node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
APA95558.1 | APA97957.1 | NS506_01487 | NS506_03908 | Putative acyl-CoA dehydrogenase AidB; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro; Belongs to the acyl-CoA dehydrogenase family. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.442 |
APA97895.1 | APA97957.1 | NS506_03846 | NS506_03908 | Acyl-CoA dehydrogenase only active with R- and S-2- methyl-C15-CoA; Belongs to the acyl-CoA dehydrogenase family; KEGG: mmi:MMAR_0156 acyl-CoA dehydrogenase. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.437 |
APA97955.1 | APA97956.1 | NS506_03906 | NS506_03907 | Hypothetical protein. | Hypothetical protein. | 0.913 |
APA97955.1 | APA97957.1 | NS506_03906 | NS506_03908 | Hypothetical protein. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.434 |
APA97956.1 | APA97955.1 | NS506_03907 | NS506_03906 | Hypothetical protein. | Hypothetical protein. | 0.913 |
APA97956.1 | APA97957.1 | NS506_03907 | NS506_03908 | Hypothetical protein. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.545 |
APA97957.1 | APA95558.1 | NS506_03908 | NS506_01487 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Putative acyl-CoA dehydrogenase AidB; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro; Belongs to the acyl-CoA dehydrogenase family. | 0.442 |
APA97957.1 | APA97895.1 | NS506_03908 | NS506_03846 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Acyl-CoA dehydrogenase only active with R- and S-2- methyl-C15-CoA; Belongs to the acyl-CoA dehydrogenase family; KEGG: mmi:MMAR_0156 acyl-CoA dehydrogenase. | 0.437 |
APA97957.1 | APA97955.1 | NS506_03908 | NS506_03906 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Hypothetical protein. | 0.434 |
APA97957.1 | APA97956.1 | NS506_03908 | NS506_03907 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Hypothetical protein. | 0.545 |
APA97957.1 | nudC | NS506_03908 | NS506_02183 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | NAD(+) diphosphatase; Belongs to the Nudix hydrolase family. NudC subfamily; Contains 1 nudix hydrolase domain; KEGG: ncy:NOCYR_4263 NAD+ diphosphatase. | 0.410 |
APA97957.1 | pdxS | NS506_03908 | NS506_03894 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | 0.551 |
APA97957.1 | pdxT | NS506_03908 | NS506_03910 | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | 0.532 |
nudC | APA97957.1 | NS506_02183 | NS506_03908 | NAD(+) diphosphatase; Belongs to the Nudix hydrolase family. NudC subfamily; Contains 1 nudix hydrolase domain; KEGG: ncy:NOCYR_4263 NAD+ diphosphatase. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.410 |
pdxS | APA97957.1 | NS506_03894 | NS506_03908 | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.551 |
pdxS | pdxT | NS506_03894 | NS506_03910 | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | 0.999 |
pdxT | APA97957.1 | NS506_03910 | NS506_03908 | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation; Belon [...] | 0.532 |
pdxT | pdxS | NS506_03910 | NS506_03894 | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing); Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | 0.999 |