Metal-dependent hydrolase HDOD (IPR013976)

Short name: HDOD

Overlapping homologous superfamilies


Domain relationships



The HD domain, named after the conserved doublet of predicted catalytic residues, is found in a wide range of bacterial, archaeal and eukaryotic proteins. It defines a superfamily of phosphohydrolases that can catalyze both metal-dependent and -independent phosphomonoesterase and phosphodiesterase reactions for a broad range of substrates [PMID: 9868367, PMID: 18353368]. The HD-domain proteins appear to be involved in nucleic acid and nucleotide metabolism, signal transduction and possibly other functions. They are diverse in terms of both domain architecture and phylogenetic distribution; each of the completely sequenced genomes encodes more than one version of this domain.

The HD domain is composed of a bundle of alpha helices with a 5-helix core. Although all HD domains share key design features, a striking diversity of catalytic centres have been identified, containing no metal, mono-, bi- or trinuclear metal binding sites [PMID: 18353368, PMID: 24176013].

The HD-related output domain (HDOD) is a protein domain of unknown function. Proteins containing the HDOD are widespread in diverse bacteria; it can be present as a stand-alone domain, and also associated with other domains, such as response regulatory (RR), GGDEF, and EAL, suggesting a role in regulation and signaling [PMID: 23137357, PMID: 26821378]. Proteins containing this domain include CdgJ from Vibrio cholerae serotype O1. CdgJ is a phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) [PMID: 20622061].

Contributing signatures

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