3.6.1.13	evolution	adenosine diphosphate ribose pyrophosphatase (ADPRase) is a member of the Nudix family	756035	
3.6.1.13	evolution	ADPRibase-Mn enzymes contain the dinuclear metal centre typical of the metallo-dependent phosphatases SCOP2 superfamily, forming within it a family of their own named as ADPRibase-Mn-like. ADPRibase-Mn proteins constitute also a functional family in the CATH classification, within cluster SC:3 of superfamily 3.60.21.10	758417	
3.6.1.13	malfunction	improved seed yield parameters and early flowering time upon overexpression of AtNUDX7 in Arabidopsis thaliana. Different levels of constitutive overexpresxadsion of the Arabidopsis AtNUDX7 gene in Arabidopsis and also in maize do not result in a mild drought stress tolerance phenotype. But downregulation of AtNUDX7 results in mild drought stress tolerance under water deficit but growth under normal conditions is reduced, phenotypes, overview	-, 756976	
3.6.1.13	metabolism	the poly(ADP-ribosyl)ation (PAR) pathway is a postxadtranslational protein modification process, activated upon single- or double-stranded DNA breaks, in which ADP-ribose subunits from nicotinamide adenine dinucleotide (NAD+) are covalently attached to target proteins mediated by the poly(ADP-ribose) polymerase enzyme (PARP, EC 2.4.2.30). PARP activity can be reversed by a poly(ADP-ribose) glycohydrolase enzyme (PARG, EC 3.2.1.143) generating free ADP-ribose molecules that can be degraded into adenosine monophosphate (AMP) and ribose-5-phosphate by the ADP-ribose-specific Nudix hydrolase enzyme. AMP can be utilized to replenish the ATP and NAD+, leading to maintenance of cellular homeostasis. Cytosolic enzymes AtNUDX2, AtNUDX6, AtNUDX7, and AtNUDX10 have pyrophosphohydrolase activity toward both ADP-ribose and NADH. Role of the poly(ADP-ribosyl)ation pathway in stress response and energy homeostasis, overview	-, 756976	
3.6.1.13	additional information	the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site) and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview	756035	
3.6.1.13	additional information	the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site)and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview	-, 756035	
3.6.1.13	physiological function	cyclic ADP-ribose (cADPR) is a messenger for Ca2+ mobilization. Its turnover is believed to occur by glycohydrolysis to ADP-ribose. ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cADPR phosphohydrolase with much lower efficiency than on its major substrates	758417	
3.6.1.13	physiological function	NUDX7 contributes to 23% of the total diphosphohydrolase activity toward ADP-ribose under normal conditions, while under oxidative stress, the contribution of NUDX7 to the activity increases to 34%. Additionally, NUDX7 accounts for 53% of the total pyrophosphohydrolase activity toward NADH under normal conditions and the activity is increased by oxidative stress with NUDX7 contributing 57%	720769	
3.6.1.13	physiological function	TtADPRase catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P)	756035