protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 4
Myotubularin related phosphoinositide phosphatase 4 (MTMR4), also known as FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2) or zinc finger FYVE domain-containing protein 11 (ZFYVE11), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR4 localizes at the interface of early and recycling endosomes to regulate trafficking through this pathway. It plays a role in bacterial pathogenesis by stabilizing the integrity of bacteria-containing vacuoles.
Feature 1: catalytic site [active site], 2 residue positions
Conserved feature residue pattern:C R
Evidence:
Comment:the catalytic cysteine initiates a nucleophilic attack on the phosphate group of the substrate, forming a transient phosphoenzyme intermediate and releasing the substrate dephosphorylated; the transition state is stabilized by the arginine present in the catalytic pocket
Jiyao W et al.(2023). "The conserved domain database in 2023.",