L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Kynurenine formamidase, KynB; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation; Belongs to the Cyclase 1 superfamily. KynB family.

L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Probable coenzyme A ligase; Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate.

L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Probable FAD-dependent monooxygenase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene).

Kynurenine formamidase, KynB; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation; Belongs to the Cyclase 1 superfamily. KynB family.

L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Kynurenine formamidase, KynB; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation; Belongs to the Cyclase 1 superfamily. KynB family.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

L-Tryptophan:oxygen 2,3-oxidoreductase (decyclizing) KynA; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

Kynurenine formamidase, KynB; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation; Belongs to the Cyclase 1 superfamily. KynB family.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

Probable coenzyme A ligase; Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate.

Kynureninase KynU; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.

Probable FAD-dependent monooxygenase; Involved in the terminal step of the biosynthesis of quinolone which in addition to serve as a potent signal for quorum sensing, chelates iron and promotes the formation of membrane vesicles (MVs). Catalyzes the hydroxylation of 2-heptyl-4-quinolone (C7-HHQ) to yield 2-heptyl-3-hydroxy-4-quinolone (PQS). Belongs to the 3-hydroxybenzoate 6-hydroxylase family.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Autoinducer synthesis protein LasI; Required for the synthesis of PAI consisting of 3-oxo-N- (tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3- oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Transcriptional regulator MvfR; Transcription regulator that plays a critical role in virulence by positively regulating the expression of multiple quorum sensing (QS)-regulated virulence factors, genes involved in protein secretion, translation, response to oxidative stress and the phnAB operon. At the stationary phase, negatively autoregulates its function through cleavage and translocation to the extracellular space ; Belongs to the LysR transcriptional regulatory family.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Probable coenzyme A ligase; Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

PqsB; Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)- quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. The PqsC/PqsB complex catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form HHQ. PqsB, together with PqsC, catalyzes the coupling of 2-ABA with the octanoate group, leading to decarboxylation and dehydration, and resulting in closure of the quinoline ring. PqsB is probably required for the proper folding of PqsC ra [...]

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

PqsC; Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)- quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. The PqsC/PqsB complex catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form HHQ. First, PqsC acquires an octanoyl group from octanoyl-CoA and forms an octanoyl-PqsC intermediate. Then, together with PqsB, it catalyzes the coupling of 2-ABA with the octanoate group, leading to decarboxylation and dehydration, and re [...]

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

3-oxoacyl-[acyl-carrier-protein] synthase III; Required for the biosynthesis of a number of signaling molecules, such as the quinolone signal 2-heptyl-3-hydroxy-4(1H)- quinolone (PQS), 2-heptyl-4-hydroxyquinoline (HHQ) and 2,4- dihydroxyquinoline (DHQ). These molecules are required for normal biofilm formation. Catalyzes the transfer of the anthraniloyl moiety from anthraniloyl-CoA to malonyl-CoA to form 2-aminobenzoylacetyl-CoA. The first step of the reaction is the formation of a covalent anthraniloyl-PqsD intermediate. Next, the short-lived intermediate 3-(2-aminophenyl)- 3-oxopropa [...]

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Quinolone signal response protein; Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)- quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. Catalyzes the hydrolysis of the intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2- aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also hydrolyze other substrates such as S-ethyl-acetothioacetate and acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA and octanoyl-CoA. Be [...]

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Probable FAD-dependent monooxygenase; Involved in the terminal step of the biosynthesis of quinolone which in addition to serve as a potent signal for quorum sensing, chelates iron and promotes the formation of membrane vesicles (MVs). Catalyzes the hydroxylation of 2-heptyl-4-quinolone (C7-HHQ) to yield 2-heptyl-3-hydroxy-4-quinolone (PQS). Belongs to the 3-hydroxybenzoate 6-hydroxylase family.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

ATP-dependent RNA helicase RhlB; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. Belongs to the DEAD box helicase family. RhlB subfamily.

Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.

Autoinducer synthesis protein RhlI; Required for the synthesis of BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone) autoinducer molecules which bind to RhlR and thus acts in elastase biosynthesis regulation.