| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bshC | ydeA | BSU15120 | BSU05110 | Malate glucosamine cysteine ligase; Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH. | Putative enzyme; 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 peptidase C56 family. | 0.689 |
| iolS | ydeA | BSU39780 | BSU05110 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | Putative enzyme; 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 peptidase C56 family. | 0.720 |
| iolS | yhaU | BSU39780 | BSU09850 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...] | 0.485 |
| iolS | yraA | BSU39780 | BSU27020 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | General stress protein; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins. | 0.493 |
| iolS | yrpG | BSU39780 | BSU26850 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | 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 aldo/keto reductase family. Aldo/keto reductase 2 subfamily. | 0.421 |
| iolS | yurT | BSU39780 | BSU32660 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | Putative methylglyoxalase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glyoxalase I family. | 0.506 |
| iolS | ywbC | BSU39780 | BSU38370 | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | Putative lyase; 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 glyoxalase I family. | 0.699 |
| yceJ | ydeA | BSU02960 | BSU05110 | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | Putative enzyme; 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 peptidase C56 family. | 0.556 |
| ydeA | bshC | BSU05110 | BSU15120 | Putative enzyme; 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 peptidase C56 family. | Malate glucosamine cysteine ligase; Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH. | 0.689 |
| ydeA | iolS | BSU05110 | BSU39780 | Putative enzyme; 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 peptidase C56 family. | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | 0.720 |
| ydeA | yceJ | BSU05110 | BSU02960 | Putative enzyme; 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 peptidase C56 family. | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.556 |
| ydeA | yhaU | BSU05110 | BSU09850 | Putative enzyme; 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 peptidase C56 family. | Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...] | 0.709 |
| ydeA | yhdN | BSU05110 | BSU09530 | Putative enzyme; 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 peptidase C56 family. | Aldo/keto reductase specific for NADPH; Aldo-keto reductase (AKR) that displays broad substrate specificity in vitro. Is able to reduce the standard AKR substrates DL- glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde, benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use NADH as a cosubstrate. Does not act on glucose, 2-pyridine carboxyaldehyde, fructose and xylose. The physiological function of this enzyme is not clear. May play a role in bacterial stress response and/or in detoxification of reactive aldehydes. Belongs to the aldo/keto reductase family. A [...] | 0.541 |
| ydeA | yqkF | BSU05110 | BSU23620 | Putative enzyme; 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 peptidase C56 family. | NADPH-dependent aldo-keto reductase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme; Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. | 0.722 |
| ydeA | yraA | BSU05110 | BSU27020 | Putative enzyme; 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 peptidase C56 family. | General stress protein; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins. | 0.485 |
| ydeA | yrpG | BSU05110 | BSU26850 | Putative enzyme; 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 peptidase C56 family. | 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 aldo/keto reductase family. Aldo/keto reductase 2 subfamily. | 0.788 |
| ydeA | yurT | BSU05110 | BSU32660 | Putative enzyme; 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 peptidase C56 family. | Putative methylglyoxalase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glyoxalase I family. | 0.833 |
| ydeA | ywbC | BSU05110 | BSU38370 | Putative enzyme; 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 peptidase C56 family. | Putative lyase; 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 glyoxalase I family. | 0.913 |
| yhaU | iolS | BSU09850 | BSU39780 | Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...] | Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...] | 0.485 |
| yhaU | ydeA | BSU09850 | BSU05110 | Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...] | Putative enzyme; 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 peptidase C56 family. | 0.709 |
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