IMP biosynthesis enzyme PurP, C-terminal (IPR009720)

Short name: IMP_biosynth_PurP_C

Overlapping homologous superfamilies


Domain relationships

  • ATP-grasp fold (IPR011761)
    • IMP biosynthesis enzyme PurP, C-terminal (IPR009720)


The last two steps of de novo purine biosynthesis are:

  • i) conversion of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate (FAICAR)
  • ii) conversion of FAICAR to inosine5'-monophopsphate (IMP)
In bacteria and eukaryotes, these steps are catalysed by the well-characterised bifunctional enzyme PurH [PMID: 11323713]. Archaea do not appear to posses PurH, however, and perform these reactions by a different mechanism [PMID: 9150241]. In archaea, step i) is catalysed by the well-conserved PurP protein, while step ii) is catalysed by the PurO enzyme in some (though not all) species [PMID: 15623504, PMID: 11844782].

This entry represents the C-terminal domain of PurP, which is homologous to the ATP-GRASP fold and thus may be involved in ATP-binding. It is almost always found in association with .

GO terms

Biological Process

GO:0006188 IMP biosynthetic process

Molecular Function

GO:0005524 ATP binding
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0000287 magnesium ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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