| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bvgS | gltB | plu2284 | plu4009 | Virulence sensor protein BvgS precursor. | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | 0.515 |
| bvgS | plu1176 | plu2284 | plu1176 | Virulence sensor protein BvgS 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. | 0.478 |
| gltB | bvgS | plu4009 | plu2284 | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | Virulence sensor protein BvgS precursor. | 0.515 |
| gltB | miaB | plu4009 | plu1312 | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | tRNA-methylthiotransferase MiaB protein; 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. | 0.400 |
| gltB | plu1176 | plu4009 | plu1176 | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | 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. | 0.477 |
| gltB | proC | plu4009 | plu1179 | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | Pyrroline-5-carboxylate reductase (P5CR) (P5C reductase); Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.478 |
| miaB | gltB | plu1312 | plu4009 | tRNA-methylthiotransferase MiaB protein; 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. | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | 0.400 |
| miaB | plu1176 | plu1312 | plu1176 | tRNA-methylthiotransferase MiaB protein; 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. | 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. | 0.656 |
| miaB | plu4068 | plu1312 | plu4068 | tRNA-methylthiotransferase MiaB protein; 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. | dTTP/UTP pyrophosphatase; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.421 |
| miaB | rlmN | plu1312 | plu1373 | tRNA-methylthiotransferase MiaB protein; 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. | Dual-specificity RNA methyltransferase RlmN; 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. | 0.744 |
| plu1176 | bvgS | plu1176 | plu2284 | 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. | Virulence sensor protein BvgS precursor. | 0.478 |
| plu1176 | gltB | plu1176 | plu4009 | 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. | Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain). | 0.477 |
| plu1176 | miaB | plu1176 | plu1312 | 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. | tRNA-methylthiotransferase MiaB protein; 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. | 0.656 |
| plu1176 | plu1177 | plu1176 | plu1177 | 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. | dITP/XTP pyrophosphatase; 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. | 0.919 |
| plu1176 | plu1178 | plu1176 | plu1178 | 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. | Unnamed protein product; Similar to putative resistance protein YggT of Escherichia coli. | 0.729 |
| plu1176 | plu1180 | plu1176 | plu1180 | 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. | Pyridoxal phosphate homeostasis protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. | 0.824 |
| plu1176 | plu1181 | plu1176 | plu1181 | 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. | T2SP_E domain-containing protein; Unnamed protein product; Similar to putative protein transporter YggR of Escherichia coli. | 0.561 |
| plu1176 | plu4068 | plu1176 | plu4068 | 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. | dTTP/UTP pyrophosphatase; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.541 |
| plu1176 | proC | plu1176 | plu1179 | 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. | Pyrroline-5-carboxylate reductase (P5CR) (P5C reductase); Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.729 |
| plu1176 | rlmN | plu1176 | plu1373 | 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. | Dual-specificity RNA methyltransferase RlmN; 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. | 0.663 |