v5.1.0.3
Cicer data from the Legume Information System
Type | Homologous_superfamily |
Description | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including cobalamin (vitamin B12), haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [].These enzymes catalyse the methylation of their substrates using S-adenosyl-L-methionine as a methyl source. Enzymes in this family include:Uroporphyrinogen III methyltransferase ( ) (SUMT), which catalyses the conversion of uroporphyrinogen III to precorrin-2 at the first branch-point of the tetrapyrrole synthesis pathway, directing the pathway towards cobalamin or sirohaem synthesis [ ].Precorrin-2 C20-methyltransferase CobI/CbiL ( ), which introduces a methyl group at C-20 on precorrin-2 to produce precorrin-3A during cobalamin biosynthesis. This reaction is key to the conversion of a porphyrin-type tetrapyrrole ring to a corrin ring [ ]. In some species, this enzyme is part of a bifunctional protein.Precorrin-4 C11-methyltransferase CobM/CbiF ( ), which introduces a methyl group at C-11 on precorrin-4 to produce precorrin-5 during cobalamin biosynthesis [ ].Sirohaem synthase CysG ( ), domains 4 and 5, which synthesizes sirohaem from uroporphyrinogen III, at the first branch-point in the tetrapyrrole biosynthetic pathway, directing the pathway towards sirohaem synthesis [ ].Diphthine synthase ( ), which carries out the methylation step during the modification of a specific histidine residue of elongation factor 2 (EF-2) during diphthine synthesis. This entry represents a tetrapyrrole methylase domain, which consist of two non-similar subdomains [ ]. The first domain has parallel sheet of five strands,while the second domain has mixed sheet of five strands, with strands 4 and 5 antiparallel to the rest. |
Short Name | 4pyrrol_Methylase_sf |