5.3.1.12	D-Fructuronate	first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism	Escherichia coli	?	-	?	369283	
5.3.1.12	D-Galacturonate	-	Escherichia coli	D-Tagaturonate	-	?	1018	
5.3.1.12	D-Galacturonate	-	Pectobacterium carotovorum	D-Tagaturonate	-	?	1018	
5.3.1.12	D-Galacturonate	-	Halalkalibacterium halodurans	D-Tagaturonate	-	?	1018	
5.3.1.12	D-Galacturonate	-	Halalkalibacterium halodurans	D-Tagaturonate	-	r	1018	
5.3.1.12	D-Galacturonate	-	Escherichia coli	D-Tagaturonate	-	r	1018	
5.3.1.12	D-Galacturonate	r	Escherichia coli	D-Tagaturonate	-	?	1018	
5.3.1.12	D-Galacturonate	r	Pedobacter heparinus	D-Tagaturonate	-	?	1018	
5.3.1.12	D-Galacturonate	first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism	Escherichia coli	?	-	?	369282	
5.3.1.12	D-Glucuronate	-	Escherichia coli	D-Fructuronate	-	?	1017	
5.3.1.12	D-Glucuronate	-	Pectobacterium carotovorum	D-Fructuronate	-	?	1017	
5.3.1.12	D-Glucuronate	-	Pedobacter heparinus	D-Fructuronate	-	?	1017	
5.3.1.12	D-Glucuronate	-	Halalkalibacterium halodurans	D-Fructuronate	-	?	1017	
5.3.1.12	D-Glucuronate	-	Halalkalibacterium halodurans	D-Fructuronate	-	r	1017	
5.3.1.12	D-Glucuronate	-	Escherichia coli	D-Fructuronate	-	r	1017	
5.3.1.12	D-Glucuronate	the mononuclear metal center in the active site is ligated to the C6 carboxylate and the C5 hydroxyl group of the substrate, this hydroxyl group is also hydrogen-bonded to Asp355. The C2 and C3 hydroxyl groups of the substrate are hydrogen bonded to Arg357 and the carbonyl group at C1 is hydrogen bonded to Tyr50	Halalkalibacterium halodurans	D-Fructuronate	-	r	1017	
5.3.1.12	D-Glucuronate	first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism	Escherichia coli	?	-	?	369281	
5.3.1.12	D-Tagaturonate	first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism	Escherichia coli	?	-	?	369284	
5.3.1.12	additional information	the enzyme does not participate in the metabolism of heparin or chondroitin sulfate	Pedobacter heparinus	?	-	?	89	
5.3.1.12	additional information	active site structure and molecular reaction mechanism, proton transfer from C2 of D-glucuronate to C1 that is initiated by the combined actions of Asp-355 from the end of ?-strand 8 and the C-5 hydroxyl of the substrate that is bound to the metal ion. Formation of the proposed cis-enediol intermediate is further facilitated by the shuttling of the proton between the C2 and C1 oxygens by the conserved Tyr50 and/or Arg355	Halalkalibacterium halodurans	?	-	?	89	
5.3.1.12	additional information	chemical mechanism and active site structure, mutational analysis, overview	Escherichia coli	?	-	?	89