| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa0089 | PSHAa0091 | PSHAa0089 | PSHAa0091 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | 0.888 |
| PSHAa0089 | dapF | PSHAa0089 | PSHAa0092 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.885 |
| PSHAa0089 | fre | PSHAa0089 | PSHAa0104 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | NAD(P)H-flavin reductase; Function of strongly homologous gene; enzyme. | 0.903 |
| PSHAa0089 | lysA | PSHAa0089 | PSHAa0093 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. | 0.819 |
| PSHAa0089 | ribC | PSHAa0089 | PSHAa1734 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Riboflavin synthase; Function of strongly homologous gene; enzyme. | 0.902 |
| PSHAa0089 | ribD | PSHAa0089 | PSHAa2374 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Riboflavin biosynthesis protein; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.935 |
| PSHAa0089 | ribE | PSHAa0089 | PSHAa2373 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Riboflavin synthase subunit E; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.902 |
| PSHAa0089 | ribF | PSHAa0089 | PSHAa0917 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Bifunctional protein [Includes: Riboflavin kinase (Flavokinase); Function of strongly homologous gene; enzyme; Belongs to the ribF family. | 0.909 |
| PSHAa0089 | ribH | PSHAa0089 | PSHAa2371 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family. | 0.903 |
| PSHAa0089 | xerC | PSHAa0089 | PSHAa0090 | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Site-specific recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.891 |
| PSHAa0091 | PSHAa0089 | PSHAa0091 | PSHAa0089 | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.888 |
| PSHAa0091 | dapF | PSHAa0091 | PSHAa0092 | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.961 |
| PSHAa0091 | lysA | PSHAa0091 | PSHAa0093 | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | Putative diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. | 0.824 |
| PSHAa0091 | ribD | PSHAa0091 | PSHAa2374 | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | Riboflavin biosynthesis protein; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.422 |
| PSHAa0091 | xerC | PSHAa0091 | PSHAa0090 | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | Site-specific recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.933 |
| dapF | PSHAa0089 | PSHAa0092 | PSHAa0089 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.885 |
| dapF | PSHAa0091 | PSHAa0092 | PSHAa0091 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. | 0.961 |
| dapF | lysA | PSHAa0092 | PSHAa0093 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Putative diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. | 0.994 |
| dapF | ribD | PSHAa0092 | PSHAa2374 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Riboflavin biosynthesis protein; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.503 |
| dapF | xerC | PSHAa0092 | PSHAa0090 | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | Site-specific recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.938 |