node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
abnA | eglS | BSU28810 | BSU18130 | Arabinan-endo 1,5-alpha-L-arabinase; Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p- nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substitu [...] | Endo-1,4-beta-glucanase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.729 |
abnA | ysdC | BSU28810 | BSU28820 | Arabinan-endo 1,5-alpha-L-arabinase; Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p- nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substitu [...] | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.447 |
cdd | ysdC | BSU25300 | BSU28820 | Cytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.464 |
eglS | abnA | BSU18130 | BSU28810 | Endo-1,4-beta-glucanase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Arabinan-endo 1,5-alpha-L-arabinase; Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p- nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substitu [...] | 0.729 |
eglS | ysdC | BSU18130 | BSU28820 | Endo-1,4-beta-glucanase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.695 |
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 | ysdC | BSU10250 | BSU28820 | 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 aminopeptidase ysdC; Putative aminopeptidase. | 0.509 |
mccA | ysdC | BSU27260 | BSU28820 | Cystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.681 |
mccA | ytkP | BSU27260 | BSU29970 | Cystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine. | Putative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.823 |
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 | ysdC | BSU10240 | BSU28820 | 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. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.426 |
yqjQ | yqjT | BSU23780 | BSU23750 | Putative metabolite dehydrogenase, NAD-binding; 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 short-chain dehydrogenases/reductases (SDR) 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. | 0.943 |
yqjQ | ysdC | BSU23780 | BSU28820 | Putative metabolite dehydrogenase, NAD-binding; 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 short-chain dehydrogenases/reductases (SDR) family. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.425 |
yqjT | yqjQ | BSU23750 | BSU23780 | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Putative metabolite dehydrogenase, NAD-binding; 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 short-chain dehydrogenases/reductases (SDR) family. | 0.943 |
yqjT | ysdC | BSU23750 | BSU28820 | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.436 |
ysdB | ysdC | BSU28830 | BSU28820 | Conserved hypothetical protein; May mediate a negative feedback loop that down-regulates the expression of the sigma-W regulon following the activation of sigma-W in response to conditions of cell envelope stress. Might interact with and inhibit the activity of the protease PrsW, or could bind to the anti-sigma-W factor RsiW and thereby protect it from PrsW-mediated cleavage. | Putative aminopeptidase ysdC; Putative aminopeptidase. | 0.535 |
ysdC | abnA | BSU28820 | BSU28810 | Putative aminopeptidase ysdC; Putative aminopeptidase. | Arabinan-endo 1,5-alpha-L-arabinase; Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p- nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substitu [...] | 0.447 |
ysdC | cdd | BSU28820 | BSU25300 | Putative aminopeptidase ysdC; Putative aminopeptidase. | Cytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. | 0.464 |
ysdC | eglS | BSU28820 | BSU18130 | Putative aminopeptidase ysdC; Putative aminopeptidase. | Endo-1,4-beta-glucanase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.695 |
ysdC | lplJ | BSU28820 | BSU10250 | Putative aminopeptidase ysdC; Putative aminopeptidase. | 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. | 0.509 |