GGDEF domain is homologous to adenylyl cyclase

Jimin Pei, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

116 Scopus citations


The GGDEF domain is detected in many prokaryotic proteins, most of which are of unknown function. Several bacteria carry 12-22 different GGDEF homologues in their genomes. Conducting extensive profile-based searches, we detect statistically supported sequence similarity between GGDEF domain and adenylyl cyclase catalytic domain. From this homology, we deduce that the prokaryotic GGDEF domain is a regulatory enzyme involved in nucleotide cyclization, with the fold similar to that of the eukaryotic cyclase catalytic domain. This prediction 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. Domain architecture analysis shows that GGDEF is typically present in multidomain proteins containing regulatory domains of signaling pathways or protein-protein interaction modules. Evolutionary tree analysis indicates that GGDEF/cyclase superfamily forms a large diversified cluster of orthologous proteins present in bacteria, archaea, and eukaryotes.

Original languageEnglish (US)
Pages (from-to)210-216
Number of pages7
JournalProteins: Structure, Function and Genetics
Issue number2
StatePublished - Feb 1 2001


  • Bacterial signaling pathways
  • Diguanylate cyclase
  • Domain architecture
  • Ferredoxin fold
  • Structure prediction

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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