Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| datA | ilvA | ZOBELLIA_3959 | ZOBELLIA_4566 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 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. | 0.872 |
| datA | ilvB | ZOBELLIA_3959 | ZOBELLIA_4570 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity. | 0.629 |
| datA | ilvC | ZOBELLIA_3959 | ZOBELLIA_4567 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | Ketol-acid reductoisomerase; 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. | 0.410 |
| datA | ilvD1 | ZOBELLIA_3959 | ZOBELLIA_4571 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid; Binds a 4Fe-4S cluster; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.972 |
| datA | ilvE | ZOBELLIA_3959 | ZOBELLIA_2819 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | Branched-chain-amino-acid aminotransferase is involved in leucine, isoleucine and valine biosynthesis from L-glutamic acid; It forms a homohexamer and used one Pyridoxal phosphate as cofactor per subunit; Belongs to the Aminotransferase class IV; Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
| datA | ilvH | ZOBELLIA_3959 | ZOBELLIA_4568 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | Acetolactate synthase is a complex of a large catalytic chain and a smaller regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The regulatory subunit, IlvH, features an ACT domain. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration; Localized in the cytoplasm; High confidence in function and specificity. | 0.515 |
| datA | leuA2 | ZOBELLIA_3959 | ZOBELLIA_4723 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 2-Isopropylmalate synthase catalyzes the first step in the L-leucine biosynthesis pathway. LeuA condensates the acetyl group of acetyl-CoA with 3-methyl-2- oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). LeuA2 is a paralogue of leuA1 which misses the C-terminal LeuA-dimerization domain. Localized in the cytoplasm; Specificity unclear; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.967 |
| datA | leuC | ZOBELLIA_3959 | ZOBELLIA_4556 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 3-Isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.466 |
| datA | panB | ZOBELLIA_3959 | ZOBELLIA_4717 | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 3-Methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.914 |
| ilvA | datA | ZOBELLIA_4566 | ZOBELLIA_3959 | 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. | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 0.872 |
| ilvA | ilvB | ZOBELLIA_4566 | ZOBELLIA_4570 | 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. | Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity. | 0.971 |
| ilvA | ilvC | ZOBELLIA_4566 | ZOBELLIA_4567 | 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. | Ketol-acid reductoisomerase; 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. | 0.824 |
| ilvA | ilvD1 | ZOBELLIA_4566 | ZOBELLIA_4571 | 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. | Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid; Binds a 4Fe-4S cluster; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.896 |
| ilvA | ilvE | ZOBELLIA_4566 | ZOBELLIA_2819 | 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. | Branched-chain-amino-acid aminotransferase is involved in leucine, isoleucine and valine biosynthesis from L-glutamic acid; It forms a homohexamer and used one Pyridoxal phosphate as cofactor per subunit; Belongs to the Aminotransferase class IV; Localized in the cytoplasm; High confidence in function and specificity. | 0.872 |
| ilvA | ilvH | ZOBELLIA_4566 | ZOBELLIA_4568 | 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. | Acetolactate synthase is a complex of a large catalytic chain and a smaller regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The regulatory subunit, IlvH, features an ACT domain. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration; Localized in the cytoplasm; High confidence in function and specificity. | 0.984 |
| ilvA | leuC | ZOBELLIA_4566 | ZOBELLIA_4556 | 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. | 3-Isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.451 |
| ilvA | leuD | ZOBELLIA_4566 | ZOBELLIA_4557 | 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. | 3-Isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.474 |
| ilvB | datA | ZOBELLIA_4570 | ZOBELLIA_3959 | Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity. | D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...] | 0.629 |
| ilvB | ilvA | ZOBELLIA_4570 | ZOBELLIA_4566 | Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity. | 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. | 0.971 |
| ilvB | ilvC | ZOBELLIA_4570 | ZOBELLIA_4567 | Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity. | Ketol-acid reductoisomerase; 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. | 0.991 |
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