STRINGSTRING
proB proB araB araB proA proA hisB hisB fucK fucK metC metC xylB xylB lyxK lyxK ilvE ilvE serB serB
Nodes:
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:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
proBGamma-glutamate kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (367 aa)
araBL-ribulokinase; Protein involved in carbohydrate catabolic process; Belongs to the ribulokinase family. (566 aa)
proAGamma-glutamylphosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (417 aa)
hisBImidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase; Protein involved in histidine biosynthetic process. (355 aa)
fucKL-fuculokinase; Catalyzes the phosphorylation of L-fuculose. Can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D- fructose. (472 aa)
metCCystathionine beta-lyase, PLP-dependent; Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine. In addition, under certain growth conditions, exhibits significant alanine racemase coactivity. (395 aa)
xylBXylulokinase; Catalyzes the phosphorylation of D-xylulose to D-xylulose 5- phosphate. Also catalyzes the phosphorylation of 1- deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. Can also use D-ribulose, xylitol and D- arabitol, but D-xylulose is preferred over the other substrates. Has a weak substrate-independent Mg-ATP-hydrolyzing activity ; Belongs to the FGGY kinase family. (484 aa)
lyxKL-xylulose kinase; Catalyzes the phosphorylation of L-xylulose and 3-keto-L- gulonate. Is involved in L-lyxose utilization via xylulose, and may also be involved in the utilization of 2,3-diketo-L-gulonate. (498 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. (309 aa)
serB3-phosphoserine phosphatase; Catalyzes the dephosphorylation of phosphoserine (P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr). Belongs to the HAD-like hydrolase superfamily. SerB family. (322 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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