node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Ahcy | AhcyL1 | FBpp0312000 | FBpp0072886 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.936 |
Ahcy | AhcyL2 | FBpp0312000 | FBpp0089085 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.913 |
Ahcy | CG10621 | FBpp0312000 | FBpp0309709 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | FI01821p; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.931 |
Ahcy | CG10623 | FBpp0312000 | FBpp0311160 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.959 |
Ahcy | CG31800 | FBpp0312000 | FBpp0080721 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Uncharacterized protein. | 0.877 |
Ahcy | Cbs | FBpp0312000 | FBpp0076938 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.979 |
Ahcy | Eip55E | FBpp0312000 | FBpp0311547 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.955 |
Ahcy | Kyat | FBpp0312000 | FBpp0081994 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Kynurenine aminotransferase, isoform A; Pyridoxal phosphate binding; cysteine-S-conjugate beta-lyase activity; kynurenine-oxoglutarate transaminase activity. It is involved in the biological process described with: biosynthetic process; kynurenine metabolic process. | 0.927 |
Ahcy | Sam-S | FBpp0312000 | FBpp0088450 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. | 0.855 |
Ahcy | Srr | FBpp0312000 | FBpp0081504 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Serine racemase, isoform B; Serine racemase activity; L-serine ammonia-lyase activity; L-threonine ammonia-lyase activity. It is involved in the biological process described with: threonine catabolic process; L-serine catabolic process. | 0.833 |
AhcyL1 | Ahcy | FBpp0072886 | FBpp0312000 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | 0.936 |
AhcyL1 | AhcyL2 | FBpp0072886 | FBpp0089085 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.940 |
AhcyL1 | CG10621 | FBpp0072886 | FBpp0309709 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | FI01821p; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.931 |
AhcyL1 | CG10623 | FBpp0072886 | FBpp0311160 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.931 |
AhcyL1 | Cbs | FBpp0072886 | FBpp0076938 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.973 |
AhcyL1 | Eip55E | FBpp0072886 | FBpp0311547 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.904 |
AhcyL1 | Kyat | FBpp0072886 | FBpp0081994 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Kynurenine aminotransferase, isoform A; Pyridoxal phosphate binding; cysteine-S-conjugate beta-lyase activity; kynurenine-oxoglutarate transaminase activity. It is involved in the biological process described with: biosynthetic process; kynurenine metabolic process. | 0.916 |
AhcyL1 | Sam-S | FBpp0072886 | FBpp0088450 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. | 0.862 |
AhcyL1 | Srr | FBpp0072886 | FBpp0081504 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Serine racemase, isoform B; Serine racemase activity; L-serine ammonia-lyase activity; L-threonine ammonia-lyase activity. It is involved in the biological process described with: threonine catabolic process; L-serine catabolic process. | 0.833 |
AhcyL2 | Ahcy | FBpp0089085 | FBpp0312000 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | 0.913 |