node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
B0228.7 | C47B2.2 | B0228.7.3 | C47B2.2.1 | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | Uncharacterized protein. | 0.516 |
B0228.7 | K02D7.1 | B0228.7.3 | K02D7.1b.1 | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 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. | 0.619 |
B0228.7 | cpin-1 | B0228.7.3 | F38E11.3.1 | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | Amidohydro-rel domain-containing protein. | 0.795 |
B0228.7 | upp-1 | B0228.7.3 | ZK783.2.1 | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 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. | 0.911 |
C44E12.1 | cpin-1 | C44E12.1.1 | F38E11.3.1 | M20_dimer domain-containing protein. | Amidohydro-rel domain-containing protein. | 0.903 |
C47B2.2 | B0228.7 | C47B2.2.1 | B0228.7.3 | Uncharacterized protein. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.516 |
C47B2.2 | K02D7.1 | C47B2.2.1 | K02D7.1b.1 | Uncharacterized protein. | 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. | 0.959 |
C47B2.2 | cpin-1 | C47B2.2.1 | F38E11.3.1 | Uncharacterized protein. | Amidohydro-rel domain-containing protein. | 0.909 |
C47B2.2 | upp-1 | C47B2.2.1 | ZK783.2.1 | Uncharacterized protein. | 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. | 0.989 |
K02D7.1 | B0228.7 | K02D7.1b.1 | B0228.7.3 | 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. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.619 |
K02D7.1 | C47B2.2 | K02D7.1b.1 | C47B2.2.1 | 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. | Uncharacterized protein. | 0.959 |
K02D7.1 | cpin-1 | K02D7.1b.1 | F38E11.3.1 | 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. | Amidohydro-rel domain-containing protein. | 0.864 |
K02D7.1 | upp-1 | K02D7.1b.1 | ZK783.2.1 | 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 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. | 0.989 |
bcs-1 | cpin-1 | F54C9.6a.1 | F38E11.3.1 | BCS1 (Mitochondrial chaperone) homolog; Belongs to the AAA ATPase family. | Amidohydro-rel domain-containing protein. | 0.768 |
bcs-1 | phip-1 | F54C9.6a.1 | F36A2.8.1 | BCS1 (Mitochondrial chaperone) homolog; Belongs to the AAA ATPase family. | Protein HIstidine Phosphatase. | 0.782 |
bcs-1 | pinn-4 | F54C9.6a.1 | Y48C3A.16.1 | BCS1 (Mitochondrial chaperone) homolog; Belongs to the AAA ATPase family. | Peptidyl-prolyl cis-trans isomerase. | 0.822 |
cpin-1 | B0228.7 | F38E11.3.1 | B0228.7.3 | Amidohydro-rel domain-containing protein. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.795 |
cpin-1 | C44E12.1 | F38E11.3.1 | C44E12.1.1 | Amidohydro-rel domain-containing protein. | M20_dimer domain-containing protein. | 0.903 |
cpin-1 | C47B2.2 | F38E11.3.1 | C47B2.2.1 | Amidohydro-rel domain-containing protein. | Uncharacterized protein. | 0.909 |
cpin-1 | K02D7.1 | F38E11.3.1 | K02D7.1b.1 | Amidohydro-rel domain-containing protein. | 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. | 0.864 |