| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gltB | hom | azo3642 | azo2081 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.641 |
| gltB | ilvA | azo3642 | azo0500 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.690 |
| gltB | ilvC | azo3642 | azo3156 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.812 |
| gltB | leuD | azo3642 | azo1040 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | LeuD protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.673 |
| gltB | lysC | azo3642 | azo3115 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family. | 0.593 |
| gltB | serC | azo3642 | azo1067 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | Phosphoserine transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine.; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.448 |
| gltB | thrC | azo3642 | azo2080 | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | ThrC protein; Threonine synthase is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate,using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. Similar to trembl|Q8XZR7 (68%), to sprot|THRC_METGL (69%) and to sprot|THRC_PSEAE (42%). TIGRFAM: thrC, threonine synthase Pfam (PF00291): Pyridoxal-phosphate dependent enzyme; High confidence in f [...] | 0.692 |
| hom | gltB | azo2081 | azo3642 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.641 |
| hom | ilvA | azo2081 | azo0500 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.753 |
| hom | ilvC | azo2081 | azo3156 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.469 |
| hom | leuD | azo2081 | azo1040 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | LeuD protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.448 |
| hom | lysC | azo2081 | azo3115 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family. | 0.984 |
| hom | serC | azo2081 | azo1067 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Phosphoserine transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine.; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.424 |
| hom | thrB | azo2081 | azo3604 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable homoserine kinase. Homology to thrB of M. flagellum of 51% (sprot|KHSE_METFL). CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-homoserine. Pfam: Aminoglycoside phosphotransferase no signal peptide no TMHs; High confidence in function and specificity; Belongs to the pseudomonas-type ThrB family. | 0.945 |
| hom | thrC | azo2081 | azo2080 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | ThrC protein; Threonine synthase is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate,using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. Similar to trembl|Q8XZR7 (68%), to sprot|THRC_METGL (69%) and to sprot|THRC_PSEAE (42%). TIGRFAM: thrC, threonine synthase Pfam (PF00291): Pyridoxal-phosphate dependent enzyme; High confidence in f [...] | 0.988 |
| hom | thrH | azo2081 | azo3743 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable homoserine kinase; ThrH encodes a protein with an in vivo homoserine-kinase-like activity in P. aeruginosa. Homoserine kinase,the product of the thrB gene, catalyzes an obligatory step of threonine biosynthesis. Similar trembl|Q9I2Y2 (62%). Pfam (PF00702): haloacid dehalogenase-like hydrolase; Function unclear. | 0.882 |
| ilvA | gltB | azo0500 | azo3642 | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.690 |
| ilvA | hom | azo0500 | azo2081 | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.753 |
| ilvA | ilvC | azo0500 | azo3156 | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.791 |
| ilvA | leuD | azo0500 | azo1040 | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | LeuD protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.646 |
