node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DR97_3352 | DR97_3353 | DR97_3352 | DR97_3353 | Hypothetical protein; DUF3392 domain-containing protein | Radical sam superfamily protein; 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 | 0.689 |
DR97_3352 | DR97_3355 | DR97_3352 | DR97_3355 | Hypothetical protein; DUF3392 domain-containing protein | Conserved hypothetical protein | 0.524 |
DR97_3352 | rdgB | DR97_3352 | DR97_3354 | Hypothetical protein; DUF3392 domain-containing protein | Non-canonical purine ntp pyrophosphatase, rdgb/ham1 family; 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 | 0.535 |
DR97_3353 | DR97_3352 | DR97_3353 | DR97_3352 | Radical sam superfamily protein; 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 | Hypothetical protein; DUF3392 domain-containing protein | 0.689 |
DR97_3353 | DR97_3355 | DR97_3353 | DR97_3355 | Radical sam superfamily protein; 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 | Conserved hypothetical protein | 0.688 |
DR97_3353 | DR97_3362 | DR97_3353 | DR97_3362 | Radical sam superfamily protein; 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 | Plp dependent protein; Perhaps involved in proline biosynthesis | 0.669 |
DR97_3353 | metW | DR97_3353 | DR97_3356 | Radical sam superfamily protein; 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 | Putative methionine biosynthesis protein; metW: methionine biosynthesis protein MetW | 0.602 |
DR97_3353 | mltF | DR97_3353 | DR97_4111 | Radical sam superfamily protein; 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 | Bacterial extracellular solute-binding s, 3 family protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella | 0.581 |
DR97_3353 | pnp | DR97_3353 | DR97_2083 | Radical sam superfamily protein; 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 | Polynucleotide phosphorylase/polyadenylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction | 0.710 |
DR97_3353 | rdgB | DR97_3353 | DR97_3354 | Radical sam superfamily protein; 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 | Non-canonical purine ntp pyrophosphatase, rdgb/ham1 family; 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 | 0.717 |
DR97_3353 | rlmN | DR97_3353 | DR97_4063 | Radical sam superfamily protein; 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 | 23S rRNA (adenine2503-C2)-methyltransferase; 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 | 0.680 |
DR97_3353 | rph | DR97_3353 | DR97_2705 | Radical sam superfamily protein; 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 | 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 | 0.704 |
DR97_3353 | rpoA | DR97_3353 | DR97_3673 | Radical sam superfamily protein; 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 | Dna-directed rna polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | 0.683 |
DR97_3355 | DR97_3352 | DR97_3355 | DR97_3352 | Conserved hypothetical protein | Hypothetical protein; DUF3392 domain-containing protein | 0.524 |
DR97_3355 | DR97_3353 | DR97_3355 | DR97_3353 | Conserved hypothetical protein | Radical sam superfamily protein; 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 | 0.688 |
DR97_3355 | DR97_3362 | DR97_3355 | DR97_3362 | Conserved hypothetical protein | Plp dependent protein; Perhaps involved in proline biosynthesis | 0.469 |
DR97_3355 | metW | DR97_3355 | DR97_3356 | Conserved hypothetical protein | Putative methionine biosynthesis protein; metW: methionine biosynthesis protein MetW | 0.923 |
DR97_3355 | rdgB | DR97_3355 | DR97_3354 | Conserved hypothetical protein | Non-canonical purine ntp pyrophosphatase, rdgb/ham1 family; 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 | 0.894 |
DR97_3362 | DR97_3353 | DR97_3362 | DR97_3353 | Plp dependent protein; Perhaps involved in proline biosynthesis | Radical sam superfamily protein; 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 | 0.669 |
DR97_3362 | DR97_3355 | DR97_3362 | DR97_3355 | Plp dependent protein; Perhaps involved in proline biosynthesis | Conserved hypothetical protein | 0.469 |