| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_0169 | BF49_0170 | BF49_0169 | BF49_0170 | Nucleoside 5triphosphatase RdgB dHAPTP dITP XTPspecific EC 36115; 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. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.922 |
| BF49_0169 | hrcA | BF49_0169 | BF49_0167 | Nucleoside 5triphosphatase RdgB dHAPTP dITP XTPspecific EC 36115; 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. | Heatinducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.554 |
| BF49_0169 | rph | BF49_0169 | BF49_0168 | Nucleoside 5triphosphatase RdgB dHAPTP dITP XTPspecific EC 36115; 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. | Ribonuclease PH EC 27756; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.993 |
| BF49_0170 | BF49_0169 | BF49_0170 | BF49_0169 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Nucleoside 5triphosphatase RdgB dHAPTP dITP XTPspecific EC 36115; 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. | 0.922 |
| BF49_0170 | BF49_0327 | BF49_0170 | BF49_0327 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribosomal RNA large subunit methyltransferase N EC 211. | 0.724 |
| BF49_0170 | BF49_1925 | BF49_0170 | BF49_1925 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Cytochrome c oxidase subunit CcoN EC 1931; Belongs to the heme-copper respiratory oxidase family. | 0.684 |
| BF49_0170 | BF49_3351 | BF49_0170 | BF49_3351 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Outer membrane protein W precursor. | 0.674 |
| BF49_0170 | BF49_7356 | BF49_0170 | BF49_7356 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNAi6A37 methylthiotransferase. | 0.602 |
| BF49_0170 | hemE | BF49_0170 | BF49_2403 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Uroporphyrinogen III decarboxylase EC 41137; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.662 |
| BF49_0170 | hrcA | BF49_0170 | BF49_0167 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Heatinducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.620 |
| BF49_0170 | miaB | BF49_0170 | BF49_0031 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNAi6A37 methylthiotransferase; 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. | 0.602 |
| BF49_0170 | rlmN | BF49_0170 | BF49_0320 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribosomal RNA large subunit methyltransferase N EC 211; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.724 |
| BF49_0170 | rph | BF49_0170 | BF49_0168 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribonuclease PH EC 27756; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.814 |
| BF49_0327 | BF49_0170 | BF49_0327 | BF49_0170 | Ribosomal RNA large subunit methyltransferase N EC 211. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.724 |
| BF49_0327 | BF49_7356 | BF49_0327 | BF49_7356 | Ribosomal RNA large subunit methyltransferase N EC 211. | tRNAi6A37 methylthiotransferase. | 0.738 |
| BF49_0327 | hemE | BF49_0327 | BF49_2403 | Ribosomal RNA large subunit methyltransferase N EC 211. | Uroporphyrinogen III decarboxylase EC 41137; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.457 |
| BF49_0327 | miaB | BF49_0327 | BF49_0031 | Ribosomal RNA large subunit methyltransferase N EC 211. | tRNAi6A37 methylthiotransferase; 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. | 0.738 |
| BF49_1925 | BF49_0170 | BF49_1925 | BF49_0170 | Cytochrome c oxidase subunit CcoN EC 1931; Belongs to the heme-copper respiratory oxidase family. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.684 |
| BF49_1925 | BF49_3351 | BF49_1925 | BF49_3351 | Cytochrome c oxidase subunit CcoN EC 1931; Belongs to the heme-copper respiratory oxidase family. | Outer membrane protein W precursor. | 0.864 |
| BF49_3351 | BF49_0170 | BF49_3351 | BF49_0170 | Outer membrane protein W precursor. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.674 |