| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| lepA | nuoCD | bbp_241 | bbp_145 | 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. | NADH dehydrogenase I chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.487 |
| lepA | pta | bbp_241 | bbp_165 | 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. | Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family. | 0.463 |
| lepA | yggW | bbp_241 | bbp_498 | 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. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.443 |
| mfd | yggW | bbp_275 | bbp_498 | Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site (By similarity); In the N-terminal section; belongs to the UvrB family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.416 |
| nuoCD | lepA | bbp_145 | bbp_241 | NADH dehydrogenase I chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit 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. | 0.487 |
| nuoCD | yggW | bbp_145 | bbp_498 | NADH dehydrogenase I chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.445 |
| nuoCD | yhgI | bbp_145 | bbp_486 | NADH dehydrogenase I chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | YhgI; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | 0.621 |
| pta | lepA | bbp_165 | bbp_241 | Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ 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. | 0.463 |
| pta | yggW | bbp_165 | bbp_498 | Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.565 |
| yfgB | yggW | bbp_265 | bbp_498 | Conserved hypothetical protein; 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. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.553 |
| yfgB | yleA | bbp_265 | bbp_392 | Conserved hypothetical protein; 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. | Hypothetical 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. | 0.469 |
| yggS | yggW | bbp_497 | bbp_498 | Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 0.622 |
| yggW | lepA | bbp_498 | bbp_241 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | 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. | 0.443 |
| yggW | mfd | bbp_498 | bbp_275 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site (By similarity); In the N-terminal section; belongs to the UvrB family. | 0.416 |
| yggW | nuoCD | bbp_498 | bbp_145 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | NADH dehydrogenase I chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.445 |
| yggW | pta | bbp_498 | bbp_165 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family. | 0.565 |
| yggW | yfgB | bbp_498 | bbp_265 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Conserved hypothetical protein; 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. | 0.553 |
| yggW | yggS | bbp_498 | bbp_497 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.622 |
| yggW | yhgI | bbp_498 | bbp_486 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | YhgI; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | 0.429 |
| yggW | yleA | bbp_498 | bbp_392 | Putative oxidase; Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily. | Hypothetical 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. | 0.428 |
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