| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA60584.1 | EHA62282.1 | Syn8016DRAFT_2371 | Syn8016DRAFT_1577 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | 0.781 |
| EHA60584.1 | EHA62345.1 | Syn8016DRAFT_2371 | Syn8016DRAFT_1640 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.985 |
| EHA60584.1 | EHA63856.1 | Syn8016DRAFT_2371 | Syn8016DRAFT_0898 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | TIGRFAM: Glucose-1-phosphate adenylyltransferase; KEGG: pmf:P9303_16851 glucose-1-phosphate adenylyltransferase; PFAM: Nucleotidyl transferase; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | 0.916 |
| EHA60584.1 | cugP | Syn8016DRAFT_2371 | Syn8016DRAFT_1860 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Mannose-1-phosphate guanylyltransferase; Catalyzes the formation of UDP-glucose, from UTP and glucose 1-phosphate. | 0.856 |
| EHA60584.1 | glmU | Syn8016DRAFT_2371 | Syn8016DRAFT_0645 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Bifunctional protein glmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. | 0.484 |
| EHA60584.1 | pgi | Syn8016DRAFT_2371 | Syn8016DRAFT_0448 | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | KEGG: pmf:P9303_15071 glucose-6-phosphate isomerase; HAMAP: Phosphoglucose isomerase (PGI); PFAM: Phosphoglucose isomerase (PGI); Belongs to the GPI family. | 0.982 |
| EHA62282.1 | EHA60584.1 | Syn8016DRAFT_1577 | Syn8016DRAFT_2371 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | 0.781 |
| EHA62282.1 | EHA62283.1 | Syn8016DRAFT_1577 | Syn8016DRAFT_1578 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Nucleoside-triphosphatase rdgB; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.826 |
| EHA62282.1 | EHA62345.1 | Syn8016DRAFT_1577 | Syn8016DRAFT_1640 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | 0.903 |
| EHA62282.1 | EHA62424.1 | Syn8016DRAFT_1577 | Syn8016DRAFT_1719 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | TIGRFAM: Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; KEGG: pmf:P9303_26031 mannose-1-phosphate guanylyltransferase; PFAM: Mannose-6-phosphate isomerase, type II, C-terminal; Nucleotidyl transferase. | 0.910 |
| EHA62282.1 | EHA63856.1 | Syn8016DRAFT_1577 | Syn8016DRAFT_0898 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | TIGRFAM: Glucose-1-phosphate adenylyltransferase; KEGG: pmf:P9303_16851 glucose-1-phosphate adenylyltransferase; PFAM: Nucleotidyl transferase; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | 0.907 |
| EHA62282.1 | cugP | Syn8016DRAFT_1577 | Syn8016DRAFT_1860 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Mannose-1-phosphate guanylyltransferase; Catalyzes the formation of UDP-glucose, from UTP and glucose 1-phosphate. | 0.883 |
| EHA62282.1 | dacA | Syn8016DRAFT_1577 | Syn8016DRAFT_0182 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Conserved hypothetical protein CHP00159; Catalyzes the condensation of 2 ATP molecules into cyclic di- AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria. | 0.811 |
| EHA62282.1 | glmS | Syn8016DRAFT_1577 | Syn8016DRAFT_1721 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Glucosamine--fructose-6-phosphate aminotransferase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.815 |
| EHA62282.1 | glmU | Syn8016DRAFT_1577 | Syn8016DRAFT_0645 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | Bifunctional protein glmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. | 0.783 |
| EHA62282.1 | pgi | Syn8016DRAFT_1577 | Syn8016DRAFT_0448 | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | KEGG: pmf:P9303_15071 glucose-6-phosphate isomerase; HAMAP: Phosphoglucose isomerase (PGI); PFAM: Phosphoglucose isomerase (PGI); Belongs to the GPI family. | 0.872 |
| EHA62283.1 | EHA62282.1 | Syn8016DRAFT_1578 | Syn8016DRAFT_1577 | Nucleoside-triphosphatase rdgB; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | 0.826 |
| EHA62345.1 | EHA60584.1 | Syn8016DRAFT_1640 | Syn8016DRAFT_2371 | Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | 0.985 |
| EHA62345.1 | EHA62282.1 | Syn8016DRAFT_1640 | Syn8016DRAFT_1577 | Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. | 0.903 |
| EHA62345.1 | EHA63856.1 | Syn8016DRAFT_1640 | Syn8016DRAFT_0898 | Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | TIGRFAM: Glucose-1-phosphate adenylyltransferase; KEGG: pmf:P9303_16851 glucose-1-phosphate adenylyltransferase; PFAM: Nucleotidyl transferase; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | 0.991 |