| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM3334 | ygdH | STM3334 | STM2969 | Similar to E. coli cytosine deaminase (AAC73440.1); Blastp hit to AAC73440.1 (427 aa), 83% identity in aa 1 - 427. | Putative nucleotide binding; Similar to E. coli orf, hypothetical protein (AAC75837.1); Blastp hit to AAC75837.1 (454 aa), 94% identity in aa 1 - 453. | 0.913 |
| amn | apt | STM2009 | STM0483 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.913 |
| amn | surE | STM2009 | STM2927 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | 0.900 |
| amn | xapA | STM2009 | STM2422 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | Xanthosine phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.912 |
| amn | ygdH | STM2009 | STM2969 | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | Putative nucleotide binding; Similar to E. coli orf, hypothetical protein (AAC75837.1); Blastp hit to AAC75837.1 (454 aa), 94% identity in aa 1 - 453. | 0.911 |
| apt | amn | STM0483 | STM2009 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | 0.913 |
| apt | surE | STM0483 | STM2927 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | 0.925 |
| apt | xapA | STM0483 | STM2422 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Xanthosine phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.930 |
| apt | ygdH | STM0483 | STM2969 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Putative nucleotide binding; Similar to E. coli orf, hypothetical protein (AAC75837.1); Blastp hit to AAC75837.1 (454 aa), 94% identity in aa 1 - 453. | 0.907 |
| surE | amn | STM2927 | STM2009 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. | 0.900 |
| surE | apt | STM2927 | STM0483 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.925 |
| surE | tdk | STM2927 | STM1750 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Similar to E. coli thymidine kinase (AAC74320.1); Blastp hit to AAC74320.1 (205 aa), 92% identity in aa 1 - 204. | 0.900 |
| surE | thyA | STM2927 | STM3001 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Thymidylate synthetase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | 0.926 |
| surE | xapA | STM2927 | STM2422 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Xanthosine phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.911 |
| surE | yfbR | STM2927 | STM2332 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Putative hydrolase of HD superfamily; Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. | 0.964 |
| surE | ygdH | STM2927 | STM2969 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Putative nucleotide binding; Similar to E. coli orf, hypothetical protein (AAC75837.1); Blastp hit to AAC75837.1 (454 aa), 94% identity in aa 1 - 453. | 0.908 |
| surE | ygjP | STM2927 | STM3221 | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | Putative metal-dependent hydrolase; Similar to E. coli orf, hypothetical protein (AAC76120.1); Blastp hit to AAC76120.1 (179 aa), 88% identity in aa 13 - 174. | 0.900 |
| tdk | surE | STM1750 | STM2927 | Similar to E. coli thymidine kinase (AAC74320.1); Blastp hit to AAC74320.1 (205 aa), 92% identity in aa 1 - 204. | Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. | 0.900 |
| tdk | thyA | STM1750 | STM3001 | Similar to E. coli thymidine kinase (AAC74320.1); Blastp hit to AAC74320.1 (205 aa), 92% identity in aa 1 - 204. | Thymidylate synthetase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | 0.992 |
| tdk | yfbR | STM1750 | STM2332 | Similar to E. coli thymidine kinase (AAC74320.1); Blastp hit to AAC74320.1 (205 aa), 92% identity in aa 1 - 204. | Putative hydrolase of HD superfamily; Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. | 0.901 |