node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADZ89614.1 | ADZ89975.1 | Marme_0311 | Marme_0692 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.930 |
ADZ89614.1 | ADZ90231.1 | Marme_0311 | Marme_0956 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | 0.474 |
ADZ89614.1 | ADZ90946.1 | Marme_0311 | Marme_1689 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | KEGG: mmw:Mmwyl1_2758 sarcosine oxidase subunit alpha family protein; TIGRFAM: Sarcosine oxidase, alpha subunit, heterotetrameric; PFAM: Glycine cleavage T-protein, N-terminal; Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; Glycine cleavage T-protein, C-terminal barrel; Belongs to the GcvT family. | 0.923 |
ADZ89614.1 | gcvP | Marme_0311 | Marme_2175 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.962 |
ADZ89614.1 | ilvA | Marme_0311 | Marme_3751 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 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. | 0.938 |
ADZ89614.1 | kbl | Marme_0311 | Marme_1285 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.911 |
ADZ89614.1 | tdh | Marme_0311 | Marme_0597 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.901 |
ADZ89614.1 | tdh-2 | Marme_0311 | Marme_1286 | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.902 |
ADZ89975.1 | ADZ89614.1 | Marme_0692 | Marme_0311 | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.930 |
ADZ89975.1 | gcvP | Marme_0692 | Marme_2175 | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.514 |
ADZ89975.1 | ilvA | Marme_0692 | Marme_3751 | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, 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. | 0.972 |
ADZ89975.1 | tdh | Marme_0692 | Marme_0597 | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.902 |
ADZ89975.1 | tdh-2 | Marme_0692 | Marme_1286 | TIGRFAM: Threonine synthase; KEGG: mmw:Mmwyl1_3764 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.902 |
ADZ90231.1 | ADZ89614.1 | Marme_0956 | Marme_0311 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.474 |
ADZ90231.1 | ADZ90946.1 | Marme_0956 | Marme_1689 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | KEGG: mmw:Mmwyl1_2758 sarcosine oxidase subunit alpha family protein; TIGRFAM: Sarcosine oxidase, alpha subunit, heterotetrameric; PFAM: Glycine cleavage T-protein, N-terminal; Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; Glycine cleavage T-protein, C-terminal barrel; Belongs to the GcvT family. | 0.572 |
ADZ90231.1 | bioF | Marme_0956 | Marme_3250 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | 8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | 0.730 |
ADZ90231.1 | gcvP | Marme_0956 | Marme_2175 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.525 |
ADZ90231.1 | ilvA | Marme_0956 | Marme_3751 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | 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. | 0.672 |
ADZ90231.1 | kbl | Marme_0956 | Marme_1285 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.730 |
ADZ90231.1 | tdh | Marme_0956 | Marme_0597 | Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; TIGRFAM: Amino acid adenylation; KEGG: pfs:PFLU3223 putative non-ribosomal peptide synthetase; PFAM: AMP-dependent synthetase/ligase; Condensation domain; Phosphopantetheine-binding. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.691 |