node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cypB | ptkA | BSU27160 | BSU36250 | 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. | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | 0.495 |
cypB | yhgD | BSU27160 | BSU10150 | 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 transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.765 |
cypB | yrhH | BSU27160 | BSU27180 | 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 methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.901 |
fadR | yhgD | BSU28550 | BSU10150 | Transcriptional regulator of fatty acids degradation (TetR/AcrR family); Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.556 |
hemY | hmoB | BSU10140 | BSU10100 | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 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. | 0.706 |
hemY | yhgD | BSU10140 | BSU10150 | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.543 |
hmoB | hemY | BSU10100 | BSU10140 | 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. | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 0.706 |
hmoB | yhgD | BSU10100 | BSU10150 | 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 transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.843 |
ptkA | cypB | BSU36250 | BSU27160 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB 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. | 0.495 |
ptkA | yhgD | BSU36250 | BSU10150 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.573 |
srtA | yhgD | BSU09200 | BSU10150 | Sortase A; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-Asp-Thr-Ser/Ala (LPDTS/A) motif. It has two substrates, YhcR and YfkN. Belongs to the bacterial sortase family. Class D subfamily. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.644 |
ydgG | ydgH | BSU05640 | BSU05650 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Putative membrane component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. | 0.976 |
ydgG | yhgD | BSU05640 | BSU10150 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.579 |
ydgH | ydgG | BSU05650 | BSU05640 | Putative membrane component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.976 |
ydgH | yhgD | BSU05650 | BSU10150 | Putative membrane component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.647 |
ydgH | yhgE | BSU05650 | BSU10160 | Putative membrane component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. | Putative methyl-accepting protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | 0.530 |
yhgD | cypB | BSU10150 | BSU27160 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 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. | 0.765 |
yhgD | fadR | BSU10150 | BSU28550 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | Transcriptional regulator of fatty acids degradation (TetR/AcrR family); Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. | 0.556 |
yhgD | hemY | BSU10150 | BSU10140 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 0.543 |
yhgD | hmoB | BSU10150 | BSU10100 | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 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. | 0.843 |