PurM-like, N-terminal domain (IPR016188)

Short name: PurM-like_N

Overlapping homologous superfamilies

Domain relationships



This entry represents a structural domain with a core structure consisting of beta-alpha-beta-alpha-beta(2), which is found in two enzymes of the purine biosynthetic pathway: at the N-terminal of aminoimidazole ribonucleotide (AIR) synthetase (PurM) [PMID: 10508786], as well as the N1 and N2 domains of formylglycinamide ribonucleotide (FGAR) amidotransferase (PurL) (PurM-like module) [PMID: 15301531]. PurM and PurL utilise ATP to activate the oxygen of an amide within their substrate toward nucleophilic attack by a nitrogen. PurM uses the product of PurL, formylglycinamidine ribonucleotide (FGAM) and ATP to make AIR, ADP and P(i). It is also found as domains 1 and 3 in phosphoribosylformylglycinamidine synthase II (smPurL) (EC: (carries a duplication: tandem repeats of two PurM-like units arranged like the PurM subunits in the dimer) [PMID: 16544324].

This domain is also found at the N-terminal of thiamine monophosphate kinase (EC: (ThiL) [PMID: 9188462]. ThiL phosphorylates thiamin monophosphate to form thiamin pyrophosphate, an essential cofactor that is synthsised de novo by Salmonella typhimurium.

Contributing signatures

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