node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95265.1 | tyrDC | ZOBELLIA_1209 | ZOBELLIA_3227 | FAD-dependent amine oxidoreductase of unknown substrate specificity; Belongs to the amine oxydase family; Localized in the cytoplasm; Specificity unclear. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.912 |
CAZ95622.1 | tyrDC | ZOBELLIA_1567 | ZOBELLIA_3227 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.841 |
CAZ96431.1 | tdoA1 | ZOBELLIA_2275 | ZOBELLIA_300 | N-formylkynurenine (aryl-) formamidase is an enzyme involved in the tryptophan metabolism. It hydrolyses the N-formyl-L-kynurenine to L-kynurenine and formate; belongs to the cyclase family; Localized in the cytoplasm; High confidence in function and specificity. | Tryptophan 2,3-dioxygenase is Involved in L-kynurenine metabolism from L-tryptophan,incorporating oxygen into the indole moiety of tryptophan. It has a broad specificity towards tryptamine and derivatives including D-and L-tryptophan, 5-hydroxytryptophan and serotonin; This enzyme forms a tetramer and binds 2 hemes per subunit; Localized in the cytoplasm; High confidence in function and specificity. | 0.972 |
CAZ96431.1 | tdoA2 | ZOBELLIA_2275 | ZOBELLIA_1440 | N-formylkynurenine (aryl-) formamidase is an enzyme involved in the tryptophan metabolism. It hydrolyses the N-formyl-L-kynurenine to L-kynurenine and formate; belongs to the cyclase family; Localized in the cytoplasm; High confidence in function and specificity. | Tryptophan 2,3-dioxygenase is Involved in L-kynurenine metabolism from L-tryptophan,incorporating oxygen into the indole moiety of tryptophan. It has a broad specificity towards tryptamine and derivatives including D-and L-tryptophan, 5-hydroxytryptophan and serotonin; This enzyme forms a tetramer and binds 2 hemes per subunit; Localized in the cytoplasm; High confidence in function and specificity. | 0.973 |
CAZ96431.1 | tyrDC | ZOBELLIA_2275 | ZOBELLIA_3227 | N-formylkynurenine (aryl-) formamidase is an enzyme involved in the tryptophan metabolism. It hydrolyses the N-formyl-L-kynurenine to L-kynurenine and formate; belongs to the cyclase family; Localized in the cytoplasm; High confidence in function and specificity. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
aatA-2 | aatB | ZOBELLIA_756 | ZOBELLIA_705 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.916 |
aatA-2 | hisC | ZOBELLIA_756 | ZOBELLIA_4514 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | 0.823 |
aatA-2 | hisC2 | ZOBELLIA_756 | ZOBELLIA_2870 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity. | 0.823 |
aatA-2 | phhA | ZOBELLIA_756 | ZOBELLIA_969 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Phenylalanine 4-monooxygenase, also known as phenylalanine-4-hydroxylase, is involved in L-phenylalanine biodegradation. It catalyzes the reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. It binds Fe(2+) ion as a cofactor. PhhA belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Localized in the cytoplasm; High confidence in function and specificity. | 0.908 |
aatA-2 | tyrDC | ZOBELLIA_756 | ZOBELLIA_3227 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.906 |
aatB | aatA-2 | ZOBELLIA_705 | ZOBELLIA_756 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.916 |
aatB | hisC | ZOBELLIA_705 | ZOBELLIA_4514 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | 0.835 |
aatB | hisC2 | ZOBELLIA_705 | ZOBELLIA_2870 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity. | 0.823 |
aatB | phhA | ZOBELLIA_705 | ZOBELLIA_969 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Phenylalanine 4-monooxygenase, also known as phenylalanine-4-hydroxylase, is involved in L-phenylalanine biodegradation. It catalyzes the reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. It binds Fe(2+) ion as a cofactor. PhhA belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Localized in the cytoplasm; High confidence in function and specificity. | 0.908 |
aatB | tyrDC | ZOBELLIA_705 | ZOBELLIA_3227 | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.906 |
hisC | aatA-2 | ZOBELLIA_4514 | ZOBELLIA_756 | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.823 |
hisC | aatB | ZOBELLIA_4514 | ZOBELLIA_705 | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.835 |
hisC | hisC2 | ZOBELLIA_4514 | ZOBELLIA_2870 | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity. | 0.911 |
hisC | phhA | ZOBELLIA_4514 | ZOBELLIA_969 | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | Phenylalanine 4-monooxygenase, also known as phenylalanine-4-hydroxylase, is involved in L-phenylalanine biodegradation. It catalyzes the reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. It binds Fe(2+) ion as a cofactor. PhhA belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Localized in the cytoplasm; High confidence in function and specificity. | 0.908 |
hisC | tyrDC | ZOBELLIA_4514 | ZOBELLIA_3227 | The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity. | Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.901 |