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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
gloA_1Lactoylglutathione lyase. (121 aa)    
Predicted Functional Partners:
gloA_2
Lactoylglutathione lyase.
 
 
0.925
ACWI_18940
Putative metallo-hydrolase.
     
  0.900
sdhA
L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.800
sdhB
L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.800
trpB_1
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.800
trpA
Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
     
  0.800
trpB_2
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.800
tdcB
L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
     
  0.800
ACWI_20900
Hypothetical protein.
       0.723
ycdT_2
Putative diguanylate cyclase YcdT.
       0.550
Your Current Organism:
Acetobacterium wieringae
NCBI taxonomy Id: 52694
Other names: A. wieringae, ATCC 43740, JCM 2380, LMG 7579, LMG:7579, strain C
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