| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rv1106c | choD | Rv1106c | Rv3409c | 3-beta-hydroxysteroid dehydrogenase; 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively. | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | 0.987 |
| Rv1106c | cyp125 | Rv1106c | Rv3545c | 3-beta-hydroxysteroid dehydrogenase; 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively. | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | 0.960 |
| Rv1106c | cyp142 | Rv1106c | Rv3518c | 3-beta-hydroxysteroid dehydrogenase; 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively. | Probable cytochrome P450 monooxygenase 142 Cyp142; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4- en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. In vitro, Cyp142 catalyzes with equal preference the oxidation of both (25R)- and (25S)-26- hydroxycholest-4-en-3-one diastereomers to the corresponding carboxy [...] | 0.968 |
| Rv3541c | cyp125 | Rv3541c | Rv3545c | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | 0.968 |
| Rv3541c | fadA5 | Rv3541c | Rv3546 | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Probable acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase); Involved in the beta-oxidation of the cholesterol side chain. It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection. Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl- CoA (3-OPC-CoA) and acetyl-CoA. Also able to use acetoacetyl-CoA (AcAcCoA) as substrate. | 0.920 |
| Rv3541c | fadE28 | Rv3541c | Rv3544c | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Probable acyl-CoA dehydrogenase FadE28; Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. May play an important role for the initial macrophage invasion, possibly in response to the acidification of phagosome. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4- pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene- 20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol- [...] | 0.997 |
| Rv3541c | fadE29 | Rv3541c | Rv3543c | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Probable acyl-CoA dehydrogenase FadE29; Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. Contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4- pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene- 20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2'-propanoyl- CoA)-3a-alpha-H- 7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), [...] | 0.999 |
| Rv3541c | kshB | Rv3541c | Rv3571 | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Reductase component of 3-ketosteroid-9-alpha-hydroxylase KshB; Involved in the degradation of cholesterol. Catalyzes the introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) intermediate which spontaneously form 3-hydroxy-9,10-seconandrost- 1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with concomitant aromatization of ring A. KSH is also able to use 4- androstene-3,17-dione (AD), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4- BNC), 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4 [...] | 0.426 |
| Rv3541c | ltp2 | Rv3541c | Rv3540c | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | Rv3540c, (MTCY03C7.16), len: 386 aa. Probable ltp2,lipid-transfer protein or keto acyl-CoA thiolase, similar to several e.g. Q9X4X2|DITF DITF protein (hypothetical protein, similar to non-specific lipid-transfer protein and 3-ketoacyl-CoA thiolase) from Pseudomonas abietaniphila (397 aa), FASTA scores: opt: 665, E(): 5.3e-34, (33.4% identity in 392 aa overlap); O30255|AF2416 3-ketoacyl-CoA thiolase (ACAB-12) from Archaeoglobus fulgidus (384 aa),FASTA scores: opt: 496, E(): 1.6e-23, (30.35% identity in 389 aa overlap); O28978|AF1291 3-ketoacyl-CoA thiolase (ACAB-11) from Archaeoglobus f [...] | 0.999 |
| choD | Rv1106c | Rv3409c | Rv1106c | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | 3-beta-hydroxysteroid dehydrogenase; 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively. | 0.987 |
| choD | cyp125 | Rv3409c | Rv3545c | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | 0.933 |
| choD | cyp142 | Rv3409c | Rv3518c | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | Probable cytochrome P450 monooxygenase 142 Cyp142; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4- en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. In vitro, Cyp142 catalyzes with equal preference the oxidation of both (25R)- and (25S)-26- hydroxycholest-4-en-3-one diastereomers to the corresponding carboxy [...] | 0.944 |
| choD | fadA5 | Rv3409c | Rv3546 | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | Probable acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase); Involved in the beta-oxidation of the cholesterol side chain. It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection. Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl- CoA (3-OPC-CoA) and acetyl-CoA. Also able to use acetoacetyl-CoA (AcAcCoA) as substrate. | 0.532 |
| cyp125 | Rv1106c | Rv3545c | Rv1106c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | 3-beta-hydroxysteroid dehydrogenase; 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively. | 0.960 |
| cyp125 | Rv3541c | Rv3545c | Rv3541c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Conserved protein; Rv3541c, (MTCY03C7.15), len: 129 aa. Conserved protein, showing some similarity to Q9CBJ7|ML1909 hypothetical protein from Mycobacterium leprae (142 aa) FASTA scores: opt: 110, E(): 1.2, (27.95% identity in 118 aa overlap); and other (see also blastp results) e.g. Q9L0M3|SCD82.08 hypothetical 15.2 KDA protein from Streptomyces coelicolor (142 aa), FASTA scores: opt: 127,E(): 0.086, (27.65% identity in 123 aa overlap). Contains PS00075 Dihydrofolate reductase signature. | 0.968 |
| cyp125 | choD | Rv3545c | Rv3409c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Cholesterol oxidase ChoD (cholesterol-O2 oxidoreductase); Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Belongs to the GMC oxidoreductase family. Highly divergent. | 0.933 |
| cyp125 | cyp142 | Rv3545c | Rv3518c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Probable cytochrome P450 monooxygenase 142 Cyp142; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4- en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. In vitro, Cyp142 catalyzes with equal preference the oxidation of both (25R)- and (25S)-26- hydroxycholest-4-en-3-one diastereomers to the corresponding carboxy [...] | 0.943 |
| cyp125 | fadA5 | Rv3545c | Rv3546 | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Probable acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase); Involved in the beta-oxidation of the cholesterol side chain. It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection. Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl- CoA (3-OPC-CoA) and acetyl-CoA. Also able to use acetoacetyl-CoA (AcAcCoA) as substrate. | 0.932 |
| cyp125 | fadE28 | Rv3545c | Rv3544c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Probable acyl-CoA dehydrogenase FadE28; Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. May play an important role for the initial macrophage invasion, possibly in response to the acidification of phagosome. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4- pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene- 20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol- [...] | 0.987 |
| cyp125 | fadE29 | Rv3545c | Rv3543c | Probable cytochrome P450 125 Cyp125; Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one. Belongs to the cytochrome P450 family. | Probable acyl-CoA dehydrogenase FadE29; Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. Contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4- pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene- 20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2'-propanoyl- CoA)-3a-alpha-H- 7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), [...] | 0.983 |