| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ98744.1 | katA2 | ZOBELLIA_4609 | ZOBELLIA_3559 | Peroxiredoxins are thiol peroxidase involved in redox regulation of the cell. Can reduce H(2)O(2), short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. It oxidized the peroxide substrate to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin; Localized in the cytoplasm; Specificity unclear. | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | 0.760 |
| CAZ98744.1 | trxB1 | ZOBELLIA_4609 | ZOBELLIA_151 | Peroxiredoxins are thiol peroxidase involved in redox regulation of the cell. Can reduce H(2)O(2), short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. It oxidized the peroxide substrate to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin; Localized in the cytoplasm; Specificity unclear. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.446 |
| cysS | trxB1 | ZOBELLIA_2759 | ZOBELLIA_151 | Cysteinyl-tRNA synthetase catalyzes the attachment of cysteine to its cognate transfer RNA molecule in a highly specific two-step reaction. It is a monomer and belongs to the class I of the aminoacyl-tRNA synthetases. It binds one zinc ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.448 |
| katA2 | CAZ98744.1 | ZOBELLIA_3559 | ZOBELLIA_4609 | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | Peroxiredoxins are thiol peroxidase involved in redox regulation of the cell. Can reduce H(2)O(2), short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. It oxidized the peroxide substrate to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin; Localized in the cytoplasm; Specificity unclear. | 0.760 |
| katA2 | trxB1 | ZOBELLIA_3559 | ZOBELLIA_151 | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.445 |
| metB | trxB1 | ZOBELLIA_1454 | ZOBELLIA_151 | The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.905 |
| moeB | sufS | ZOBELLIA_3684 | ZOBELLIA_1842 | Molybdopterin synthase activating protein; Enzyme involved in the biosynthesis of molybdopterin cofactor, necessary for molybdoenzymes. Plays a role in the activation of the small subunit of the molybdopterin converting factor (moaD); Contains a N- terminal transmembrane segment and a C-terminal rhodanese domain; Belongs to the hesA/moeB/thiF family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | 0.620 |
| moeB | trxB1 | ZOBELLIA_3684 | ZOBELLIA_151 | Molybdopterin synthase activating protein; Enzyme involved in the biosynthesis of molybdopterin cofactor, necessary for molybdoenzymes. Plays a role in the activation of the small subunit of the molybdopterin converting factor (moaD); Contains a N- terminal transmembrane segment and a C-terminal rhodanese domain; Belongs to the hesA/moeB/thiF family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.547 |
| rplE | rplF | ZOBELLIA_2522 | ZOBELLIA_2525 | Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | 0.999 |
| rplE | trxB1 | ZOBELLIA_2522 | ZOBELLIA_151 | Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.542 |
| rplF | rplE | ZOBELLIA_2525 | ZOBELLIA_2522 | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | 0.999 |
| rplF | trxB1 | ZOBELLIA_2525 | ZOBELLIA_151 | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.454 |
| sufS | moeB | ZOBELLIA_1842 | ZOBELLIA_3684 | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | Molybdopterin synthase activating protein; Enzyme involved in the biosynthesis of molybdopterin cofactor, necessary for molybdoenzymes. Plays a role in the activation of the small subunit of the molybdopterin converting factor (moaD); Contains a N- terminal transmembrane segment and a C-terminal rhodanese domain; Belongs to the hesA/moeB/thiF family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.620 |
| sufS | trxB1 | ZOBELLIA_1842 | ZOBELLIA_151 | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.905 |
| trxA | trxB1 | ZOBELLIA_2179 | ZOBELLIA_151 | Thioredoxin is a small disulfide-containing redox protein that participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Localized in the cytoplasm; High confidence in function and specificity. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.958 |
| trxA-3 | trxB1 | ZOBELLIA_3485 | ZOBELLIA_151 | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | 0.516 |
| trxB1 | CAZ98744.1 | ZOBELLIA_151 | ZOBELLIA_4609 | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | Peroxiredoxins are thiol peroxidase involved in redox regulation of the cell. Can reduce H(2)O(2), short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. It oxidized the peroxide substrate to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin; Localized in the cytoplasm; Specificity unclear. | 0.446 |
| trxB1 | cysS | ZOBELLIA_151 | ZOBELLIA_2759 | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | Cysteinyl-tRNA synthetase catalyzes the attachment of cysteine to its cognate transfer RNA molecule in a highly specific two-step reaction. It is a monomer and belongs to the class I of the aminoacyl-tRNA synthetases. It binds one zinc ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | 0.448 |
| trxB1 | katA2 | ZOBELLIA_151 | ZOBELLIA_3559 | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | 0.445 |
| trxB1 | metB | ZOBELLIA_151 | ZOBELLIA_1454 | Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity. | The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.905 |
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