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 |
| DIP0427 | ilvA | DIP0427 | DIP1579 | Similar to Clostridium acetobutylicum lactate dehydrogenase CAC3552 TR:AAK81477 (EMBL:AE007851) (320 aa) fasta scores: E(): 1.6e-36, 38.6% id in 316 aa, and to Bacillus subtilis L-lactate dehydrogenase Ldh or LctE SW:LDH_BACSU (P13714) (320 aa) fasta scores: E(): 2.9e-25, 33.95% id in 324 aa; Belongs to the LDH/MDH superfamily. | 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. | 0.818 |
| DIP0427 | ilvE | DIP0427 | DIP1636 | Similar to Clostridium acetobutylicum lactate dehydrogenase CAC3552 TR:AAK81477 (EMBL:AE007851) (320 aa) fasta scores: E(): 1.6e-36, 38.6% id in 316 aa, and to Bacillus subtilis L-lactate dehydrogenase Ldh or LctE SW:LDH_BACSU (P13714) (320 aa) fasta scores: E(): 2.9e-25, 33.95% id in 324 aa; Belongs to the LDH/MDH superfamily. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.801 |
| DIP0427 | ldh | DIP0427 | DIP2255 | Similar to Clostridium acetobutylicum lactate dehydrogenase CAC3552 TR:AAK81477 (EMBL:AE007851) (320 aa) fasta scores: E(): 1.6e-36, 38.6% id in 316 aa, and to Bacillus subtilis L-lactate dehydrogenase Ldh or LctE SW:LDH_BACSU (P13714) (320 aa) fasta scores: E(): 2.9e-25, 33.95% id in 324 aa; Belongs to the LDH/MDH superfamily. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family. | 0.921 |
| DIP0427 | leuA | DIP0427 | DIP0266 | Similar to Clostridium acetobutylicum lactate dehydrogenase CAC3552 TR:AAK81477 (EMBL:AE007851) (320 aa) fasta scores: E(): 1.6e-36, 38.6% id in 316 aa, and to Bacillus subtilis L-lactate dehydrogenase Ldh or LctE SW:LDH_BACSU (P13714) (320 aa) fasta scores: E(): 2.9e-25, 33.95% id in 324 aa; Belongs to the LDH/MDH superfamily. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.831 |
| DIP2136 | ilvD | DIP2136 | DIP1096 | Putative aminotransferase; Similar to Mycobacterium tuberculosis probable aspartate aminotransferase AspC or Rv0337c or MT0351 or MTCY279.04c SW:AAT_MYCTU (O33267) (429 aa) fasta scores: E(): 2.4e-120, 71.32% id in 415 aa, and to Escherichia coli probable aminotransferase YfbQ or B2290 SW:YFBQ_ECOLI (P77727) (405 aa) fasta scores: E(): 1.8e-101, 61.59% id in 401 aa, and to Methylobacillus flagellatum aspartate aminotransferase Aat TR:Q9RAN0 (EMBL:L78665) (429 aa) fasta scores: E(): 1.7e-87, 55.08% id in 403 aa. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.912 |
| DIP2136 | ilvE | DIP2136 | DIP1636 | Putative aminotransferase; Similar to Mycobacterium tuberculosis probable aspartate aminotransferase AspC or Rv0337c or MT0351 or MTCY279.04c SW:AAT_MYCTU (O33267) (429 aa) fasta scores: E(): 2.4e-120, 71.32% id in 415 aa, and to Escherichia coli probable aminotransferase YfbQ or B2290 SW:YFBQ_ECOLI (P77727) (405 aa) fasta scores: E(): 1.8e-101, 61.59% id in 401 aa, and to Methylobacillus flagellatum aspartate aminotransferase Aat TR:Q9RAN0 (EMBL:L78665) (429 aa) fasta scores: E(): 1.7e-87, 55.08% id in 403 aa. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.902 |
| DIP2136 | leuA | DIP2136 | DIP0266 | Putative aminotransferase; Similar to Mycobacterium tuberculosis probable aspartate aminotransferase AspC or Rv0337c or MT0351 or MTCY279.04c SW:AAT_MYCTU (O33267) (429 aa) fasta scores: E(): 2.4e-120, 71.32% id in 415 aa, and to Escherichia coli probable aminotransferase YfbQ or B2290 SW:YFBQ_ECOLI (P77727) (405 aa) fasta scores: E(): 1.8e-101, 61.59% id in 401 aa, and to Methylobacillus flagellatum aspartate aminotransferase Aat TR:Q9RAN0 (EMBL:L78665) (429 aa) fasta scores: E(): 1.7e-87, 55.08% id in 403 aa. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.905 |
| ilvA | DIP0427 | DIP1579 | DIP0427 | 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. | Similar to Clostridium acetobutylicum lactate dehydrogenase CAC3552 TR:AAK81477 (EMBL:AE007851) (320 aa) fasta scores: E(): 1.6e-36, 38.6% id in 316 aa, and to Bacillus subtilis L-lactate dehydrogenase Ldh or LctE SW:LDH_BACSU (P13714) (320 aa) fasta scores: E(): 2.9e-25, 33.95% id in 324 aa; Belongs to the LDH/MDH superfamily. | 0.818 |
| ilvA | ilvC | DIP1579 | DIP1100 | 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. | 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. | 0.880 |
| ilvA | ilvD | DIP1579 | DIP1096 | 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. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.906 |
| ilvA | ilvE | DIP1579 | DIP1636 | 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. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.975 |
| ilvA | ldh | DIP1579 | DIP2255 | 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. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family. | 0.818 |
| ilvA | leuA | DIP1579 | DIP0266 | 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. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.614 |
| ilvA | thrA | DIP1579 | DIP1036 | 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. | Similar to Corynebacterium glutamicum homoserine dehydrogenase Hom or ThrA SW:DHOM_CORGL (P08499) (445 aa) fasta scores: E(): 4.2e-117, 75.28% id in 437 aa, and to Bacillus subtilis homoserine dehydrogenase Hom or Tdm SW:DHOM_BACSU (P19582) (433 aa) fasta scores: E(): 4.2e-54, 40.18% id in 433 aa. | 0.889 |
| ilvA | thrB | DIP1579 | DIP1037 | 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.823 |
| ilvC | ilvA | DIP1100 | DIP1579 | 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. | 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. | 0.880 |
| ilvC | ilvD | DIP1100 | DIP1096 | 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. | Similar to Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.998 |
| ilvC | ilvE | DIP1100 | DIP1636 | 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. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.907 |
| ilvC | leuA | DIP1100 | DIP0266 | 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. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.914 |
| ilvC | thrA | DIP1100 | DIP1036 | 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. | Similar to Corynebacterium glutamicum homoserine dehydrogenase Hom or ThrA SW:DHOM_CORGL (P08499) (445 aa) fasta scores: E(): 4.2e-117, 75.28% id in 437 aa, and to Bacillus subtilis homoserine dehydrogenase Hom or Tdm SW:DHOM_BACSU (P19582) (433 aa) fasta scores: E(): 4.2e-54, 40.18% id in 433 aa. | 0.418 |
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