| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94937.1 | hdc | ZOBELLIA_872 | ZOBELLIA_4435 | Conserved hypothetical protein; Localized in the cytoplasm. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. 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 |
| CAZ94937.1 | hisD | ZOBELLIA_872 | ZOBELLIA_4515 | Conserved hypothetical protein; Localized in the cytoplasm. | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | 0.900 |
| CAZ94937.1 | hutH | ZOBELLIA_872 | ZOBELLIA_2081 | Conserved hypothetical protein; Localized in the cytoplasm. | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
| CAZ97894.1 | hdc | ZOBELLIA_3756 | ZOBELLIA_4435 | 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. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.541 |
| CAZ98569.1 | hdc | ZOBELLIA_4434 | ZOBELLIA_4435 | Protein homologous to the C-terminal domain of the deaminase-reductase RidB. The exact function of this protein is unknown; Localized in the cytoplasm; Function unclear. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.486 |
| CAZ98571.1 | hdc | ZOBELLIA_4436 | ZOBELLIA_4435 | The AsnC/Lrp-type transcriptional regulator family appears to be an important regulatory system of the amino acid metabolism and related processes; Contains a N-terminal DNA binding AsnC/Lrp-type HTH domain. The C-terminal part contains an effector-binding domain and/or an oligomerization domain; Localized in the cytoplasm; Family membership. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.528 |
| ddc | hdc | ZOBELLIA_4235 | ZOBELLIA_4435 | L-2,4-diaminobutyrate decarboxylase catalyzes the reaction : L-2,4-diaminobutanoate = propane-1,3-diamine + CO2. It is involved in 1,3-diaminopropane biosynthesis. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.631 |
| hdc | CAZ94937.1 | ZOBELLIA_4435 | ZOBELLIA_872 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.900 |
| hdc | CAZ97894.1 | ZOBELLIA_4435 | ZOBELLIA_3756 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. 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. | 0.541 |
| hdc | CAZ98569.1 | ZOBELLIA_4435 | ZOBELLIA_4434 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | Protein homologous to the C-terminal domain of the deaminase-reductase RidB. The exact function of this protein is unknown; Localized in the cytoplasm; Function unclear. | 0.486 |
| hdc | CAZ98571.1 | ZOBELLIA_4435 | ZOBELLIA_4436 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | The AsnC/Lrp-type transcriptional regulator family appears to be an important regulatory system of the amino acid metabolism and related processes; Contains a N-terminal DNA binding AsnC/Lrp-type HTH domain. The C-terminal part contains an effector-binding domain and/or an oligomerization domain; Localized in the cytoplasm; Family membership. | 0.528 |
| hdc | ddc | ZOBELLIA_4435 | ZOBELLIA_4235 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | L-2,4-diaminobutyrate decarboxylase catalyzes the reaction : L-2,4-diaminobutanoate = propane-1,3-diamine + CO2. It is involved in 1,3-diaminopropane biosynthesis. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.631 |
| hdc | hisD | ZOBELLIA_4435 | ZOBELLIA_4515 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | 0.900 |
| hdc | hutH | ZOBELLIA_4435 | ZOBELLIA_2081 | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | 0.904 |
| hisD | CAZ94937.1 | ZOBELLIA_4515 | ZOBELLIA_872 | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.900 |
| hisD | hdc | ZOBELLIA_4515 | ZOBELLIA_4435 | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. 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 |
| hisD | hutH | ZOBELLIA_4515 | ZOBELLIA_2081 | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | 0.930 |
| hutH | CAZ94937.1 | ZOBELLIA_2081 | ZOBELLIA_872 | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.900 |
| hutH | hdc | ZOBELLIA_2081 | ZOBELLIA_4435 | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | Histidine decarboxylase catalyzes the decarboxylation of L-histidine releasing histamine, a siderophore precursor. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.904 |
| hutH | hisD | ZOBELLIA_2081 | ZOBELLIA_4515 | Histidine ammonia-lyase converts L-histidine to urocanate and ammonia. This is the first step of the histidine degradation pathway. The active site is 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly; Localized in the cytoplasm; High confidence in function and specificity. | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | 0.930 |