| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lgee_0800 | hemN | Lgee_0800 | Lgee_0400 | Pyridoxal-5'-phosphate dependent enzyme family transporter protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.479 |
| Lgee_0800 | yfgB | Lgee_0800 | Lgee_0235 | Pyridoxal-5'-phosphate dependent enzyme family transporter protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Fe-S containing enzyme; 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. | 0.530 |
| flgF_2 | hemN | Lgee_1280 | Lgee_0400 | Flagellar basal body rod protein FlgF. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.492 |
| hemE | hemN | Lgee_0637 | Lgee_0400 | Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.711 |
| hemN | Lgee_0800 | Lgee_0400 | Lgee_0800 | Oxygen-independent coproporphyrinogen III oxidase; 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-5'-phosphate dependent enzyme family transporter protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.479 |
| hemN | flgF_2 | Lgee_0400 | Lgee_1280 | Oxygen-independent coproporphyrinogen III oxidase; 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. | Flagellar basal body rod protein FlgF. | 0.492 |
| hemN | hemE | Lgee_0400 | Lgee_0637 | Oxygen-independent coproporphyrinogen III oxidase; 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 decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.711 |
| hemN | lepA-2 | Lgee_0400 | Lgee_1144 | Oxygen-independent coproporphyrinogen III oxidase; 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. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.481 |
| hemN | mdh | Lgee_0400 | Lgee_0402 | Oxygen-independent coproporphyrinogen III oxidase; 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. | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. | 0.763 |
| hemN | miaB | Lgee_0400 | Lgee_0984 | Oxygen-independent coproporphyrinogen III oxidase; 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. | (dimethylallyl)adenosine tRNA 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. | 0.520 |
| hemN | nudE | Lgee_0400 | Lgee_0401 | Oxygen-independent coproporphyrinogen III oxidase; 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. | NUDIX hydrolase. | 0.763 |
| hemN | plsY | Lgee_0400 | Lgee_0399 | Oxygen-independent coproporphyrinogen III oxidase; 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. | Transmembrane protein; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | 0.801 |
| hemN | pnp | Lgee_0400 | Lgee_0318 | Oxygen-independent coproporphyrinogen III oxidase; 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. | Polynucleotide phosphorylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.467 |
| hemN | yfgB | Lgee_0400 | Lgee_0235 | Oxygen-independent coproporphyrinogen III oxidase; 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. | Fe-S containing enzyme; 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. | 0.711 |
| lepA-2 | hemN | Lgee_1144 | Lgee_0400 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.481 |
| lepA-2 | miaB | Lgee_1144 | Lgee_0984 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | (dimethylallyl)adenosine tRNA 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. | 0.589 |
| mdh | hemN | Lgee_0402 | Lgee_0400 | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.763 |
| mdh | nudE | Lgee_0402 | Lgee_0401 | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. | NUDIX hydrolase. | 0.863 |
| mdh | plsY | Lgee_0402 | Lgee_0399 | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. | Transmembrane protein; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | 0.741 |
| miaB | hemN | Lgee_0984 | Lgee_0400 | (dimethylallyl)adenosine tRNA 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. | Oxygen-independent coproporphyrinogen III oxidase; 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. | 0.520 |