node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95796.1 | asnB1 | ZOBELLIA_1743 | ZOBELLIA_2743 | Conserved hypothetical protein; Localized in the cytoplasm. | Asparagine synthase (glutamine-hdrolysing) catalyses the conversion of aspartate to asparagine from glutamine as amido-N-donor. Contains a N-terminal class-2 glutamine amidotransferase domain (GATase domain). Forms a homodimer. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
CAZ95796.1 | purA | ZOBELLIA_1743 | ZOBELLIA_3674 | Conserved hypothetical protein; Localized in the cytoplasm. | Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. | 0.912 |
CAZ95796.1 | pyrB | ZOBELLIA_1743 | ZOBELLIA_504 | Conserved hypothetical protein; Localized in the cytoplasm. | 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. | 0.912 |
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 | pucH | ZOBELLIA_3756 | ZOBELLIA_1306 | 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. | Allantoinase is involved in purine metabolism. It catalyzes the reaction: (S)-allantoin + H2O = allantoate. Binds one zinc ion. Localized in the cytoplasm; High confidence in function and specificity. | 0.739 |
CAZ97894.1 | purA | ZOBELLIA_3756 | ZOBELLIA_3674 | 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. | Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. | 0.484 |
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 |
CAZ97894.1 | pyrC | ZOBELLIA_3756 | ZOBELLIA_4080 | 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. | Dihydroorotase is involved in Pyrimidine biosynthesis. It catalyzes the reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. It forms a homodimer and binds 2 zinc ions per subunit. Localized in the cytoplasm; High confidence in function and specificity. | 0.739 |
CAZ97894.1 | pyrR1 | ZOBELLIA_3756 | ZOBELLIA_505 | 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. | Bifunctional protein pyrR; PyrR regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. It forms in equilibrium a homodimer and a homohexamer. Localized in the cytoplasm; High confidence in function and specificity. | 0.710 |
CAZ97894.1 | pyrR2 | ZOBELLIA_3756 | ZOBELLIA_3014 | 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. | Bifunctional protein PyrR; PyrR regulates transcriptional attenuation of the pyrimidine nucleotide operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. Forms momodimer and homohexamer in equilibrium. Localized in the cytoplasm; High confidence in function and specificity. | 0.710 |
asnB1 | CAZ95796.1 | ZOBELLIA_2743 | ZOBELLIA_1743 | Asparagine synthase (glutamine-hdrolysing) catalyses the conversion of aspartate to asparagine from glutamine as amido-N-donor. Contains a N-terminal class-2 glutamine amidotransferase domain (GATase domain). Forms a homodimer. Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.900 |
asnB1 | purA | ZOBELLIA_2743 | ZOBELLIA_3674 | Asparagine synthase (glutamine-hdrolysing) catalyses the conversion of aspartate to asparagine from glutamine as amido-N-donor. Contains a N-terminal class-2 glutamine amidotransferase domain (GATase domain). Forms a homodimer. Localized in the cytoplasm; High confidence in function and specificity. | Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. | 0.912 |
asnB1 | pyrB | ZOBELLIA_2743 | ZOBELLIA_504 | Asparagine synthase (glutamine-hdrolysing) catalyses the conversion of aspartate to asparagine from glutamine as amido-N-donor. Contains a N-terminal class-2 glutamine amidotransferase domain (GATase domain). Forms a homodimer. 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. | 0.912 |
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 | pucH | ZOBELLIA_2537 | ZOBELLIA_1306 | 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. | Allantoinase is involved in purine metabolism. It catalyzes the reaction: (S)-allantoin + H2O = allantoate. Binds one zinc ion. Localized in the cytoplasm; High confidence in function and specificity. | 0.981 |
carA | purA | ZOBELLIA_2537 | ZOBELLIA_3674 | 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. | Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. | 0.678 |
carA | pyrB | ZOBELLIA_2537 | ZOBELLIA_504 | 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. | 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. | 0.999 |
carA | pyrC | ZOBELLIA_2537 | ZOBELLIA_4080 | 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. | Dihydroorotase is involved in Pyrimidine biosynthesis. It catalyzes the reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. It forms a homodimer and binds 2 zinc ions per subunit. Localized in the cytoplasm; High confidence in function and specificity. | 0.905 |