| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AcsL | DR97_419 | DR97_4371 | DR97_419 | Amp-binding enzyme family protein; Belongs to the ATP-dependent AMP-binding enzyme family | annotation not available | 0.578 |
| AcsL | acsA1 | DR97_4371 | DR97_1056 | Amp-binding enzyme family protein; Belongs to the ATP-dependent AMP-binding enzyme family | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.920 |
| AcsL | acsA2 | DR97_4371 | DR97_2076 | Amp-binding enzyme family protein; Belongs to the ATP-dependent AMP-binding enzyme family | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.917 |
| DR97_4095 | DR97_419 | DR97_4095 | DR97_419 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | annotation not available | 0.740 |
| DR97_4095 | acsA1 | DR97_4095 | DR97_1056 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.478 |
| DR97_4095 | acsA2 | DR97_4095 | DR97_2076 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.479 |
| DR97_4095 | aphB | DR97_4095 | DR97_3285 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | Histone deacetylase domain protein; Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. Shows nearly no activity against N(1)- acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial trifluoroacetylated lysine-derivative, and to a lesser extent, acety [...] | 0.462 |
| DR97_4095 | ppiA | DR97_4095 | DR97_4708 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | Peptidyl-prolyl cis-trans isomerase a (cyclophilin a); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This protein is not essential for growth. Presumably plays a role in signal transduction | 0.681 |
| DR97_4095 | ppiB | DR97_4095 | DR97_93 | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | Cyclophilin type peptidyl-prolyl cis-trans isomerase/cld family protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.681 |
| DR97_419 | AcsL | DR97_419 | DR97_4371 | annotation not available | Amp-binding enzyme family protein; Belongs to the ATP-dependent AMP-binding enzyme family | 0.578 |
| DR97_419 | DR97_4095 | DR97_419 | DR97_4095 | annotation not available | Putative acetylpolyamine aminohydrolase; Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines | 0.740 |
| DR97_419 | DR97_420 | DR97_419 | DR97_420 | annotation not available | annotation not available | 0.904 |
| DR97_419 | DR97_5632 | DR97_419 | DR97_5632 | annotation not available | annotation not available | 0.726 |
| DR97_419 | acsA1 | DR97_419 | DR97_1056 | annotation not available | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.578 |
| DR97_419 | acsA2 | DR97_419 | DR97_2076 | annotation not available | Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA | 0.578 |
| DR97_419 | aphA | DR97_419 | DR97_614 | annotation not available | Acetylpolyamine aminohydrolase; Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N(1)-acetylspermine and N(1)- acetylspermidine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. In vitro, can also hydrolyze artificial trifluoroacetylated and acetylated lysine-derivatives | 0.740 |
| DR97_419 | aphB | DR97_419 | DR97_3285 | annotation not available | Histone deacetylase domain protein; Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. Shows nearly no activity against N(1)- acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial trifluoroacetylated lysine-derivative, and to a lesser extent, acety [...] | 0.740 |
| DR97_419 | ppiA | DR97_419 | DR97_4708 | annotation not available | Peptidyl-prolyl cis-trans isomerase a (cyclophilin a); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This protein is not essential for growth. Presumably plays a role in signal transduction | 0.645 |
| DR97_419 | ppiB | DR97_419 | DR97_93 | annotation not available | Cyclophilin type peptidyl-prolyl cis-trans isomerase/cld family protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.645 |
| DR97_420 | DR97_419 | DR97_420 | DR97_419 | annotation not available | annotation not available | 0.904 |
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