| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ascD | camA | azo3496 | azo2529 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | 0.460 |
| ascD | carBa1 | azo3496 | azo1122 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | 0.760 |
| ascD | carBa2 | azo3496 | azo1984 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Putative dioxygenase, hydroxylase small component; Hydroxylase large component of 1,2-dioxygenase protein complex, involved in aromatic compounds degradation. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyX: Benzoate 12-dioxygenase alpha subunit (EC 1.14.12.10). DEGRADATION OF BENZOATE TO 2-HYDRO-12-DIHYDROXYBENZOATE (DHB). Benzoate 12-dioxygenase beta subunit (EC 1.14.12.10). DEGRADATION OF BENZOATE TO 2-HYDRO-12-DIHYDROXYBENZOATE (DHB). THE BETA SUBUNIT MAY BE RESPONSIBLE FOR THE SUBST [...] | 0.722 |
| ascD | nagAa | azo3496 | azo2517 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity. | 0.673 |
| ascD | nagAb | azo3496 | azo2514 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Putative ferredoxin; Naphthalene 12-dioxygenase system ferredoxin component. COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. THIS SUBUNIT IS A 2FE-2S FERREDOXIN THAT TRANSFERS ELECTRONS TO IRON SULFUR PROTEIN COMPONENTS (ISP); High confidence in function and specificity. | 0.564 |
| ascD | nagG | azo3496 | azo2516 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Putative ring hydroxylating large subunit; nagG,RSc1090:putative salicylate-5-hydroxylase large oxygenase component oxidoreductase protein [EC:1.-.-.-]. Rieske-type iron-sulfur center homologous to the large subunits of dihydroxylating dioxygenases. Involved in conversion of Naphthalene to gentisate. Aromatic compounds degradation. Biphenyl dioxygenase alpha subunit (EC 1.14.12.18) (Biphenyl 23- dioxygenase); High confidence in function and specificity. | 0.627 |
| ascD | nagH | azo3496 | azo2515 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Putative ring hydroxylating beta subunit; NagH: probable salicylate-5-hydroxylase small oxygenase component oxidoreductase protein. Involved in conversion of Naphthalene to gentisate. Aromatic compounds degradation; Family membership. | 0.722 |
| ascD | vanB1 | azo3496 | azo1124 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 40% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. InterPro: NADH:cytochrome b5 reductase (CBR)(IPR001834); Ferredoxin (IPR001041); Oxidoreductase FAD and NAD(P) binding domain (IPR001433) Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding dom [...] | 0.799 |
| ascD | vanB2 | azo3496 | azo1982 | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 42% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding domain; 2Fe-2S iron-sulfur cluster binding domain no signal peptide no TMHs; Family membership. | 0.759 |
| camA | ascD | azo2529 | azo3496 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | 0.460 |
| camA | nagAa | azo2529 | azo2517 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity. | 0.460 |
| camA | nagAb | azo2529 | azo2514 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Putative ferredoxin; Naphthalene 12-dioxygenase system ferredoxin component. COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. THIS SUBUNIT IS A 2FE-2S FERREDOXIN THAT TRANSFERS ELECTRONS TO IRON SULFUR PROTEIN COMPONENTS (ISP); High confidence in function and specificity. | 0.932 |
| camA | nagG | azo2529 | azo2516 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Putative ring hydroxylating large subunit; nagG,RSc1090:putative salicylate-5-hydroxylase large oxygenase component oxidoreductase protein [EC:1.-.-.-]. Rieske-type iron-sulfur center homologous to the large subunits of dihydroxylating dioxygenases. Involved in conversion of Naphthalene to gentisate. Aromatic compounds degradation. Biphenyl dioxygenase alpha subunit (EC 1.14.12.18) (Biphenyl 23- dioxygenase); High confidence in function and specificity. | 0.630 |
| camA | vanB1 | azo2529 | azo1124 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 40% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. InterPro: NADH:cytochrome b5 reductase (CBR)(IPR001834); Ferredoxin (IPR001041); Oxidoreductase FAD and NAD(P) binding domain (IPR001433) Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding dom [...] | 0.559 |
| camA | vanB2 | azo2529 | azo1982 | Probable putidaredoxin reductase (EC 1.18.1.-). Homology to camA of P. putida of 48% (sprot|CAMA_PSEPU). The oxidation of camphor by cytochrome p450-cam requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from nadh to p450 for oxygen activation. Interpro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IRP001327), NAD binding site (IPR000205) Pfam: Pyridine nucleotide-disulphide oxidoreductase no signal peptide no TMHs; Family membership. | Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 42% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding domain; 2Fe-2S iron-sulfur cluster binding domain no signal peptide no TMHs; Family membership. | 0.559 |
| carBa1 | ascD | azo1122 | azo3496 | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...] | 0.760 |
| carBa1 | carBa2 | azo1122 | azo1984 | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | Putative dioxygenase, hydroxylase small component; Hydroxylase large component of 1,2-dioxygenase protein complex, involved in aromatic compounds degradation. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyX: Benzoate 12-dioxygenase alpha subunit (EC 1.14.12.10). DEGRADATION OF BENZOATE TO 2-HYDRO-12-DIHYDROXYBENZOATE (DHB). Benzoate 12-dioxygenase beta subunit (EC 1.14.12.10). DEGRADATION OF BENZOATE TO 2-HYDRO-12-DIHYDROXYBENZOATE (DHB). THE BETA SUBUNIT MAY BE RESPONSIBLE FOR THE SUBST [...] | 0.420 |
| carBa1 | nagAa | azo1122 | azo2517 | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity. | 0.874 |
| carBa1 | nagAb | azo1122 | azo2514 | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | Putative ferredoxin; Naphthalene 12-dioxygenase system ferredoxin component. COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. THIS SUBUNIT IS A 2FE-2S FERREDOXIN THAT TRANSFERS ELECTRONS TO IRON SULFUR PROTEIN COMPONENTS (ISP); High confidence in function and specificity. | 0.401 |
| carBa1 | nagG | azo1122 | azo2516 | Putative dioxygenase, hydroxylase small component; Ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols. The beta subunit is may be responsible for the substrate specificity of the enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBa. Involved in the aerobic degradation of carbazole by P.resinovorans sp. strain CA10. XlyY: Benzene 12-dioxygenase beta subunit (EC 1.14.12.3), involved in benzoate degradation.Degradation of benzoate to 2-hydro-12-dihydroxybenzoate (dhb).; Conserved hypotheti [...] | Putative ring hydroxylating large subunit; nagG,RSc1090:putative salicylate-5-hydroxylase large oxygenase component oxidoreductase protein [EC:1.-.-.-]. Rieske-type iron-sulfur center homologous to the large subunits of dihydroxylating dioxygenases. Involved in conversion of Naphthalene to gentisate. Aromatic compounds degradation. Biphenyl dioxygenase alpha subunit (EC 1.14.12.18) (Biphenyl 23- dioxygenase); High confidence in function and specificity. | 0.940 |