node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Cpin_1921 | Cpin_1922 | Cpin_1921 | Cpin_1922 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | 0.999 |
Cpin_1921 | Cpin_5431 | Cpin_1921 | Cpin_5431 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.506 |
Cpin_1921 | Cpin_6128 | Cpin_1921 | Cpin_6128 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: fph:Fphi_1548 acetolactate synthase large subunit. | 0.902 |
Cpin_1921 | ilvA | Cpin_1921 | Cpin_1924 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | 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. | 0.977 |
Cpin_1921 | ilvD | Cpin_1921 | Cpin_1920 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | KEGG: pin:Ping_2151 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.987 |
Cpin_1921 | leuB | Cpin_1921 | Cpin_1985 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large 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. | 0.984 |
Cpin_1922 | Cpin_1921 | Cpin_1922 | Cpin_1921 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | 0.999 |
Cpin_1922 | Cpin_5431 | Cpin_1922 | Cpin_5431 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.744 |
Cpin_1922 | Cpin_6128 | Cpin_1922 | Cpin_6128 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: fph:Fphi_1548 acetolactate synthase large subunit. | 0.999 |
Cpin_1922 | ilvA | Cpin_1922 | Cpin_1924 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | 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. | 0.993 |
Cpin_1922 | ilvD | Cpin_1922 | Cpin_1920 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | KEGG: pin:Ping_2151 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.980 |
Cpin_1922 | leuB | Cpin_1922 | Cpin_1985 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small 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. | 0.993 |
Cpin_3667 | Cpin_6242 | Cpin_3667 | Cpin_6242 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein; KEGG: ade:Adeh_3706 cystathionine beta-synthase. | KEGG: psa:PST_3559 L-serine dehydratase, iron- sulfur-dependent, single chain form; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.931 |
Cpin_3667 | ilvA | Cpin_3667 | Cpin_1924 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein; KEGG: ade:Adeh_3706 cystathionine beta-synthase. | 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. | 0.937 |
Cpin_3667 | trpA | Cpin_3667 | Cpin_1828 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein; KEGG: ade:Adeh_3706 cystathionine beta-synthase. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.925 |
Cpin_3667 | trpB | Cpin_3667 | Cpin_1827 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein; KEGG: ade:Adeh_3706 cystathionine beta-synthase. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.917 |
Cpin_5431 | Cpin_1921 | Cpin_5431 | Cpin_1921 | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: ftn:FTN_1042 acetolactate synthase large subunit. | 0.506 |
Cpin_5431 | Cpin_1922 | Cpin_5431 | Cpin_1922 | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: sfu:Sfum_3025 acetolactate synthase, small subunit. | 0.744 |
Cpin_5431 | Cpin_6128 | Cpin_5431 | Cpin_6128 | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: fph:Fphi_1548 acetolactate synthase large subunit. | 0.516 |
Cpin_5431 | ilvA | Cpin_5431 | Cpin_1924 | KEGG: sfv:SFV_0003 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 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. | 0.973 |