Eyes absent protein phosphatase (EYA) belongs to a family of phosphatase which uses an Asp nucleophile for catalysis. Eye protein is characterized by its highly conserved C-terminal domain Eye domain(ED) ~270 amino acids, which also contains a phosphatase catalytic domain. Mammals EYA family contains four members, known as, EYA1-4 and Drosophila has only one gene (1).

Reference
1. Jemc, J. and Rebay, I. (2007) The eyes absent family of phosphotyrosine phosphatases: properties and roles in developmental regulation of transcription. Annu Rev Biochem, 76, 513-538. PMID: 17341163

    Magnesium-dependent phosphatase 1 (MDP1) belongs to a family of phosphatase which uses an Asp nucleophile for catalysis. The conserved motif DXDX[TV] is also found in MDP1. Like EYA, FCP family, MDP1 also belongs to the haloacid dehalogenase (HAD) superfamily. However, the domain proximal to the active site in HAD family is absent in MDP1, and makes a open state in active site which might be responsible for interactions with large substrates such as proteins (1).

Reference
1. Selengut, J.D. (2001) MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. Biochemistry, 40, 12704-12711. PMID: 11601995

    PGP, also known as AUM, belongs to a family of phosphatase which uses an Asp nucleophile for catalysis. PGP/AUM is the closest paralog of chronophin. Interestingly, PGP/AUM acts as a tyrosine phosphatase, whereas chronophin dephosphorylates serine/threonine-phosphorylated proteins (1). Prentki, et al., describe that a previously known phosphoglycolate phosphatase (PGP) with an uncertain function in mammalian cells acts as a specific G3PP and plays a pivotal role in the regulation of glucose and lipid metabolism and signaling, as well as in the response to metabolic stress (2). Notably, PGP/AUM is a widely conserved metabolite repair enzyme in mammals which eliminates 4-P-erythronate, a side product of GAPDH (3).

Reference
1. Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J and Gohla A. (2014) Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities. J Biol Chem, 289, 3416-31. PMID: 24338473
2. Mugabo Y, Zhao S, Seifried A, Gezzar S, Al-Mass A, Zhang D, Lamontagne J, Attane C, Poursharifi P, Iglesias J, Joly E, Peyot ML, Gohla A, Madiraju SR and Prentki M. (2016) Identification of a mammalian glycerol-3-phosphate phosphatase: Role in metabolism and signaling in pancreatic β-cells and hepatocytes. Proc Natl Acad Sci U S A, 113, E430-9. PMID: 26755581
3. Collard F, Baldin F, Gerin I, Bolsée J, Noël G, Graff J, Veiga-da-Cunha M, Stroobant V, Vertommen D, Houddane A, Rider MH, Linster CL, Van Schaftingen E and Bommer GT. (2003) A conserved phosphatase destroys toxic glycolytic side products in mammals and yeast. Nat Chem Biol, 12, 601-7. PMID: 27294321