Dihydropteroate synthase (IPR006390)

Short name: DHP_synth

Overlapping homologous superfamilies

Domain relationships


This domain is present in sequences representing dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis.

Dihydropteroate synthase (EC: (DHPS), a functional homodimer, catalyses the condensation of 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic acid to form 7,8-dihydropteroate. This is the second step in the three-step pathway leading from 6-hydroxymethyl-7,8-dihydropterin to 7,8-dihydrofolate. DHPS is the target of sulphonamides, which are substrate analogues that compete with para-aminobenzoic acid. Bacterial DHPS (gene sul or folP) [PMID: 2123867] is a protein of about 275 to 315 amino acid residues that is either chromosomally encoded or found on various antibiotic resistance plasmids. In the lower eukaryote Pneumocystis carinii, DHPS is the C-terminal domain of a multifunctional folate synthesis enzyme (gene fas) [PMID: 1313386].

Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS.

GO terms

Biological Process

GO:0009396 folic acid-containing compound biosynthetic process

Molecular Function

GO:0004156 dihydropteroate synthase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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