STRINGSTRING
rhgW rhgW rhgX rhgX yesY yesY pel pel pelC pelC yxiM yxiM
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
rhgWRhamnogalacturonan endolyase; Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin ; Belongs to the polysaccharide lyase 11 family. (620 aa)
rhgXRhamnogalacturonan exolyase YesX; Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin ; Belongs to the polysaccharide lyase 11 family. (612 aa)
yesYRhamnogalacturonan acetylesterase; May play a role in the degradation of rhamnogalacturonan derived from plant cell walls. Probably has broad substrate specificity and may degrade several types of acetylated substrates. Belongs to the 'GDSL' lipolytic enzyme family. (217 aa)
pelPectate lyase; Produces unsaturated products from polygalacturonate. (420 aa)
pelCSecreted pectate lyase; Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is also able to cleave trigalacturonate to galacturonic acid and unsaturated digalacturonate. Belongs to the polysaccharide lyase 3 family. (221 aa)
yxiMPutative esterase (lipoprotein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the 'GDSL' lipolytic enzyme family. (382 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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