| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo1819 | azo2616 | azo1819 | azo2616 | Hypothetical protein. Homology to dr0392 of D. radiodurans of 25% (trembl|Q9RXC3) Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. no signal peptide no TMHs; High confidence in function and specificity. | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.577 |
| azo2561 | azo2616 | azo2561 | azo2616 | Conserved hypothetical protein. Homology to dr0392 of D. radiodurans of 33% (trembl|Q9RXC3). Pfam: Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural [...] | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.545 |
| azo2613 | azo2616 | azo2613 | azo2616 | Hypothetical protein, 50% identity (59% simialrity)to TrEMBL;Q92TJ5. Has PF04828, Protein of unknown function (DUF636);IPR006913, GFA;This family of proteins has no known function, but several strongly conserved cysteine residues. Glutathione-dependent formaldehyde-activating enzymes catalyze the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. All known members of this family contain 5 strongly conserved cysteine residues. NO Signal peptide or TMH present; Function unclear. | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.600 |
| azo2616 | azo1819 | azo2616 | azo1819 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Hypothetical protein. Homology to dr0392 of D. radiodurans of 25% (trembl|Q9RXC3) Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. no signal peptide no TMHs; High confidence in function and specificity. | 0.577 |
| azo2616 | azo2561 | azo2616 | azo2561 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Conserved hypothetical protein. Homology to dr0392 of D. radiodurans of 33% (trembl|Q9RXC3). Pfam: Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural [...] | 0.545 |
| azo2616 | azo2613 | azo2616 | azo2613 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Hypothetical protein, 50% identity (59% simialrity)to TrEMBL;Q92TJ5. Has PF04828, Protein of unknown function (DUF636);IPR006913, GFA;This family of proteins has no known function, but several strongly conserved cysteine residues. Glutathione-dependent formaldehyde-activating enzymes catalyze the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. All known members of this family contain 5 strongly conserved cysteine residues. NO Signal peptide or TMH present; Function unclear. | 0.600 |
| azo2616 | azo2617 | azo2616 | azo2617 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | TREMBL:Q89L44: 48% identity.64% similarity. probable haloacid dehalogenase-like hydrolase. InterPro:IPR005834; Hydrolase. Pfam:PF00702; Hydrolase; Phosphoglycolate phosphatase(PGP). TIGR00099: conserved hypothetical prot; Function unclear. | 0.747 |
| azo2616 | azo2619 | azo2616 | azo2619 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Putative methyltransferase; Similar to TREMBL:Q98BY2 (39% identity); TREMBL:Q9A2R1 (40% identity); TREMBL:Q89KG6 (34% identity). Pfam (PF01209): ubiE/COQ5 methyltransferase family; Function unclear. | 0.647 |
| azo2616 | gloB1 | azo2616 | azo1208 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.571 |
| azo2616 | gloB2 | azo2616 | azo2057 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.571 |
| azo2616 | icmF | azo2616 | azo0696 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Probable methylmalonyl-coa mutase protein; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. | 0.743 |
| azo2616 | mutB | azo2616 | azo0685 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Probable Methylmalonyl-CoA mutase large subunit; FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates (By similarity). ACtivity:- (R)-2-Methylmalonyl-CoA = succinyl-CoA Entry name :- MUTB_PORGI Primary accession number :-Q59677 Identities = 467/679 (68%) InterPro :-IPR006159; Acid_CoA_mut_C. IPR006158; B12-binding. IPR006099; MMCoA_mutase. IPR006098; MMCoA_mutase_N. IPR006100; MMCoA_mutase_sub. Pfam PF02310; B12-binding; 1. PF01642; MM_CoA_mutase; 1. Prediction: Non-secretory protein Signal [...] | 0.641 |
| azo2616 | soxR | azo2616 | azo2618 | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | Probable redox-sensitive transcriptional activator,; High confidence in function and specificity. | 0.746 |
| azo2617 | azo2616 | azo2617 | azo2616 | TREMBL:Q89L44: 48% identity.64% similarity. probable haloacid dehalogenase-like hydrolase. InterPro:IPR005834; Hydrolase. Pfam:PF00702; Hydrolase; Phosphoglycolate phosphatase(PGP). TIGR00099: conserved hypothetical prot; Function unclear. | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.747 |
| azo2617 | azo2619 | azo2617 | azo2619 | TREMBL:Q89L44: 48% identity.64% similarity. probable haloacid dehalogenase-like hydrolase. InterPro:IPR005834; Hydrolase. Pfam:PF00702; Hydrolase; Phosphoglycolate phosphatase(PGP). TIGR00099: conserved hypothetical prot; Function unclear. | Putative methyltransferase; Similar to TREMBL:Q98BY2 (39% identity); TREMBL:Q9A2R1 (40% identity); TREMBL:Q89KG6 (34% identity). Pfam (PF01209): ubiE/COQ5 methyltransferase family; Function unclear. | 0.584 |
| azo2617 | soxR | azo2617 | azo2618 | TREMBL:Q89L44: 48% identity.64% similarity. probable haloacid dehalogenase-like hydrolase. InterPro:IPR005834; Hydrolase. Pfam:PF00702; Hydrolase; Phosphoglycolate phosphatase(PGP). TIGR00099: conserved hypothetical prot; Function unclear. | Probable redox-sensitive transcriptional activator,; High confidence in function and specificity. | 0.775 |
| azo2619 | azo2616 | azo2619 | azo2616 | Putative methyltransferase; Similar to TREMBL:Q98BY2 (39% identity); TREMBL:Q9A2R1 (40% identity); TREMBL:Q89KG6 (34% identity). Pfam (PF01209): ubiE/COQ5 methyltransferase family; Function unclear. | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.647 |
| azo2619 | azo2617 | azo2619 | azo2617 | Putative methyltransferase; Similar to TREMBL:Q98BY2 (39% identity); TREMBL:Q9A2R1 (40% identity); TREMBL:Q89KG6 (34% identity). Pfam (PF01209): ubiE/COQ5 methyltransferase family; Function unclear. | TREMBL:Q89L44: 48% identity.64% similarity. probable haloacid dehalogenase-like hydrolase. InterPro:IPR005834; Hydrolase. Pfam:PF00702; Hydrolase; Phosphoglycolate phosphatase(PGP). TIGR00099: conserved hypothetical prot; Function unclear. | 0.584 |
| azo2619 | soxR | azo2619 | azo2618 | Putative methyltransferase; Similar to TREMBL:Q98BY2 (39% identity); TREMBL:Q9A2R1 (40% identity); TREMBL:Q89KG6 (34% identity). Pfam (PF01209): ubiE/COQ5 methyltransferase family; Function unclear. | Probable redox-sensitive transcriptional activator,; High confidence in function and specificity. | 0.764 |
| gloB1 | azo2616 | azo1208 | azo2616 | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...] | 0.571 |