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 |
| PSM36_0586 | PSM36_2809 | PSM36_0586 | PSM36_2809 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | L-threonine aldolase; High confidence in function and specificity. | 0.922 |
| PSM36_0586 | PSM36_3285 | PSM36_0586 | PSM36_3285 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | Aspartate kinase; High confidence in function and specificity. | 0.598 |
| PSM36_0586 | gltB | PSM36_0586 | PSM36_2872 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH; High confidence in function and specificity. | 0.596 |
| PSM36_0586 | leuD | PSM36_0586 | PSM36_0864 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 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. | 0.625 |
| PSM36_0586 | pdxA | PSM36_0586 | PSM36_0871 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP); High confidence in function and specificity; Belongs to the PdxA family. | 0.903 |
| PSM36_0586 | serC | PSM36_0586 | PSM36_0622 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.930 |
| PSM36_0586 | tdh | PSM36_0586 | PSM36_1742 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 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. | 0.903 |
| PSM36_0586 | thrA | PSM36_0586 | PSM36_0078 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | Bifunctional aspartokinase; Aspartate kinase (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine; High confidence in function and specificity. | 0.954 |
| PSM36_0586 | thrC | PSM36_0586 | PSM36_0076 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine; High confidence in function and specificity. | 0.900 |
| PSM36_2809 | PSM36_0586 | PSM36_2809 | PSM36_0586 | L-threonine aldolase; High confidence in function and specificity. | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 0.922 |
| PSM36_2809 | gltB | PSM36_2809 | PSM36_2872 | L-threonine aldolase; High confidence in function and specificity. | 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH; High confidence in function and specificity. | 0.413 |
| PSM36_2809 | tdh | PSM36_2809 | PSM36_1742 | L-threonine aldolase; High confidence in function and specificity. | 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 |
| PSM36_2809 | thrA | PSM36_2809 | PSM36_0078 | L-threonine aldolase; High confidence in function and specificity. | Bifunctional aspartokinase; Aspartate kinase (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine; High confidence in function and specificity. | 0.403 |
| PSM36_2809 | thrC | PSM36_2809 | PSM36_0076 | L-threonine aldolase; High confidence in function and specificity. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine; High confidence in function and specificity. | 0.922 |
| PSM36_3285 | PSM36_0586 | PSM36_3285 | PSM36_0586 | Aspartate kinase; High confidence in function and specificity. | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants; Conser [...] | 0.598 |
| PSM36_3285 | gltB | PSM36_3285 | PSM36_2872 | Aspartate kinase; High confidence in function and specificity. | 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH; High confidence in function and specificity. | 0.450 |
| PSM36_3285 | thrA | PSM36_3285 | PSM36_0078 | Aspartate kinase; High confidence in function and specificity. | Bifunctional aspartokinase; Aspartate kinase (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine; High confidence in function and specificity. | 0.960 |
| PSM36_3285 | thrC | PSM36_3285 | PSM36_0076 | Aspartate kinase; High confidence in function and specificity. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine; High confidence in function and specificity. | 0.598 |
| apgM | thrA | PSM36_0077 | PSM36_0078 | This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsble for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate; High confidence in function and specificity. | Bifunctional aspartokinase; Aspartate kinase (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine; High confidence in function and specificity. | 0.821 |
| apgM | thrC | PSM36_0077 | PSM36_0076 | This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsble for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate; High confidence in function and specificity. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine; High confidence in function and specificity. | 0.568 |
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