| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| F09E5.3 | K02D7.1 | F09E5.3 | K02D7.1b | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Purine nucleoside 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 | 0.954 |
| F09E5.3 | R11H6.5 | F09E5.3 | R11H6.5 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Protein R11H6.5 (R11H6.5) mRNA, complete cds | 0.900 |
| F09E5.3 | T19B4.3 | F09E5.3 | T19B4.3 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis; Belongs to the purine/pyrimidine phosphoribosyltransferase family | 0.928 |
| F09E5.3 | T22F3.3 | F09E5.3 | T22F3.3a | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Alpha-1,4 glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties | 0.921 |
| F09E5.3 | cdd-1 | F09E5.3 | C47D2.2 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2’-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family | 0.952 |
| F09E5.3 | cku-70 | F09E5.3 | Y47D3A.4 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Protein CKU-70 (cku-70) mRNA, complete cds | 0.900 |
| F09E5.3 | cku-80 | F09E5.3 | R07E5.8.2 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | ATP-dependent DNA helicase II subunit 2; Single-stranded DNA-dependent ATP-dependent helicase | 0.900 |
| F09E5.3 | thk-1 | F09E5.3 | Y43C5A.5a | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Thymidine kinase; Protein THK-1, isoform a | 0.620 |
| F09E5.3 | upp-1 | F09E5.3 | ZK783.2 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | Uridine and thymidine phosphorylase; Catalyzes the reversible phosphorylytic cleavage of uridine and thymidine to uracil and ribose-phosphate or thymine and deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable). Required for normal lifespan; Belongs to the PNP/UDP phosphorylase family | 0.650 |
| F19B6.1 | K02D7.1 | F19B6.1d | K02D7.1b | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Purine nucleoside 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 | 0.634 |
| F19B6.1 | T19B4.3 | F19B6.1d | T19B4.3 | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis; Belongs to the purine/pyrimidine phosphoribosyltransferase family | 0.450 |
| F19B6.1 | T22F3.3 | F19B6.1d | T22F3.3a | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Alpha-1,4 glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties | 0.604 |
| F19B6.1 | cdd-1 | F19B6.1d | C47D2.2 | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2’-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family | 0.973 |
| F19B6.1 | thk-1 | F19B6.1d | Y43C5A.5a | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Thymidine kinase; Protein THK-1, isoform a | 0.454 |
| F19B6.1 | upp-1 | F19B6.1d | ZK783.2 | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | Uridine and thymidine phosphorylase; Catalyzes the reversible phosphorylytic cleavage of uridine and thymidine to uracil and ribose-phosphate or thymine and deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable). Required for normal lifespan; Belongs to the PNP/UDP phosphorylase family | 0.974 |
| K02D7.1 | F09E5.3 | K02D7.1b | F09E5.3 | Purine nucleoside 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 | Putative deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- D-ribose 5-phosphate | 0.954 |
| K02D7.1 | F19B6.1 | K02D7.1b | F19B6.1d | Purine nucleoside 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 | Uridine kinase; Protein F19B6.1, isoform d; Belongs to the uridine kinase family | 0.634 |
| K02D7.1 | R11H6.5 | K02D7.1b | R11H6.5 | Purine nucleoside 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 | Protein R11H6.5 (R11H6.5) mRNA, complete cds | 0.900 |
| K02D7.1 | T19B4.3 | K02D7.1b | T19B4.3 | Purine nucleoside 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 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis; Belongs to the purine/pyrimidine phosphoribosyltransferase family | 0.975 |
| K02D7.1 | T22F3.3 | K02D7.1b | T22F3.3a | Purine nucleoside 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 | Alpha-1,4 glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties | 0.968 |
