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 |
| CAZ95294.1 | CAZ97009.1 | ZOBELLIA_1238 | ZOBELLIA_2862 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | 0.914 |
| CAZ95294.1 | CAZ98687.1 | ZOBELLIA_1238 | ZOBELLIA_4552 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.926 |
| CAZ95294.1 | aatA-2 | ZOBELLIA_1238 | ZOBELLIA_756 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.804 |
| CAZ95294.1 | aatB | ZOBELLIA_1238 | ZOBELLIA_705 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.804 |
| CAZ95294.1 | ggtA | ZOBELLIA_1238 | ZOBELLIA_4414 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Gamma-glutamyltranspeptidase, family T3; Gamma-glutamyltranspeptidase is a threonine peptidase that catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GgtA plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. This enzyme consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor; Belongs to the family T3 of the peptidases; Putative lipoprotein signal peptide cleaved between the residues 19 an [...] | 0.903 |
| CAZ95294.1 | glyA | ZOBELLIA_1238 | ZOBELLIA_4742 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.824 |
| CAZ95294.1 | metB | ZOBELLIA_1238 | ZOBELLIA_1454 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.805 |
| CAZ95294.1 | metC | ZOBELLIA_1238 | ZOBELLIA_4001 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Cystathionine beta-lyase (CBL) is found in the Selenoamino acids metabolism pathway and in methionine and cysteine biosynthesis pathways. It converts (seleno)cystathionine to (seleno)homocysteine but is also able to catalyze an alpha, gamma elimination; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.805 |
| CAZ95294.1 | pepD1 | ZOBELLIA_1238 | ZOBELLIA_1554 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Xaa-His dipeptidase, also known as aminoacyl-histidine dipeptidase, catalyzes the hydrolysis of Xaa-|-His dipeptides. This dipeptidase has specificity for the unusual dipeptide beta-alanyl-L-histidine. PepD binds two co-catalytic zinc ions that activate the catalytic water molecule; Belongs to the family M20 of the metallopeptidase; Localized in the cytoplasm; High confidence in function and specificity. | 0.903 |
| CAZ95294.1 | pepD2 | ZOBELLIA_1238 | ZOBELLIA_3705 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Xaa-His dipeptidase, also known as aminoacyl-histidine dipeptidase, catalyzes the hydrolysis of Xaa-|-His dipeptides. This dipeptidase has specificity for the unusual dipeptide beta-alanyl-L-histidine. Belongs to the family M20 of the metallopeptidase. PepD binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Localized in the cytoplasm; High confidence in function and specificity. | 0.903 |
| CAZ97009.1 | CAZ95294.1 | ZOBELLIA_2862 | ZOBELLIA_1238 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.914 |
| CAZ97009.1 | CAZ98687.1 | ZOBELLIA_2862 | ZOBELLIA_4552 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.913 |
| CAZ97009.1 | aatA-2 | ZOBELLIA_2862 | ZOBELLIA_756 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.804 |
| CAZ97009.1 | aatB | ZOBELLIA_2862 | ZOBELLIA_705 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.804 |
| CAZ97009.1 | ggtA | ZOBELLIA_2862 | ZOBELLIA_4414 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Gamma-glutamyltranspeptidase, family T3; Gamma-glutamyltranspeptidase is a threonine peptidase that catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GgtA plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. This enzyme consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor; Belongs to the family T3 of the peptidases; Putative lipoprotein signal peptide cleaved between the residues 19 an [...] | 0.903 |
| CAZ97009.1 | glyA | ZOBELLIA_2862 | ZOBELLIA_4742 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.824 |
| CAZ97009.1 | metB | ZOBELLIA_2862 | ZOBELLIA_1454 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.805 |
| CAZ97009.1 | metC | ZOBELLIA_2862 | ZOBELLIA_4001 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Cystathionine beta-lyase (CBL) is found in the Selenoamino acids metabolism pathway and in methionine and cysteine biosynthesis pathways. It converts (seleno)cystathionine to (seleno)homocysteine but is also able to catalyze an alpha, gamma elimination; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.805 |
| CAZ97009.1 | pepD1 | ZOBELLIA_2862 | ZOBELLIA_1554 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Xaa-His dipeptidase, also known as aminoacyl-histidine dipeptidase, catalyzes the hydrolysis of Xaa-|-His dipeptides. This dipeptidase has specificity for the unusual dipeptide beta-alanyl-L-histidine. PepD binds two co-catalytic zinc ions that activate the catalytic water molecule; Belongs to the family M20 of the metallopeptidase; Localized in the cytoplasm; High confidence in function and specificity. | 0.903 |
| CAZ97009.1 | pepD2 | ZOBELLIA_2862 | ZOBELLIA_3705 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Localized in the cy [...] | Xaa-His dipeptidase, also known as aminoacyl-histidine dipeptidase, catalyzes the hydrolysis of Xaa-|-His dipeptides. This dipeptidase has specificity for the unusual dipeptide beta-alanyl-L-histidine. Belongs to the family M20 of the metallopeptidase. PepD binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Localized in the cytoplasm; High confidence in function and specificity. | 0.903 |
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