1.13.11.78	evolution	enzyme PhnZ belongs to a large family of hydrolytic enzymes, the HD-phosphohydrolase superfamily, which comprises enzymes that use a strictly conserved His-Asp sequence motif to bind active site metal ions. Structural comparisons of PhnZ reveal an evolutionary connection between Fe(II)-dependent hydrolysis of phosphate esters and oxidative carbon-phosphorus or carbon-carbon bond cleavage, thus uniting the diverse chemistries that are found in the HD superfamily. PhnZ is a structural homologue of myo-inositol oxygenase and Fe(II)-dependent phosphohydrolases	743680	
1.13.11.78	evolution	the enzyme is a member of the HD-domain protein superfamily	743907	
1.13.11.78	metabolism	combined with PhnY, which is a nonheme mononuclear 2-oxoglutarate-dependent dioxygenase to effect typical hydroxylation transformation of 2-amino-ethylphosphonic acid (2-AEP) to (R)-OH-AEP, the PhnY-PhnZ relay pathway affords aquatic and marine bacteria in Pi limited environments to utilize 2-AEP, the most abundant environmental 2-AEP, as the source of phosphate	743907	
1.13.11.78	additional information	enzyme PhnZ has an active site containing two Fe ions coordinated by four histidines and two aspartates that is strikingly similar to the carbon-carbon bond cleaving enzyme, myo-inositol-oxygenase. The exception is residue Y24, which forms a transient ligand interaction at the dioxygen binding site of the second Fe2+. Structure comparisons and substrate binding structures, active site structure, detailed overview	743680	
1.13.11.78	physiological function	diiron oxygenase PhnZ catalyzes the catabolism of organophosphonate (R)-2-amino-1-hydroxyethylphosphonic to glycine and inorganic phosphate (Pi). In this organophosphonate catabolism way, PhnZ oxidatively cleaves the highly stable C-P bond in Pn to produce phosphate. The reaction affords aquatic and marine bacteria in phosphate-limited environments to utilize the most abundant environmental organophosphonate 2-amino-ethylphosphonic acid as source of phosphate	743907	
1.13.11.78	physiological function	the enzymes PhnY and PhnZ comprise an oxidative catabolic pathway that enables marine bacteria to use 2-aminoethylphosphonic acid as a source of inorganic phosphate. PhnZ is notable for catalyzing the oxidative cleavage of a carbon-phosphorus bond using Fe(II) and dioxygen	743680