InterPro domain: IPR029052

This entry represents a domain found in metallo-dependent phosphatases. Proteins containing this domain include:

• Purple acid phosphatases [ 1 ].
• DNA double-strand break repair nucleases [ 2 ].
• 5'-nucleotidases (syn. UDP-sugar hydrolase).
• Protein serine/threonine phosphatase.
• Phosphoesterase-related proteins.
• TT1561-like proteins.
• YfcE-like proteins.
• Hypothetical protein aq_1666.
• DR1281-like proteins.
• TTHA0625-like proteins.
• GpdQ-like proteins.
• ADPRibase-Mn-like proteins.

Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues [ 3 , 4 ].

1. Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron center. J. Mol. Biol. 291, 135-47
2. Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Cell 105, 473-85
3. A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity. J. Biol. Chem. 283, 30942-9
4. Metallophosphoesterases: structural fidelity with functional promiscuity. Biochem. J. 467, 201-16