node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rv0948c | Rv1885c | Rv0948c | Rv1885c | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | 0.979 |
Rv0948c | aroF | Rv0948c | Rv2540c | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.975 |
Rv0948c | pheA | Rv0948c | Rv3838c | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | Rv3838c, (MTCY01A6.31), len: 321 aa. PheA,prephenate dehydratase (see citation below), equivalent to Q9CDC4|PHEA|ML0078 putative prephenate dehydratase from Mycobacterium leprae (322 aa), FASTA scores: opt: 1690,E(): 1.3e-93, (84.25% identity in 311 aa overlap). Also highly similar to others e.g. P10341|PHEA_CORGL from Corynebacterium glutamicum (Brevibacterium flavum) (315 aa), FASTA scores: opt: 843, E(): 4e-43, (45.8% identity in 308 aa overlap); Q9ZBX0|SCD78.29c from Streptomyces coelicolor (310 aa), FASTA scores: opt: 820, E(): 9.2e-42,(46.45% identity in 312 aa overlap); Q44104|P [...] | 0.940 |
Rv0948c | tyrA | Rv0948c | Rv3754 | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain. | 0.962 |
Rv1885c | Rv0948c | Rv1885c | Rv0948c | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | 0.979 |
Rv1885c | aroF | Rv1885c | Rv2540c | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.974 |
Rv1885c | pheA | Rv1885c | Rv3838c | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | Rv3838c, (MTCY01A6.31), len: 321 aa. PheA,prephenate dehydratase (see citation below), equivalent to Q9CDC4|PHEA|ML0078 putative prephenate dehydratase from Mycobacterium leprae (322 aa), FASTA scores: opt: 1690,E(): 1.3e-93, (84.25% identity in 311 aa overlap). Also highly similar to others e.g. P10341|PHEA_CORGL from Corynebacterium glutamicum (Brevibacterium flavum) (315 aa), FASTA scores: opt: 843, E(): 4e-43, (45.8% identity in 308 aa overlap); Q9ZBX0|SCD78.29c from Streptomyces coelicolor (310 aa), FASTA scores: opt: 820, E(): 9.2e-42,(46.45% identity in 312 aa overlap); Q44104|P [...] | 0.937 |
Rv1885c | tyrA | Rv1885c | Rv3754 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain. | 0.954 |
Rv3242c | tyrA | Rv3242c | Rv3754 | Conserved hypothetical protein; Rv3242c, (MTCY20B11.17c), len: 213 aa. Conserved hypothetical protein, highly similar in N-terminus to Q9CCI9|ML0776 hypothetical protein from Mycobacterium leprae (85 aa), FASTA scores: opt: 324, E(): 1.7e-13,(78.1% identity in 64 aa overlap). Also similar to Q9RUJ7|DR1389 putative competence protein COMF from Deinococcus radiodurans (219 aa), FASTA scores: opt: 223,E(): 6.3e-07, (35.8% identity in 215 aa overlap); BAB50338|MLL3453 hypothetical protein from Rhizobium loti (Mesorhizobium loti) (240 aa), FASTA scores: opt: 218, E(): 1.4e-06, (28.5% identi [...] | Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain. | 0.833 |
aroB | aroF | Rv2538c | Rv2540c | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.999 |
aroB | cobC | Rv2538c | Rv2231c | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Rv2231c, (MTCY427.12c), len: 364 aa. Possible cobC,aminotransferase. Note that initiation codon uncertain. Similar to CobC aminotransferases e.g. sp|P21633|COBC_PSEDE COBC protein (333 aa) opt: 277, E(): 1.7e-11; 28.8% identity in 313 aa overlap and also to e.g. SW:HIS8_ECOLI P06986 histidinol-phosphate aminotransferase (27.0% identity in 289 aa overlap), contains PS00105 aminotransferases class-I pyridoxal-phosphate attachment site. Real Mycobacterium tuberculosis histidinol-phosphate aminotransferase, hisC, is Rv1600 (MTCY336.04c); Belongs to the class-I pyridoxal-phosphate-dependent [...] | 0.498 |
