Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CN09_03380 | CN09_06240 | CN09_03380 | CN09_06240 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | 0.896 |
| CN09_03380 | CN09_06985 | CN09_03380 | CN09_06985 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | 0.853 |
| CN09_03380 | CN09_10375 | CN09_03380 | CN09_10375 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5'-phosphate; In the C-terminal section; belongs to the HTP reductase family | 0.999 |
| CN09_03380 | ispDF | CN09_03380 | CN09_07765 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF) | 0.999 |
| CN09_03380 | nnrD | CN09_03380 | CN09_07485 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family | 0.949 |
| CN09_03380 | ribB | CN09_03380 | CN09_16765 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the DHBP synthase family | 0.999 |
| CN09_03380 | topA | CN09_03380 | CN09_09825 | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] | 0.917 |
| CN09_06240 | CN09_03380 | CN09_06240 | CN09_03380 | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | 0.896 |
| CN09_06240 | CN09_06985 | CN09_06240 | CN09_06985 | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | 0.967 |
| CN09_06240 | fmt | CN09_06240 | CN09_14745 | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | 0.999 |
| CN09_06240 | ispDF | CN09_06240 | CN09_07765 | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF) | 0.939 |
| CN09_06240 | nnrD | CN09_06240 | CN09_07485 | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family | 0.547 |
| CN09_06985 | CN09_03380 | CN09_06985 | CN09_03380 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | 2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology | 0.853 |
| CN09_06985 | CN09_06240 | CN09_06985 | CN09_06240 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Fumarate hydratase class I; Catalyzes the reversible hydration of fumarate to (S)- malate; Belongs to the class-I fumarase family | 0.967 |
| CN09_06985 | CN09_08270 | CN09_06985 | CN09_08270 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Peptidoglycan-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology | 0.853 |
| CN09_06985 | CN09_10375 | CN09_06985 | CN09_10375 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5'-phosphate; In the C-terminal section; belongs to the HTP reductase family | 0.985 |
| CN09_06985 | aroK | CN09_06985 | CN09_27630 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Shikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family | 0.828 |
| CN09_06985 | fmt | CN09_06985 | CN09_14745 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | 0.774 |
| CN09_06985 | ispDF | CN09_06985 | CN09_07765 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF) | 0.894 |
| CN09_06985 | nnrD | CN09_06985 | CN09_07485 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family | 0.984 |
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