| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ97893.1 | CAZ97894.1 | ZOBELLIA_3755 | ZOBELLIA_3756 | The hydrolases of the superfamily HAD (Haloacid dehalogenase) catalyse a nucleophilic displacement reaction, with water as the sole co-substrate. They are structurally different from the alpha/beta hydrolase family (abhydrolase); Belongs to the haloacid dehalogenase- like hydrolase superfamily; Localized in the cytoplasm; Family membership. | 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. | 0.976 |
| CAZ97893.1 | CAZ97896.1 | ZOBELLIA_3755 | ZOBELLIA_3758 | The hydrolases of the superfamily HAD (Haloacid dehalogenase) catalyse a nucleophilic displacement reaction, with water as the sole co-substrate. They are structurally different from the alpha/beta hydrolase family (abhydrolase); Belongs to the haloacid dehalogenase- like hydrolase superfamily; Localized in the cytoplasm; Family membership. | Conserved protein involved in exopolysaccharide biosynthesis. Its exact function is unknown. Contains a N-terminal transmembrane helix. Localized in the cytoplasmic membrane; Function unclear. | 0.816 |
| CAZ97894.1 | CAZ97893.1 | ZOBELLIA_3756 | ZOBELLIA_3755 | 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. | The hydrolases of the superfamily HAD (Haloacid dehalogenase) catalyse a nucleophilic displacement reaction, with water as the sole co-substrate. They are structurally different from the alpha/beta hydrolase family (abhydrolase); Belongs to the haloacid dehalogenase- like hydrolase superfamily; Localized in the cytoplasm; Family membership. | 0.976 |
| CAZ97894.1 | CAZ97896.1 | ZOBELLIA_3756 | ZOBELLIA_3758 | 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. | Conserved protein involved in exopolysaccharide biosynthesis. Its exact function is unknown. Contains a N-terminal transmembrane helix. Localized in the cytoplasmic membrane; Function unclear. | 0.948 |
| CAZ97894.1 | argG | ZOBELLIA_3756 | ZOBELLIA_1228 | 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. | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.948 |
| 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 | 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 | 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 | 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 |
| CAZ97894.1 | pyrB | ZOBELLIA_3756 | ZOBELLIA_504 | 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. | Aspartate carbamoyltransferase catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate (). This is the second step in the de novo biosynthesis of pyrimidine nucleotides; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.975 |
| CAZ97896.1 | CAZ97893.1 | ZOBELLIA_3758 | ZOBELLIA_3755 | Conserved protein involved in exopolysaccharide biosynthesis. Its exact function is unknown. Contains a N-terminal transmembrane helix. Localized in the cytoplasmic membrane; Function unclear. | The hydrolases of the superfamily HAD (Haloacid dehalogenase) catalyse a nucleophilic displacement reaction, with water as the sole co-substrate. They are structurally different from the alpha/beta hydrolase family (abhydrolase); Belongs to the haloacid dehalogenase- like hydrolase superfamily; Localized in the cytoplasm; Family membership. | 0.816 |
| CAZ97896.1 | CAZ97894.1 | ZOBELLIA_3758 | ZOBELLIA_3756 | Conserved protein involved in exopolysaccharide biosynthesis. Its exact function is unknown. Contains a N-terminal transmembrane helix. Localized in the cytoplasmic membrane; Function unclear. | 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. | 0.948 |
| argG | CAZ97894.1 | ZOBELLIA_1228 | ZOBELLIA_3756 | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; 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. | 0.948 |
| argG | carA | ZOBELLIA_1228 | ZOBELLIA_2537 | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; 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. | 0.917 |
| argG | gltA-2 | ZOBELLIA_1228 | ZOBELLIA_909 | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 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 [...] | 0.524 |
| argG | pyrB | ZOBELLIA_1228 | ZOBELLIA_504 | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity. | Aspartate carbamoyltransferase catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate (). This is the second step in the de novo biosynthesis of pyrimidine nucleotides; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.910 |
| 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 | argG | ZOBELLIA_2537 | ZOBELLIA_1228 | 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. | Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.917 |