aroB | hisC1 | Rv2538c | Rv1600 | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Rv1600, (MTCY336.04c), len: 380 aa. Probable hisC1,histidinol-phosphate aminotransferase O06591. Similar to many e.g. HIS8_STRCO|P16246 from Streptomyces coelicolor (369 aa), FASTA results: opt: 1353, E(): 0, (59.0% identity in 356 aa overlap). Some similarity to other Mycobacterium tuberculosis aminotransferases e.g. Rv3772|MTCY13D12.06,FASTA results: E(): 7.4e-25, (33.7% identity in 365 aa overlap). Contains aminotransferases class-II pyridoxal-phosphate attachment site (PS00599). Belongs to class-II of pyridoxal-phosphate-dependent aminotransferases. Note that previously known as hisC. | 0.771 |
aroB | hisC2 | Rv2538c | Rv3772 | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Putative phenylalanine aminotransferase; May catalyze the transamination reaction in phenylalanine biosynthesis; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. | 0.558 |
aroB | pheA | Rv2538c | Rv3838c | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Rv3838c, (MTCY01A6.31), len: 321 aa. PheA,prephenate dehydratase (see citation below), equivalent to Q9CDC4|PHEA|ML0078 putative prephenate dehydratase from Mycobacterium leprae (322 aa), FASTA scores: opt: 1690,E(): 1.3e-93, (84.25% identity in 311 aa overlap). Also highly similar to others e.g. P10341|PHEA_CORGL from Corynebacterium glutamicum (Brevibacterium flavum) (315 aa), FASTA scores: opt: 843, E(): 4e-43, (45.8% identity in 308 aa overlap); Q9ZBX0|SCD78.29c from Streptomyces coelicolor (310 aa), FASTA scores: opt: 820, E(): 9.2e-42,(46.45% identity in 312 aa overlap); Q44104|P [...] | 0.722 |
aroB | tyrA | Rv2538c | Rv3754 | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain. | 0.884 |
aroF | Rv0948c | Rv2540c | Rv0948c | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | 0.975 |
aroF | Rv1885c | Rv2540c | Rv1885c | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity. | 0.974 |
aroF | aroB | Rv2540c | Rv2538c | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 3-dehydroquinate synthase AroB; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.999 |
aroF | cobC | Rv2540c | Rv2231c | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Rv2231c, (MTCY427.12c), len: 364 aa. Possible cobC,aminotransferase. Note that initiation codon uncertain. Similar to CobC aminotransferases e.g. sp|P21633|COBC_PSEDE COBC protein (333 aa) opt: 277, E(): 1.7e-11; 28.8% identity in 313 aa overlap and also to e.g. SW:HIS8_ECOLI P06986 histidinol-phosphate aminotransferase (27.0% identity in 289 aa overlap), contains PS00105 aminotransferases class-I pyridoxal-phosphate attachment site. Real Mycobacterium tuberculosis histidinol-phosphate aminotransferase, hisC, is Rv1600 (MTCY336.04c); Belongs to the class-I pyridoxal-phosphate-dependent [...] | 0.679 |
aroF | hisC1 | Rv2540c | Rv1600 | Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Rv1600, (MTCY336.04c), len: 380 aa. Probable hisC1,histidinol-phosphate aminotransferase O06591. Similar to many e.g. HIS8_STRCO|P16246 from Streptomyces coelicolor (369 aa), FASTA results: opt: 1353, E(): 0, (59.0% identity in 356 aa overlap). Some similarity to other Mycobacterium tuberculosis aminotransferases e.g. Rv3772|MTCY13D12.06,FASTA results: E(): 7.4e-25, (33.7% identity in 365 aa overlap). Contains aminotransferases class-II pyridoxal-phosphate attachment site (PS00599). Belongs to class-II of pyridoxal-phosphate-dependent aminotransferases. Note that previously known as hisC. | 0.787 |