| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| OPJ58586.1 | fhs | CLCHR_38360 | CLCHR_10230 | Vitamin B12 dependent methionine synthase, activation domain. | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | 0.763 |
| OPJ58586.1 | luxS | CLCHR_38360 | CLCHR_26000 | Vitamin B12 dependent methionine synthase, activation domain. | S-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. | 0.823 |
| OPJ58586.1 | metG | CLCHR_38360 | CLCHR_09710 | Vitamin B12 dependent methionine synthase, activation domain. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.808 |
| OPJ58586.1 | metH_2 | CLCHR_38360 | CLCHR_38370 | Vitamin B12 dependent methionine synthase, activation domain. | Methionine synthase. | 0.978 |
| OPJ58586.1 | metK_1 | CLCHR_38360 | CLCHR_13090 | Vitamin B12 dependent methionine synthase, activation domain. | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.732 |
| OPJ58586.1 | metK_2 | CLCHR_38360 | CLCHR_27570 | Vitamin B12 dependent methionine synthase, activation domain. | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.732 |
| OPJ58586.1 | nifJ_1 | CLCHR_38360 | CLCHR_02790 | Vitamin B12 dependent methionine synthase, activation domain. | Pyruvate-flavodoxin oxidoreductase. | 0.898 |
| OPJ58586.1 | nifJ_2 | CLCHR_38360 | CLCHR_11980 | Vitamin B12 dependent methionine synthase, activation domain. | Pyruvate-flavodoxin oxidoreductase. | 0.861 |
| OPJ58586.1 | nifJ_3 | CLCHR_38360 | CLCHR_46340 | Vitamin B12 dependent methionine synthase, activation domain. | Pyruvate-flavodoxin oxidoreductase. | 0.861 |
| OPJ58586.1 | yitJ | CLCHR_38360 | CLCHR_39220 | Vitamin B12 dependent methionine synthase, activation domain. | Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase. | 0.981 |
| fhs | OPJ58586.1 | CLCHR_10230 | CLCHR_38360 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Vitamin B12 dependent methionine synthase, activation domain. | 0.763 |
| fhs | metG | CLCHR_10230 | CLCHR_09710 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.648 |
| fhs | metH_2 | CLCHR_10230 | CLCHR_38370 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Methionine synthase. | 0.903 |
| fhs | nifJ_1 | CLCHR_10230 | CLCHR_02790 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Pyruvate-flavodoxin oxidoreductase. | 0.837 |
| fhs | nifJ_2 | CLCHR_10230 | CLCHR_11980 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Pyruvate-flavodoxin oxidoreductase. | 0.681 |
| fhs | nifJ_3 | CLCHR_10230 | CLCHR_46340 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Pyruvate-flavodoxin oxidoreductase. | 0.681 |
| fhs | yitJ | CLCHR_10230 | CLCHR_39220 | Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase. | 0.959 |
| luxS | OPJ58586.1 | CLCHR_26000 | CLCHR_38360 | S-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. | Vitamin B12 dependent methionine synthase, activation domain. | 0.823 |
| luxS | metH_2 | CLCHR_26000 | CLCHR_38370 | S-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. | Methionine synthase. | 0.912 |
| luxS | metK_1 | CLCHR_26000 | CLCHR_13090 | S-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.476 |