node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Galf_1819 | Galf_2517 | Galf_1819 | Galf_2517 | TIGRFAM: threonine synthase; KEGG: slt:Slit_2217 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.652 |
Galf_1819 | ilvA | Galf_1819 | Galf_2668 | TIGRFAM: threonine synthase; KEGG: slt:Slit_2217 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | Threonine dehydratase, biosynthetic; 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. | 0.970 |
Galf_1819 | leuB | Galf_1819 | Galf_0493 | TIGRFAM: threonine synthase; KEGG: slt:Slit_2217 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.582 |
Galf_2517 | Galf_1819 | Galf_2517 | Galf_1819 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | TIGRFAM: threonine synthase; KEGG: slt:Slit_2217 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.652 |
Galf_2517 | Galf_2518 | Galf_2517 | Galf_2518 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.999 |
Galf_2517 | Galf_2847 | Galf_2517 | Galf_2847 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | 0.999 |
Galf_2517 | ilvA | Galf_2517 | Galf_2668 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | Threonine dehydratase, biosynthetic; 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. | 0.983 |
Galf_2517 | ilvE | Galf_2517 | Galf_0516 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.631 |
Galf_2517 | leuB | Galf_2517 | Galf_0493 | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.991 |
Galf_2518 | Galf_2517 | Galf_2518 | Galf_2517 | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.999 |
Galf_2518 | Galf_2847 | Galf_2518 | Galf_2847 | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | 0.921 |
Galf_2518 | ilvA | Galf_2518 | Galf_2668 | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | Threonine dehydratase, biosynthetic; 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. | 0.940 |
Galf_2518 | ilvE | Galf_2518 | Galf_0516 | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.668 |
Galf_2518 | leuB | Galf_2518 | Galf_0493 | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.972 |
Galf_2847 | Galf_2517 | Galf_2847 | Galf_2517 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | KEGG: slt:Slit_2403 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.999 |
Galf_2847 | Galf_2518 | Galf_2847 | Galf_2518 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | KEGG: slt:Slit_2404 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.921 |
Galf_2847 | ilvA | Galf_2847 | Galf_2668 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | Threonine dehydratase, biosynthetic; 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. | 0.948 |
Galf_2847 | ilvE | Galf_2847 | Galf_0516 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.668 |
Galf_2847 | leuB | Galf_2847 | Galf_0493 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: bte:BTH_II1989 acetolactate synthase II, large subunit; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.973 |
glyA | glyA-2 | Galf_0904 | Galf_2348 | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.901 |