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Haloacid dehydrogenase superfamily


FieldValue
SymbolHydrolase_3
NameHydrolase_3
imagePDB 1rkq EBI.jpg
captioncrystal structure of had-like phosphatase yida from e. coli
PfamPF08282
Pfam_clanCL0137
ECOD2006.1.1

The haloacid dehydrogenase superfamily (HAD superfamily) is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.

Examples

A HAD domain is found in several distinct proteins including:

  • Phospholipid-translocating ATPase , a putative lipid-flipping enzyme involved in cold tolerance in Arabidopsis
  • 3-deoxy-D-manno-octulosonate (KDO) 8-phosphate phosphatase (), which catalyses the final step in the biosynthesis of KDO - a component of lipopolysaccharide in Gram-negative bacteria
  • Mannosyl-3-phosphoglycerate phosphatase (), which hydrolyses mannosyl-3-phosphoglycerate to form the osmolyte mannosylglycerate
  • Phosphoglycolate phosphatase (), which catalyses the dephosphorylation of 2-phosphoglycolate
  • 5´-Nucleotidase (EC 3.1.3.5) which either catalyzes the hydrolysis of IMP. or IMP and GMP
  • Hypothetical proteins

Human genes encoding proteins that contain this domain include:

  • ATP8B3, ATP8B4, ATP10A, ATP10B, ATP10D

References

References

  1. (November 1994). "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search". Journal of Molecular Biology.
  2. (December 2000). "Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases". The Plant Cell.
  3. (May 2003). "Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase". The Journal of Biological Chemistry.
  4. (November 2001). "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes". The Journal of Biological Chemistry.
  5. (January 2004). "Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum". The Journal of Biological Chemistry.
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