node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
bioI | cypB | BSU30190 | BSU27160 | Cytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 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. | 0.449 |
bioI | cypD | BSU30190 | BSU07250 | Cytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family. | 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). | 0.702 |
bioI | yetM | BSU30190 | BSU07230 | Cytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family. | Putative hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.564 |
cypA | yetM | BSU26740 | BSU07230 | Cytochrome P450; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Putative hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.537 |
cypB | bioI | BSU27160 | BSU30190 | 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. | Cytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family. | 0.449 |
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 | pksS | BSU27160 | BSU17230 | 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. | Cytochrome P450 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. | 0.674 |
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 | yetM | BSU27160 | BSU07230 | 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 hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.575 |
cypD | bioI | BSU07250 | BSU30190 | 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 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family. | 0.702 |
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 | pksS | BSU07250 | BSU17230 | 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 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. | 0.592 |
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 | yetM | BSU07250 | BSU07230 | 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 hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.561 |
cypX | yetM | BSU35060 | BSU07230 | cyclo-L-leucyl-L-leucyl dipeptide oxidase; Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with larger hydrophobic side chains bind in a similar regime to cLL. Belongs to the cytochrome P450 family. | Putative hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.572 |
ltaSB | yetM | BSU07710 | BSU07230 | Enzyme responsible for polyglycerolphosphate LTA synthesis; Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate; Belongs to the LTA synthase family. | Putative hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.847 |
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 | pksS | BSU17150 | BSU17230 | 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 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. | 0.880 |
pksG | yetM | BSU17150 | BSU07230 | 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 hydroxylase/monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.651 |