id: Pfam:PF00990
pfam_id: PF00990
name: Diguanylate cyclase, GGDEF domain
short_name: GGDEF
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF00990
counters:
  proteins: 238353
  matches: 240443
  proteomes: 13288
  taxa: 19352
  structures: 70
  alphafold_models: 144091
  domain_architectures: 6727
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:IPR000160
description: This domain is found linked to a wide range of non-homologous domains in a variety of bacteria.
  It has been shown to be homologous to the adenylyl cyclase catalytic domain [[cite:PUB00007061]] and
  has diguanylate cyclase activity [[cite:PUB00016966]]. This observation correlates with the functional
  information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase
  A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In
  the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre,
  when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing
  a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric
  guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus
  catalyses the cyclisation of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule [[cite:PUB00016971],[cite:PUB00109145],[cite:PUB00050740]].