node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rv1770 | bfrB | Rv1770 | Rv3841 | Conserved protein; Rv1770, (MTCY28.36), len: 428 aa. Conserved protein,highly similar in N-terminus to Q49882 Hypothetical protein from Mycobacterium leprae from cosmid L247 (83 aa), FASTA scores: opt: 301, E(): 1e-12, (56.5% identity in 85 aa overlap). | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | 0.593 |
Rv3839 | Rv3840 | Rv3839 | Rv3840 | Rv3839, (MTCY01A6.30c), len: 258 aa. Conserved hypothetical protein, similar in part to Q9RD78|SCF43.10cfrom hypothetical 25.8 KDA protein Streptomyces coelicolor (241 aa), FASTA scores: opt: 270,E(): 3.2e-10, (33.45% identity in 272 aa overlap); and O00320|F25451_2 hypothetical protein from Homo sapiens (Human) (339 aa), FASTA scores: opt: 126, E(): 0.77,(28.75% identity in 240 aa overlap). | Rv3840, (MTCY01A6.29c), len: 137 aa. Possible transcriptional regulator, highly similar in part to PSR proteins (penicillin binding protein repressors) e.g. Q47828|PSR PSR protein from Enterococcus hirae (293 aa) FASTA scores: opt: 221, E(): 2.2e-07, (41.65% identity in 108 aa overlap); O86213|PSRFM PSRFM protein (fragment) from Enterococcus hirae (171 aa), FASTA scores: opt: 202, E(): 2.4e-06, (40.75% identity in 108 aa overlap); Q47865|PSR penicillin binding protein repressor from Enterococcus hirae (148 aa), FASTA scores: opt: 201, E(): 2.5e-06,(51.65% identity in 60 aa overlap); et [...] | 0.755 |
Rv3839 | bfrB | Rv3839 | Rv3841 | Rv3839, (MTCY01A6.30c), len: 258 aa. Conserved hypothetical protein, similar in part to Q9RD78|SCF43.10cfrom hypothetical 25.8 KDA protein Streptomyces coelicolor (241 aa), FASTA scores: opt: 270,E(): 3.2e-10, (33.45% identity in 272 aa overlap); and O00320|F25451_2 hypothetical protein from Homo sapiens (Human) (339 aa), FASTA scores: opt: 126, E(): 0.77,(28.75% identity in 240 aa overlap). | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | 0.631 |
Rv3840 | Rv3839 | Rv3840 | Rv3839 | Rv3840, (MTCY01A6.29c), len: 137 aa. Possible transcriptional regulator, highly similar in part to PSR proteins (penicillin binding protein repressors) e.g. Q47828|PSR PSR protein from Enterococcus hirae (293 aa) FASTA scores: opt: 221, E(): 2.2e-07, (41.65% identity in 108 aa overlap); O86213|PSRFM PSRFM protein (fragment) from Enterococcus hirae (171 aa), FASTA scores: opt: 202, E(): 2.4e-06, (40.75% identity in 108 aa overlap); Q47865|PSR penicillin binding protein repressor from Enterococcus hirae (148 aa), FASTA scores: opt: 201, E(): 2.5e-06,(51.65% identity in 60 aa overlap); et [...] | Rv3839, (MTCY01A6.30c), len: 258 aa. Conserved hypothetical protein, similar in part to Q9RD78|SCF43.10cfrom hypothetical 25.8 KDA protein Streptomyces coelicolor (241 aa), FASTA scores: opt: 270,E(): 3.2e-10, (33.45% identity in 272 aa overlap); and O00320|F25451_2 hypothetical protein from Homo sapiens (Human) (339 aa), FASTA scores: opt: 126, E(): 0.77,(28.75% identity in 240 aa overlap). | 0.755 |
Rv3840 | bfrB | Rv3840 | Rv3841 | Rv3840, (MTCY01A6.29c), len: 137 aa. Possible transcriptional regulator, highly similar in part to PSR proteins (penicillin binding protein repressors) e.g. Q47828|PSR PSR protein from Enterococcus hirae (293 aa) FASTA scores: opt: 221, E(): 2.2e-07, (41.65% identity in 108 aa overlap); O86213|PSRFM PSRFM protein (fragment) from Enterococcus hirae (171 aa), FASTA scores: opt: 202, E(): 2.4e-06, (40.75% identity in 108 aa overlap); Q47865|PSR penicillin binding protein repressor from Enterococcus hirae (148 aa), FASTA scores: opt: 201, E(): 2.5e-06,(51.65% identity in 60 aa overlap); et [...] | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | 0.534 |
ahpC | bfrB | Rv2428 | Rv3841 | Alkyl hydroperoxide reductase C protein AhpC (alkyl hydroperoxidase C); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. D [...] | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | 0.664 |
