node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ97894.1 | carA | ZOBELLIA_3756 | ZOBELLIA_2537 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | 0.996 |
CAZ97894.1 | carB | ZOBELLIA_3756 | ZOBELLIA_72 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
CAZ97894.1 | glmS | ZOBELLIA_3756 | ZOBELLIA_1408 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glucosamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.922 |
CAZ97894.1 | glnA | ZOBELLIA_3756 | ZOBELLIA_2792 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class III which includes GS from Bacteroides fragilis and Butyrivibrio fibrisolvens. GSIII enzymes are much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. It forms a hexamer. Localized in the cytoplasm; High confidence in function and specificity. | 0.909 |
CAZ97894.1 | glnII | ZOBELLIA_3756 | ZOBELLIA_2791 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class II which is usually found in eukaryotes and in bacteria belonging to the Rhizobiaceae, Frankiaceae, and Streptomycetaceae families. GSII are octamer of identical subunits. Localized in the cytoplasm; High confidence in function and specificity. | 0.919 |
CAZ97894.1 | glsA | ZOBELLIA_3756 | ZOBELLIA_4211 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glutaminase catalyzes the reaction: L-glutamine + H2O = L-glutamate + NH3. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
CAZ97894.1 | gltA-2 | ZOBELLIA_3756 | ZOBELLIA_909 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...] | 0.963 |
CAZ97894.1 | gltB | ZOBELLIA_3756 | ZOBELLIA_910 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...] | 0.916 |
CAZ97894.1 | purF | ZOBELLIA_3756 | ZOBELLIA_1585 | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | Amidophosphoribosyltransferase catalyzes the first step in purine biosynthesis: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. PurF belongs to the Class-II glutamine amidotransferase family. It forms a homotetramer and binds one magnesium ion per subunit. Localized in the cytoplasm; High confidence in function and specificity. | 0.963 |
carA | CAZ97894.1 | ZOBELLIA_2537 | ZOBELLIA_3756 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | 0.996 |
carA | carB | ZOBELLIA_2537 | ZOBELLIA_72 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | 0.999 |
carA | glmS | ZOBELLIA_2537 | ZOBELLIA_1408 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glucosamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.915 |
carA | glnA | ZOBELLIA_2537 | ZOBELLIA_2792 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class III which includes GS from Bacteroides fragilis and Butyrivibrio fibrisolvens. GSIII enzymes are much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. It forms a hexamer. Localized in the cytoplasm; High confidence in function and specificity. | 0.912 |
carA | glnII | ZOBELLIA_2537 | ZOBELLIA_2791 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class II which is usually found in eukaryotes and in bacteria belonging to the Rhizobiaceae, Frankiaceae, and Streptomycetaceae families. GSII are octamer of identical subunits. Localized in the cytoplasm; High confidence in function and specificity. | 0.930 |
carA | glsA | ZOBELLIA_2537 | ZOBELLIA_4211 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glutaminase catalyzes the reaction: L-glutamine + H2O = L-glutamate + NH3. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
carA | gltA-2 | ZOBELLIA_2537 | ZOBELLIA_909 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...] | 0.928 |
carA | gltB | ZOBELLIA_2537 | ZOBELLIA_910 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...] | 0.909 |
carA | purF | ZOBELLIA_2537 | ZOBELLIA_1585 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | Amidophosphoribosyltransferase catalyzes the first step in purine biosynthesis: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. PurF belongs to the Class-II glutamine amidotransferase family. It forms a homotetramer and binds one magnesium ion per subunit. Localized in the cytoplasm; High confidence in function and specificity. | 0.968 |
carB | CAZ97894.1 | ZOBELLIA_72 | ZOBELLIA_3756 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear. | 0.900 |
carB | carA | ZOBELLIA_72 | ZOBELLIA_2537 | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family. | 0.999 |