STRINGSTRING
galM galM rhgZ rhgZ galE galE galK galK galT galT ganA ganA
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.
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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:
galMAldose 1-epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the aldose epimerase family. (325 aa)
rhgZBeta-galacturonidase; May play a role in the degradation of rhamnogalacturonan derived from plant cell walls; Belongs to the glycosyl hydrolase 42 family. (663 aa)
galEUDP-glucose 4-epimerase; Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity). (339 aa)
galKGalactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). Belongs to the GHMP kinase family. GalK subfamily. (390 aa)
galTGalactose-1-phosphate uridyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (513 aa)
ganAArabinogalactan type I oligomer exo-hydrolase (beta-galactosidase, lactase); Hydrolyzes oligosaccharides released by the endo-1,4-beta- galactosidase GalA from arabinogalactan type I, a pectic plant polysaccharide. It is unable to use lactose as a sole carbon source. Maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o- nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl [...] (687 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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