node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
amhX | dppA | BSU03010 | BSU12920 | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | D-alanyl-aminopeptidase; Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear; Belongs to the peptidase M55 family. | 0.636 |
amhX | thiQ | BSU03010 | BSU15350 | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | N-formyl-4-amino-5-aminomethyl-2- methylpyrimidinedeformylase; Catalyzes the deformylation of the formylaminopyrimidine N- formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine; Belongs to the peptidase M20A family. | 0.695 |
amhX | yhaA | BSU03010 | BSU10070 | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.495 |
bacH | yhaA | BSU37680 | BSU10070 | Cyclohexenol-containing tetrahydro-4-hydroxyphenylpyruvate H(4)HPP in bacilysin synthesis; Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the [...] | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.507 |
dppA | amhX | BSU12920 | BSU03010 | D-alanyl-aminopeptidase; Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear; Belongs to the peptidase M55 family. | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | 0.636 |
dppA | yhaA | BSU12920 | BSU10070 | D-alanyl-aminopeptidase; Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear; Belongs to the peptidase M55 family. | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.584 |
hmoB | yhaA | BSU10100 | BSU10070 | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.667 |
hmoB | yhfA | BSU10100 | BSU10080 | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.810 |
hmoB | yhgB | BSU10100 | BSU10090 | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.635 |
hmoB | yjcH | BSU10100 | BSU11860 | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.437 |
ilvH | yhaA | BSU28300 | BSU10070 | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.453 |
thiQ | amhX | BSU15350 | BSU03010 | N-formyl-4-amino-5-aminomethyl-2- methylpyrimidinedeformylase; Catalyzes the deformylation of the formylaminopyrimidine N- formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine; Belongs to the peptidase M20A family. | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | 0.695 |
thiQ | yhaA | BSU15350 | BSU10070 | N-formyl-4-amino-5-aminomethyl-2- methylpyrimidinedeformylase; Catalyzes the deformylation of the formylaminopyrimidine N- formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine; Belongs to the peptidase M20A family. | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.700 |
yhaA | amhX | BSU10070 | BSU03010 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Amidohydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase M20 family. | 0.495 |
yhaA | bacH | BSU10070 | BSU37680 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Cyclohexenol-containing tetrahydro-4-hydroxyphenylpyruvate H(4)HPP in bacilysin synthesis; Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the [...] | 0.507 |
yhaA | dppA | BSU10070 | BSU12920 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | D-alanyl-aminopeptidase; Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear; Belongs to the peptidase M55 family. | 0.584 |
yhaA | hmoB | BSU10070 | BSU10100 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.667 |
yhaA | ilvH | BSU10070 | BSU28300 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. | 0.453 |
yhaA | thiQ | BSU10070 | BSU15350 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | N-formyl-4-amino-5-aminomethyl-2- methylpyrimidinedeformylase; Catalyzes the deformylation of the formylaminopyrimidine N- formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine; Belongs to the peptidase M20A family. | 0.700 |
yhaA | yhfA | BSU10070 | BSU10080 | Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.863 |