Molybdopterin cofactor biosynthesis MoaD-related, C-terminal (IPR015272)

Short name: Mopterin_CF_MoaD-rel_C

Overlapping homologous superfamilies

Domain relationships



In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis. Proteins are found in Thermus thermophilus, including threonine synthase (EC:, which catalyses the conversion of O-phospho-L-homoserine to L-threonine and phosphate.

MoaD-related proteins have an N-terminal MoaD domain, with a fold similar to that of ubiquitin, and contain a highly conserved C-terminal Gly-Gly motif, which in its active form contains a transferrable sulphur in the form of a thiocarboxylate group [PMID: 17223713]. This entry represents the domain found at the C terminus, which consists of a TBP-like fold of beta/alpha/beta(4)/alpha.

Contributing signatures

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