| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| glpW | yhfI | BSU09240 | BSU10240 | Glycerol-3-phosphate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type pe: putative enzyme. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.520 |
| lcfB | lplJ | BSU10270 | BSU10250 | Long-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | 0.476 |
| lcfB | yhfI | BSU10270 | BSU10240 | Long-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.467 |
| lcfB | yhfK | BSU10270 | BSU10260 | Long-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. | Putative epimerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.616 |
| lplJ | lcfB | BSU10250 | BSU10270 | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | Long-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.476 |
| lplJ | rsbRB | BSU10250 | BSU13200 | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.502 |
| lplJ | yhfH | BSU10250 | BSU10230 | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | Hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.570 |
| lplJ | yhfI | BSU10250 | BSU10240 | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.961 |
| lplJ | yhfK | BSU10250 | BSU10260 | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | Putative epimerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.782 |
| pgcA | yhfI | BSU09310 | BSU10240 | Alpha-phosphoglucomutase; Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required fo [...] | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.461 |
| ppnKA | yhfI | BSU11610 | BSU10240 | Inorganic polyphosphate/ATP-NAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.475 |
| rsbRB | lplJ | BSU13200 | BSU10250 | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | 0.502 |
| rsbRB | yhfI | BSU13200 | BSU10240 | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.515 |
| yhfH | lplJ | BSU10230 | BSU10250 | Hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | 0.570 |
| yhfH | yhfI | BSU10230 | BSU10240 | Hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.580 |
| yhfI | glpW | BSU10240 | BSU09240 | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Glycerol-3-phosphate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type pe: putative enzyme. | 0.520 |
| yhfI | lcfB | BSU10240 | BSU10270 | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Long-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.467 |
| yhfI | lplJ | BSU10240 | BSU10250 | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Lipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. | 0.961 |
| yhfI | pgcA | BSU10240 | BSU09310 | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Alpha-phosphoglucomutase; Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required fo [...] | 0.461 |
| yhfI | ppnKA | BSU10240 | BSU11610 | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Inorganic polyphosphate/ATP-NAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. | 0.475 |