| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ97762.1 | CAZ98781.1 | ZOBELLIA_3624 | ZOBELLIA_4646 | Conserved hypothetical protein; This protein displays distant similarity with glycoside hydrolases of the family 74 (GH74). These proteins consist of a tandem repeat of two similar domains, which are both folded into seven-bladed beta- propeller structures. But the two conserved catalytic aspartatic residues are substituted here by two asparagine residues. Features a signal peptide cleaved between the residues 19 and 20. | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | 0.446 |
| CAZ98781.1 | CAZ97762.1 | ZOBELLIA_4646 | ZOBELLIA_3624 | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | Conserved hypothetical protein; This protein displays distant similarity with glycoside hydrolases of the family 74 (GH74). These proteins consist of a tandem repeat of two similar domains, which are both folded into seven-bladed beta- propeller structures. But the two conserved catalytic aspartatic residues are substituted here by two asparagine residues. Features a signal peptide cleaved between the residues 19 and 20. | 0.446 |
| CAZ98781.1 | ccpA3 | ZOBELLIA_4646 | ZOBELLIA_4645 | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | The Di-heme cytochrome c peroxidase reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CcpA reduce hydrogen peroxide without the need to generate semi-stable free radicals; CcpA is structured into two domains, each containing one c-type heme group, with a calcium-binding site at the domain interface; Putative lipoprotein signal peptide cleaved between the residues 16 and 17; Possibly localized in the outer membrane; High confidence in function and specificity. | 0.900 |
| CAZ98781.1 | gfoA | ZOBELLIA_4646 | ZOBELLIA_4647 | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | Glucose-fructose oxidoreductase; To protect the bacterium against osmotic shock, the periplasmic glucose-fructose oxidoreductase produces the compatible, solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone. GfoA formes a homodimer and each subunit contains tightly associated NADP which is not released during the catalytic cycle. It belongs to the GFO/IDH/MOCA family and adopts a Rossmann fold. Features an uncleaved signal peptide. Localized in the periplasm; High confidence in function and specificity. | 0.419 |
| CAZ98781.1 | phoA | ZOBELLIA_4646 | ZOBELLIA_4371 | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; High confidence in function and specificity. | 0.475 |
| CAZ98781.1 | phoB | ZOBELLIA_4646 | ZOBELLIA_2147 | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | Alkaline phosphatase; Modular protein that consists of a N-terminal conserved domain of unknown function (240 residues) and a C-terminal Alkaline phosphatase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Specificity unclear. | 0.475 |
| ccpA3 | CAZ98781.1 | ZOBELLIA_4645 | ZOBELLIA_4646 | The Di-heme cytochrome c peroxidase reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CcpA reduce hydrogen peroxide without the need to generate semi-stable free radicals; CcpA is structured into two domains, each containing one c-type heme group, with a calcium-binding site at the domain interface; Putative lipoprotein signal peptide cleaved between the residues 16 and 17; Possibly localized in the outer membrane; High confidence in function and specificity. | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | 0.900 |
| gfoA | CAZ98781.1 | ZOBELLIA_4647 | ZOBELLIA_4646 | Glucose-fructose oxidoreductase; To protect the bacterium against osmotic shock, the periplasmic glucose-fructose oxidoreductase produces the compatible, solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone. GfoA formes a homodimer and each subunit contains tightly associated NADP which is not released during the catalytic cycle. It belongs to the GFO/IDH/MOCA family and adopts a Rossmann fold. Features an uncleaved signal peptide. Localized in the periplasm; High confidence in function and specificity. | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | 0.419 |
| phoA | CAZ98781.1 | ZOBELLIA_4371 | ZOBELLIA_4646 | Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; High confidence in function and specificity. | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | 0.475 |
| phoA | phoB | ZOBELLIA_4371 | ZOBELLIA_2147 | Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; High confidence in function and specificity. | Alkaline phosphatase; Modular protein that consists of a N-terminal conserved domain of unknown function (240 residues) and a C-terminal Alkaline phosphatase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Specificity unclear. | 0.925 |
| phoB | CAZ98781.1 | ZOBELLIA_2147 | ZOBELLIA_4646 | Alkaline phosphatase; Modular protein that consists of a N-terminal conserved domain of unknown function (240 residues) and a C-terminal Alkaline phosphatase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Specificity unclear. | Conserved hypothetical protein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Lcocalized in the outer membrane. | 0.475 |
| phoB | phoA | ZOBELLIA_2147 | ZOBELLIA_4371 | Alkaline phosphatase; Modular protein that consists of a N-terminal conserved domain of unknown function (240 residues) and a C-terminal Alkaline phosphatase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Specificity unclear. | Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; High confidence in function and specificity. | 0.925 |