node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PSHAa1965 | mltF | PSHAa1965 | PSHAa2331 | Homologs of previously reported genes of unknown function. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.454 |
PSHAa2327 | PSHAa2328 | PSHAa2327 | PSHAa2328 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.978 |
PSHAa2327 | mltF | PSHAa2327 | PSHAa2331 | Homologs of previously reported genes of unknown function. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.446 |
PSHAa2327 | purL | PSHAa2327 | PSHAa2330 | Homologs of previously reported genes of unknown function. | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.709 |
PSHAa2328 | PSHAa2327 | PSHAa2328 | PSHAa2327 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.978 |
PSHAa2328 | mltF | PSHAa2328 | PSHAa2331 | Homologs of previously reported genes of unknown function. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.435 |
PSHAa2328 | purL | PSHAa2328 | PSHAa2330 | Homologs of previously reported genes of unknown function. | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.717 |
PSHAa2332 | mltF | PSHAa2332 | PSHAa2331 | Homologs of previously reported genes of unknown function. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.526 |
PSHAa2522 | mltF | PSHAa2522 | PSHAa2331 | Putative lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.432 |
mltD | mltF | PSHAa0293 | PSHAa2331 | Putative membrane-bound lytic murein transglycosylase D [Precursor]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.528 |
mltF | PSHAa1965 | PSHAa2331 | PSHAa1965 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Homologs of previously reported genes of unknown function. | 0.454 |
mltF | PSHAa2327 | PSHAa2331 | PSHAa2327 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Homologs of previously reported genes of unknown function. | 0.446 |
mltF | PSHAa2328 | PSHAa2331 | PSHAa2328 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Homologs of previously reported genes of unknown function. | 0.435 |
mltF | PSHAa2332 | PSHAa2331 | PSHAa2332 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Homologs of previously reported genes of unknown function. | 0.526 |
mltF | PSHAa2522 | PSHAa2331 | PSHAa2522 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Putative lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.432 |
mltF | mltD | PSHAa2331 | PSHAa0293 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Putative membrane-bound lytic murein transglycosylase D [Precursor]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.528 |
mltF | purL | PSHAa2331 | PSHAa2330 | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.705 |
purL | PSHAa2327 | PSHAa2330 | PSHAa2327 | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | Homologs of previously reported genes of unknown function. | 0.709 |
purL | PSHAa2328 | PSHAa2330 | PSHAa2328 | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | Homologs of previously reported genes of unknown function. | 0.717 |
purL | mltF | PSHAa2330 | PSHAa2331 | Phophoribosylformylglycinamidine synthase (FGAM synthetase); Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | Putative transport binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.705 |