STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
alaCGlutamate--pyruvate aminotransferase alac; Involved in the biosynthesis of alanine (412 aa)    
Predicted Functional Partners:
Alanine racemase, catabolic, plp-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA
Alanine racemase, biosynthetic, plp-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis
Valine--pyruvate aminotransferase; Involved in the biosynthesis of alanine
O-succinylhomoserine(thiol)-lyase/o-succinylhomoserine lyase; Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia
Glutamate synthase (nadph) large chain; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate
Pyruvate-ferredoxin/flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway
Broad-specificity exoaminopeptidase; Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue
Transcriptional dna-binding transcriptional activator of sgrs srna; Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions; this repression likely provides one measure of control over sgrR at the level of synthesis. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute- binding domain
Glycine decarboxylase, plp-dependent, subunit p of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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