Enterobactin synthase multienzyme complex component, ATP-dependent; Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Enterobactin synthase multienzyme complex component, ATP-dependent; Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).

NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...]

Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.

L-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates.

Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.

L-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family.

Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.

NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...]

L-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates.

Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.

L-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates.

L-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family.

L-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates.

NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...]

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Enterobactin synthase multienzyme complex component, ATP-dependent; Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Putative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily.

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...]

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily.

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

NADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...]

Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Ureidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2.

Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.

Putative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily.