| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aspC | azo3433 | azo0819 | azo3433 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | 0.663 |
| aspC | gltB | azo0819 | azo3642 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.937 |
| aspC | lpdA | azo0819 | azo1371 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Dihydrolipoamide dehydrogenase. Homology to lpdA of N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); biotin/Lipoyl attachment (IPR000089) [...] | 0.727 |
| aspC | maeB1 | azo0819 | azo0821 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) (NADP-ME). Homology to dme of S. meliloti of 60% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. Tigrfam: pta: phosphotransacetylase Pfam: Malic enzyme; Phosphate acetyl/butaryltransferase no signal peptide no TMHs; High confidence in function and specificity. | 0.786 |
| aspC | maeB2 | azo0819 | azo3211 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+). Homology to dme of S. meliloti of 61% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. InterPro: Phosphate acetyl/butaryl transferase (IPR002505); Malic enzyme (IPR001891) Pfam: Malic enzyme; Phosphate acetyl/butaryl transferase Tigrfam: pta: phosphotransacetylase no signal peptide no TMHs; High confidence in function and specificity. | 0.719 |
| aspC | metH | azo0819 | azo3726 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.691 |
| aspC | pabB | azo0819 | azo0198 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Para-aminobenzoate synthase component I (EC 4.1.3.-) (ADC synthase). CATALYZES THE BIOSYNTHESIS OF 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND GLUTAMINE. InterPro: Anthranilate synthase component I and chorismate binding enzyme pabB: para-aminobenzoate synthase component I; Specificity unclear. | 0.680 |
| aspC | pckG | azo0819 | azo0820 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Probable phosphoenolpyruvate carboxykinase; Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle; Belongs to the phosphoenolpyruvate carboxykinase [GTP] family. | 0.698 |
| aspC | pheA | azo0819 | azo1068 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity. | 0.938 |
| aspC | putA | azo0819 | azo3753 | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.690 |
| azo3433 | aspC | azo3433 | azo0819 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | 0.663 |
| azo3433 | gltB | azo3433 | azo3642 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.911 |
| azo3433 | lpdA | azo3433 | azo1371 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Dihydrolipoamide dehydrogenase. Homology to lpdA of N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); biotin/Lipoyl attachment (IPR000089) [...] | 0.926 |
| azo3433 | maeB1 | azo3433 | azo0821 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) (NADP-ME). Homology to dme of S. meliloti of 60% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. Tigrfam: pta: phosphotransacetylase Pfam: Malic enzyme; Phosphate acetyl/butaryltransferase no signal peptide no TMHs; High confidence in function and specificity. | 0.895 |
| azo3433 | maeB2 | azo3433 | azo3211 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+). Homology to dme of S. meliloti of 61% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. InterPro: Phosphate acetyl/butaryl transferase (IPR002505); Malic enzyme (IPR001891) Pfam: Malic enzyme; Phosphate acetyl/butaryl transferase Tigrfam: pta: phosphotransacetylase no signal peptide no TMHs; High confidence in function and specificity. | 0.895 |
| azo3433 | metH | azo3433 | azo3726 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.432 |
| azo3433 | pabB | azo3433 | azo0198 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Para-aminobenzoate synthase component I (EC 4.1.3.-) (ADC synthase). CATALYZES THE BIOSYNTHESIS OF 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND GLUTAMINE. InterPro: Anthranilate synthase component I and chorismate binding enzyme pabB: para-aminobenzoate synthase component I; Specificity unclear. | 0.630 |
| azo3433 | pckG | azo3433 | azo0820 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Probable phosphoenolpyruvate carboxykinase; Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle; Belongs to the phosphoenolpyruvate carboxykinase [GTP] family. | 0.575 |
| azo3433 | putA | azo3433 | azo3753 | Conserved hypothetical pyruvate ferredoxin/flavodoxin oxidoreductase. Homology to rsc3122 of R. solanacearum (trembl|Q8XUR3). CATALYZES THE FERREDOXIN-DEPENDENT OXIDATIVE DECARBOXYLATION OF ARYLPYRUVATES (BY SIMILARITY). InterPro: Pyruvate ferredoxin/flavodoxin oxidoreductase (IPR002869). Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase. no singal peptide. no TMHs; Conserved hypothetical protein. | Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.427 |
| gltB | aspC | azo3642 | azo0819 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 (55%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding site H [...] | 0.937 |