node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
azo2056 | dnaQ | azo2056 | azo2054 | Conserved hypothetical protein; Similar to TREMBL:Q82XV9 (41% identity, generic methyl-transferase); TREMBL:Q7NYL9 (45% identity). | DNA-directed DNA polymerase; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. | 0.815 |
azo2056 | gloB2 | azo2056 | azo2057 | Conserved hypothetical protein; Similar to TREMBL:Q82XV9 (41% identity, generic methyl-transferase); TREMBL:Q7NYL9 (45% identity). | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.648 |
azo2056 | rnhA2 | azo2056 | azo2055 | Conserved hypothetical protein; Similar to TREMBL:Q82XV9 (41% identity, generic methyl-transferase); TREMBL:Q7NYL9 (45% identity). | Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | 0.868 |
azo2279 | gloB2 | azo2279 | azo2057 | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.608 |
azo2279 | ycbL | azo2279 | azo3823 | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | Hypothetical protein ycbL. TREMBL:Q7P1X5-63% identity. Interpro:IPR001279-Blactamase like Pfam-GlyoxylaseII family relationship. Phosphoribosylglycinamide synthetase,Respiratory chain NADH dehydrogenase; KH domain and RTX toxin acyltransferase family relationship. ispD: 4-diphosphocytidyl-2C-methyl-D-ery; High confidence in function and specificity. | 0.608 |
azo2616 | azo2654 | azo2616 | azo2654 | 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 [...] | Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. 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-hydroxyp [...] | 0.413 |
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 |
azo2654 | azo2616 | azo2654 | azo2616 | Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. 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-hydroxyp [...] | 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 [...] | 0.413 |
azo2654 | gloB2 | azo2654 | azo2057 | Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. 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-hydroxyp [...] | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.593 |
dnaQ | azo2056 | azo2054 | azo2056 | DNA-directed DNA polymerase; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. | Conserved hypothetical protein; Similar to TREMBL:Q82XV9 (41% identity, generic methyl-transferase); TREMBL:Q7NYL9 (45% identity). | 0.815 |
dnaQ | gloB2 | azo2054 | azo2057 | DNA-directed DNA polymerase; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.635 |
dnaQ | rnhA2 | azo2054 | azo2055 | DNA-directed DNA polymerase; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. | Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | 0.925 |
gloA1 | gloB2 | azo0692 | azo2057 | Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction: glutathione + methylglyoxal = (R)-S-lactoylglutathione,; Function unclear. | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.813 |
gloA2 | gloB2 | azo3228 | azo2057 | Lactoylglutathione lyase; Glyoxalase I catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. Similar to trembl|Q9HY85 (74%) and to sprot|LGUL_NEIMA (70%). Pfam (PF00903): Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily ProDom (PD002334): Glyoxalase I; High confidence in function and specificity. | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.907 |
gloA2 | ycbL | azo3228 | azo3823 | Lactoylglutathione lyase; Glyoxalase I catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. Similar to trembl|Q9HY85 (74%) and to sprot|LGUL_NEIMA (70%). Pfam (PF00903): Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily ProDom (PD002334): Glyoxalase I; High confidence in function and specificity. | Hypothetical protein ycbL. TREMBL:Q7P1X5-63% identity. Interpro:IPR001279-Blactamase like Pfam-GlyoxylaseII family relationship. Phosphoribosylglycinamide synthetase,Respiratory chain NADH dehydrogenase; KH domain and RTX toxin acyltransferase family relationship. ispD: 4-diphosphocytidyl-2C-methyl-D-ery; High confidence in function and specificity. | 0.906 |
gloB2 | azo2056 | azo2057 | azo2056 | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | Conserved hypothetical protein; Similar to TREMBL:Q82XV9 (41% identity, generic methyl-transferase); TREMBL:Q7NYL9 (45% identity). | 0.648 |
gloB2 | azo2279 | azo2057 | azo2279 | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.608 |
gloB2 | azo2616 | azo2057 | 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 |
gloB2 | azo2654 | azo2057 | azo2654 | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. 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-hydroxyp [...] | 0.593 |
gloB2 | dnaQ | azo2057 | azo2054 | Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | DNA-directed DNA polymerase; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. | 0.635 |