Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Chromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...]

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Chromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...]

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Chromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...]

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Chromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...]

Transcriptional repressor for the nemRA-gloA operon, quinone-, glyoxal-, and HOCl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.

Rut operon transcriptional repressor for; Master transcription regulator which represses the degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for maintenance of metabolic balance between pyrimidines and purines. It also regulates the synthesis of pyrimidine nucleotides and arginine from glutamine (carAB) and the supply of glutamate (gadABWX).

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA 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.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA 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.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily.

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.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily.

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.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily.

flavin:NADH reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily.

Pyrimidine permease; May function as a proton-driven pyrimidine uptake system.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily.

Rut operon transcriptional repressor for; Master transcription regulator which represses the degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for maintenance of metabolic balance between pyrimidines and purines. It also regulates the synthesis of pyrimidine nucleotides and arginine from glutamine (carAB) and the supply of glutamate (gadABWX).

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.

Pyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA 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.

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.

flavin:NADH reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo.

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.

Pyrimidine permease; May function as a proton-driven pyrimidine uptake system.