inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP)
LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Comment:based on human LHPP, on human and mouse HDHD2, and on other haloacid dehalogenase (HAD) superfamily members with structure
Structure:2X4D: human LHPP binds phosphoric acid and Mg2+ in the active site - View structure with Cn3D
Structure:3HLT: human haloacid dehalogenase-like hydrolase domain containing 2 (HDHD2), binds Na+ and sulfate ion in the active site - View structure with Cn3D
Structure:2HO4: Mus musculus haloacid dehalogenase-like hydrolase domain containing 2 protein binds Mg2+ and phosphate ion in the active site - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",