| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cypB | cypD | BSU27160 | BSU07250 | 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). | 0.933 |
| cypB | pksG | BSU27160 | BSU17150 | 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. | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | 0.439 |
| cypB | pksJ | BSU27160 | BSU17180 | 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. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.998 |
| cypB | pksN | BSU27160 | BSU17210 | 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. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.963 |
| cypB | srfAB | BSU27160 | BSU03490 | 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. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.890 |
| cypB | yesF | BSU27160 | BSU06880 | 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 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 NmrA-type oxidoreductase family. | 0.571 |
| cypB | yhjG | BSU27160 | BSU10500 | 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 aromatic compound monooxygenase/hydroxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.744 |
| cypD | cypB | BSU07250 | BSU27160 | 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. | 0.933 |
| cypD | pksJ | BSU07250 | BSU17180 | 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). | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.998 |
| cypD | pksN | BSU07250 | BSU17210 | 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). | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.962 |
| cypD | srfAB | BSU07250 | BSU03490 | 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). | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.890 |
| cypD | yesF | BSU07250 | BSU06880 | 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). | Putative 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 NmrA-type oxidoreductase family. | 0.572 |
| cypD | yhjG | BSU07250 | BSU10500 | 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). | Putative aromatic compound monooxygenase/hydroxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.735 |
| pksG | cypB | BSU17150 | BSU27160 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase 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. | 0.439 |
| pksG | pksJ | BSU17150 | BSU17180 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.996 |
| pksG | pksN | BSU17150 | BSU17210 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.991 |
| pksG | srfAB | BSU17150 | BSU03490 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.640 |
| pksG | yesE | BSU17150 | BSU06870 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the limonene-1,2-epoxide hydrolase family. | 0.438 |
| pksG | yhjG | BSU17150 | BSU10500 | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. | Putative aromatic compound monooxygenase/hydroxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.705 |
| pksJ | cypB | BSU17180 | BSU27160 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 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. | 0.998 |