| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA0449 | RPA0452 | RPA0449 | RPA0452 | Possible hydrolases/phosphatases. | Glycoprotease (M22) metalloprotease. | 0.506 |
| RPA0449 | fur-2 | RPA0449 | RPA0450 | Possible hydrolases/phosphatases. | Transcriptional regulator, FUR family; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the Fur family. | 0.684 |
| RPA0449 | miaB | RPA0449 | RPA0448 | Possible hydrolases/phosphatases. | tRNA-i(6)A37 modification enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.610 |
| RPA0449 | rimI | RPA0449 | RPA0451 | Possible hydrolases/phosphatases. | Putative RimI protein, peptide N-acetyltransferase. | 0.535 |
| RPA0452 | RPA0449 | RPA0452 | RPA0449 | Glycoprotease (M22) metalloprotease. | Possible hydrolases/phosphatases. | 0.506 |
| RPA0452 | RPA0453 | RPA0452 | RPA0453 | Glycoprotease (M22) metalloprotease. | Possible NifU-like domain (residues 119-187); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.559 |
| RPA0452 | fur-2 | RPA0452 | RPA0450 | Glycoprotease (M22) metalloprotease. | Transcriptional regulator, FUR family; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the Fur family. | 0.620 |
| RPA0452 | miaB | RPA0452 | RPA0448 | Glycoprotease (M22) metalloprotease. | tRNA-i(6)A37 modification enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.502 |
| RPA0452 | rimI | RPA0452 | RPA0451 | Glycoprotease (M22) metalloprotease. | Putative RimI protein, peptide N-acetyltransferase. | 0.872 |
| RPA0453 | RPA0452 | RPA0453 | RPA0452 | Possible NifU-like domain (residues 119-187); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Glycoprotease (M22) metalloprotease. | 0.559 |
| RPA0453 | fur-2 | RPA0453 | RPA0450 | Possible NifU-like domain (residues 119-187); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Transcriptional regulator, FUR family; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the Fur family. | 0.451 |
| RPA0453 | miaB | RPA0453 | RPA0448 | Possible NifU-like domain (residues 119-187); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | tRNA-i(6)A37 modification enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.489 |
| RPA0453 | rimI | RPA0453 | RPA0451 | Possible NifU-like domain (residues 119-187); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative RimI protein, peptide N-acetyltransferase. | 0.531 |
| RPA2507 | rimI | RPA2507 | RPA0451 | Possible haloacid dehalogenase. | Putative RimI protein, peptide N-acetyltransferase. | 0.487 |
| RPA3113 | rimI | RPA3113 | RPA0451 | Conserved hypothetical protein; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF nuclease family. | Putative RimI protein, peptide N-acetyltransferase. | 0.443 |
| aceA | aceK | RPA4394 | RPA0347 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.958 |
| aceA | rimI | RPA4394 | RPA0451 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative RimI protein, peptide N-acetyltransferase. | 0.529 |
| aceK | aceA | RPA0347 | RPA4394 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.958 |
| aceK | rimI | RPA0347 | RPA0451 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Putative RimI protein, peptide N-acetyltransferase. | 0.431 |
| fur-2 | RPA0449 | RPA0450 | RPA0449 | Transcriptional regulator, FUR family; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the Fur family. | Possible hydrolases/phosphatases. | 0.684 |