetic process

Molecular Function

GO:0003871 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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