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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gltB | ilvA | Rv3859c | Rv1559 | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Probable threonine dehydratase IlvA; 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 (By similarity). | 0.865 |
| gltB | ilvB1 | Rv3859c | Rv3003c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | 0.556 |
| gltB | ilvC | Rv3859c | Rv3001c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Ketol-acid reductoisomerase (NADP(+)); 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. It is also able to use 3-hydroxypyruvate (HP). | 0.864 |
| gltB | ilvD | Rv3859c | Rv0189c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Rv0189c, (MTCI28.28c), len: 575 aa. Probable ilvD,dihydroxy-acid dehydratase, similar to many e.g. ILVD_LACLA|Q02139 dihydroxy-acid dehydratase (dad) from Lactococcus lactis (subsp. lactis) (Streptococcus lactis) (570 aa), FASTA scores: opt: 1605, E(): 0, (46.0% identity in 561 aa overlap). Also similar to ML2608|MLCL622.06c|O06069|ILVD_MYCLE dihydroxy-acid dehydratase from Mycobacterium leprae (564 aa). Contains PS00886 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. Belongs to the ILVD / EDD family. Cofactor: binds 1 4FE-4S cluster (potential). | 0.933 |
| gltB | ilvE | Rv3859c | Rv2210c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Branched-chain amino acid transaminase IlvE; Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.558 |
| gltB | ilvN | Rv3859c | Rv3002c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Probable acetolactate synthase (small subunit) IlvN (acetohydroxy-acid synthase) (AHAS) (ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the acetolactate synthase small subunit family. | 0.868 |
| gltB | leuA | Rv3859c | Rv3710 | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | 2-isopropylmalate synthase LeuA (alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS); 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). | 0.422 |
| gltB | leuB | Rv3859c | Rv2995c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | Probable 3-isopropylmalate dehydrogenase LeuB (beta-IPM dehydrogenase) (IMDH) (3-IPM-DH); 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; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.806 |
| gltB | leuC | Rv3859c | Rv2988c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.855 |
| gltB | leuD | Rv3859c | Rv2987c | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | 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. | 0.806 |
| ilvA | gltB | Rv1559 | Rv3859c | Probable threonine dehydratase IlvA; 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 (By similarity). | Glutamate synthase [NADPH] large chain; Rv3859c, (MTCY01A6.09), len: 1527 aa. Probable gltB,ferredoxin-dependent glutamate synthase large subunit,equivalent to Q9CDD5|GLTB|ML0061 putative ferredoxin-dependent glutamate synthase from Mycobacterium leprae (1527 aa), FASTA scores: opt: 9277, E(): 0, (90.25% identity in 1527 aa overlap). Also highly similar to many e.g. Q9S2Y9|SC3A3.04c from Streptomyces coelicolor (1514 aa), FASTA scores: opt: 5939, E(): 0, (64.3% identity in 1544 aa overlap); Q9Z465|GLTB from Corynebacterium glutamicum (Brevibacterium flavum) (1510 aa), FASTA scores: opt [...] | 0.865 |
| ilvA | ilvB1 | Rv1559 | Rv3003c | Probable threonine dehydratase IlvA; 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 (By similarity). | Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2- hydroxybutyrate. | 0.972 |
| ilvA | ilvC | Rv1559 | Rv3001c | Probable threonine dehydratase IlvA; 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 (By similarity). | Ketol-acid reductoisomerase (NADP(+)); 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. It is also able to use 3-hydroxypyruvate (HP). | 0.900 |
| ilvA | ilvD | Rv1559 | Rv0189c | Probable threonine dehydratase IlvA; 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 (By similarity). | Rv0189c, (MTCI28.28c), len: 575 aa. Probable ilvD,dihydroxy-acid dehydratase, similar to many e.g. ILVD_LACLA|Q02139 dihydroxy-acid dehydratase (dad) from Lactococcus lactis (subsp. lactis) (Streptococcus lactis) (570 aa), FASTA scores: opt: 1605, E(): 0, (46.0% identity in 561 aa overlap). Also similar to ML2608|MLCL622.06c|O06069|ILVD_MYCLE dihydroxy-acid dehydratase from Mycobacterium leprae (564 aa). Contains PS00886 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. Belongs to the ILVD / EDD family. Cofactor: binds 1 4FE-4S cluster (potential). | 0.946 |
| ilvA | ilvE | Rv1559 | Rv2210c | Probable threonine dehydratase IlvA; 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 (By similarity). | Branched-chain amino acid transaminase IlvE; Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.974 |
| ilvA | ilvN | Rv1559 | Rv3002c | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable acetolactate synthase (small subunit) IlvN (acetohydroxy-acid synthase) (AHAS) (ALS); Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Belongs to the acetolactate synthase small subunit family. | 0.991 |
| ilvA | leuA | Rv1559 | Rv3710 | Probable threonine dehydratase IlvA; 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 (By similarity). | 2-isopropylmalate synthase LeuA (alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS); 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). | 0.651 |
| ilvA | leuB | Rv1559 | Rv2995c | Probable threonine dehydratase IlvA; 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 (By similarity). | Probable 3-isopropylmalate dehydrogenase LeuB (beta-IPM dehydrogenase) (IMDH) (3-IPM-DH); 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; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.977 |
| ilvA | leuC | Rv1559 | Rv2988c | Probable threonine dehydratase IlvA; 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 (By similarity). | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.700 |
| ilvA | leuD | Rv1559 | Rv2987c | Probable threonine dehydratase IlvA; 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 (By similarity). | 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. | 0.785 |
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