1.1.1.305	additional information	one activity is to decarboxylate UDP-glucuronic acid to UDP-beta-L-threo-pentopyranosyl-4-ulose in the presence of NAD+. The second activity converts UDP-beta-L-threo-pentopyranosyl-4-ulose and NADH to UDP-xylose and NAD+, albeit at a lower rate. Following decarboxylation, there is stereospecific protonation at the C5pro-R position	Ralstonia solanacearum	?	-	?	89	
1.1.1.305	additional information	UGA decarboxylase produces NADH and UDP-alpha-D-4-dehyroxylose as products, it can rebind NADH and UDP-alpha-D-4-dehyroxylose to slowly make UDP-alpha-D-xylose	Escherichia coli	?	-	?	89	
1.1.1.305	additional information	hUXS contains a bound NAD+ cofactor that it recycles by first oxidizing UDP-alpha-D-glucuronic acid, and then reducing the UDP-alpha-D-4-dehydroxylose to produce UDP-alpha-D-xylose	Homo sapiens	?	-	?	89	
1.1.1.305	UDP-alpha-D-glucuronate + NAD+	-	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	r	425075	
1.1.1.305	UDP-alpha-D-glucuronate + NAD+	-	Homo sapiens	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	r	425075	
1.1.1.305	UDP-alpha-D-glucuronate + NAD+	-	Ralstonia solanacearum	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	425075	
1.1.1.305	UDP-glucuronate + NAD+	-	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	ArnA is a bi-functional enzyme, the oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-L-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and 4-amino-4-deoxy-L-arabinose modification of lipid A. only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	the modification of lipid A with 4-amino-4-deoxy-L-arabinose allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. ArnA is the first enzyme specific to the lipid A-Ara4N pathway. It contains two functionally and physically separable domains: a dehydrogenase domain (ArnA_DH) catalyzing the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid, and a transformylase domain that formylates UDP-4-amino-4-deoxy-L-arabinose	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	ArnA is a bi-functional enzyme. The oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose)	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The NAD+-dependent decarboxylating activity is contained in the 360 amino acid C-terminal domain of ArnA. This domain is separable from the N-terminal fragment, and its activity is identical to that of the full-length enzyme. T432, Y463, K467, R619, and S433 are involved in the mechanism of NAD+-dependent oxidation of the 4''-OH of the UDP-glucuronic acid and decarboxylation of the UDP-4-keto-glucuronic acid intermediate	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose. Residues Ser433 and Glu434 of the decarboxylase domain are required for the oxidative decarboxylation of UDP-glucuronate. Decarboxylase domain catalyzes both hydride abstraction (oxidation) from the C-4' position and the subsequent decarboxylation	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968	
1.1.1.305	UDP-glucuronate + NAD+	ordered mechanism of substrate binding and product release is proposed. R619 functions as a general acid in catalysis	Escherichia coli	UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+	-	?	402968