acyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids.

Electron transfer flavoprotein (alpha subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).

acyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids.

Electron transfer flavoprotein (beta subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).

acyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids.

acyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Electron transfer flavoprotein (alpha subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Electron transfer flavoprotein (beta subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

acyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Branched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Succinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Alkyl hydroperoxide reductase (large subunit); Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).

Flavohemoglobin; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity). In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Alkyl hydroperoxide reductase (large subunit); Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).

Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Glycerol-3-phosphate oxidase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family.

Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Acetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.

Putative enzyme with pyruvate as substrate; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.

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.

Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family.