ahpC | gap | Rv2428 | Rv1436 | Alkyl hydroperoxide reductase C protein AhpC (alkyl hydroperoxidase C); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. D [...] | Probable glyceraldehyde 3-phosphate dehydrogenase Gap (GAPDH); Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG; Belongs to the glyceraldehyde-3-ph [...] | 0.520 |
bfrA | bfrB | Rv1876 | Rv3841 | Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | 0.995 |
bfrA | hemZ | Rv1876 | Rv1485 | Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. | Ferrochelatase HemZ (protoheme ferro-lyase) (heme synthetase); Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. | 0.936 |
bfrA | ideR | Rv1876 | Rv2711 | Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. | Iron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators. | 0.861 |
bfrA | mmcO | Rv1876 | Rv0846c | Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. | Probable oxidase; Required for copper resistance. In vitro, oxidizes organic substrates and Fe(2+). May act in vivo by oxidation of toxic periplasmic Cu(+); Belongs to the multicopper oxidase family. | 0.919 |
bfrB | Rv1770 | Rv3841 | Rv1770 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Conserved protein; Rv1770, (MTCY28.36), len: 428 aa. Conserved protein,highly similar in N-terminus to Q49882 Hypothetical protein from Mycobacterium leprae from cosmid L247 (83 aa), FASTA scores: opt: 301, E(): 1e-12, (56.5% identity in 85 aa overlap). | 0.593 |
bfrB | Rv3839 | Rv3841 | Rv3839 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Rv3839, (MTCY01A6.30c), len: 258 aa. Conserved hypothetical protein, similar in part to Q9RD78|SCF43.10cfrom hypothetical 25.8 KDA protein Streptomyces coelicolor (241 aa), FASTA scores: opt: 270,E(): 3.2e-10, (33.45% identity in 272 aa overlap); and O00320|F25451_2 hypothetical protein from Homo sapiens (Human) (339 aa), FASTA scores: opt: 126, E(): 0.77,(28.75% identity in 240 aa overlap). | 0.631 |
bfrB | Rv3840 | Rv3841 | Rv3840 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Rv3840, (MTCY01A6.29c), len: 137 aa. Possible transcriptional regulator, highly similar in part to PSR proteins (penicillin binding protein repressors) e.g. Q47828|PSR PSR protein from Enterococcus hirae (293 aa) FASTA scores: opt: 221, E(): 2.2e-07, (41.65% identity in 108 aa overlap); O86213|PSRFM PSRFM protein (fragment) from Enterococcus hirae (171 aa), FASTA scores: opt: 202, E(): 2.4e-06, (40.75% identity in 108 aa overlap); Q47865|PSR penicillin binding protein repressor from Enterococcus hirae (148 aa), FASTA scores: opt: 201, E(): 2.5e-06,(51.65% identity in 60 aa overlap); et [...] | 0.534 |
bfrB | ahpC | Rv3841 | Rv2428 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Alkyl hydroperoxide reductase C protein AhpC (alkyl hydroperoxidase C); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. D [...] | 0.664 |
bfrB | bfrA | Rv3841 | Rv1876 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. | 0.995 |
bfrB | gap | Rv3841 | Rv1436 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Probable glyceraldehyde 3-phosphate dehydrogenase Gap (GAPDH); Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG; Belongs to the glyceraldehyde-3-ph [...] | 0.575 |
bfrB | hemZ | Rv3841 | Rv1485 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Ferrochelatase HemZ (protoheme ferro-lyase) (heme synthetase); Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. | 0.913 |
bfrB | ideR | Rv3841 | Rv2711 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Iron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators. | 0.775 |
bfrB | lpqL | Rv3841 | Rv0418 | Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. | Probable lipoprotein aminopeptidase LpqL; An aminopeptidase; acts on free N-terminal amino groups with a very strong preference for Leu in the first position. Belongs to the peptidase M28 family. M28A subfamily. | 0.593 |