1.3.1.12	L-arogenate + NAD+	-	Escherichia coli	L-tyrosine + NADH + CO2	-	?	258346	
1.3.1.12	L-arogenate + NAD+	-	Klebsiella pneumoniae	L-tyrosine + NADH + CO2	-	?	258346	
1.3.1.12	L-arogenate + NAD+	-	Aquifex aeolicus	L-tyrosine + NADH + CO2	-	?	258346	
1.3.1.12	additional information	a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview	Haemophilus influenzae	?	-	?	89	
1.3.1.12	additional information	no activity with arogenate	Saccharomyces cerevisiae	?	-	?	89	
1.3.1.12	additional information	no activity with arogenate	Pleurotus ostreatus	?	-	?	89	
1.3.1.12	additional information	a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview	Haemophilus influenzae KW20	?	-	?	89	
1.3.1.12	prephenate + NAD+	-	Bacillus subtilis	4-hydroxyphenylpyruvate + NADH + CO2	-	?	258345	
1.3.1.12	prephenate + NAD+	-	Escherichia coli	4-hydroxyphenylpyruvate + NADH + CO2	-	?	258345	
1.3.1.12	prephenate + NAD+	-	Saccharomyces cerevisiae	4-hydroxyphenylpyruvate + NADH + CO2	-	?	258345