Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.

Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).

Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).

Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.

Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Sulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.

Oxidoreductase, NAD(P)H-FMN and ferric iron reductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity; Belongs to the azoreductase type 2 family.

Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.

Nitroreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family.

Putative NADH-dependent flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family.

NADPH-dependent flavin oxidoreductase; Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.

Oxidoreductase, NAD(P)H-FMN and ferric iron reductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity; Belongs to the azoreductase type 2 family.

Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.

Oxidoreductase, NAD(P)H-FMN and ferric iron reductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity; Belongs to the azoreductase type 2 family.

NADPH-dependent flavin oxidoreductase; Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.

Oxidoreductase, NAD(P)H-FMN and ferric iron reductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity; Belongs to the azoreductase type 2 family.

NADH:dichloroindophenol oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.

Oxidoreductase, NAD(P)H-FMN and ferric iron reductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity; Belongs to the azoreductase type 2 family.

Nitroreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Sulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Short-chain flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.

Putative NADH-dependent flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Putative NAD(P)H oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NAD(P)H dehydrogenase (quinone) family.

Putative NADH-dependent flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

NADPH-dependent flavin oxidoreductase; Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.