id: Pfam:PF16332
pfam_id: PF16332
name: Dermatan-sulfate epimerase-like, N-terminal
short_name: DSE-like_N
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF16332
counters:
  proteins: 3098
  matches: 3125
  proteomes: 1686
  taxa: 4044
  structures: 14
  alphafold_models: 2372
  domain_architectures: 101
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR032518
description: This entry represents the N-terminal of dermatan-sulfate epimerase (DSE) from mammals, and
  heparin-sulfate lyase (HepB) from bacteria [[cite:PUB00076523]]. DSE converts D-glucuronic acid to L-iduronic
  acid (IdoUA) residues. It plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide
  dermatan sulfate [[cite:PUB00162452],[cite:PUB00109125]]. HepB cleaves both heparin and heparan sulfate
  glycosaminoglycans through a beta-elimination mechanism. It cleaves heparin at alpha-D-GlcNp2S6S(1->4)
  alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp [[cite:PUB00016410]].
  This domain is composed of helical hairpins.