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.
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
cysEcysE: serine O-acetyltransferase. (273 aa)    
Predicted Functional Partners:
cysK
cysK: cysteine synthase A; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 0.992
cysM
cysM: cysteine synthase B.
 
 0.986
cysE_1
Bacterial transferase hexapeptide family protein.
 
  
 
0.983
cysS
cysS: cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.917
sdaB_1
Sda_mono: L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
 0.912
sdaA
Sda_mono: L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
 0.912
thrA
Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family.
    
 0.855
metL
Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family.
    
 0.855
serB
serB: phosphoserine phosphatase SerB.
  
 
 0.830
ilvA
Threonine ammonia-lyase, biosynthetic; 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.
  
  
 0.830
Your Current Organism:
Proteus vulgaris
NCBI taxonomy Id: 585
Other names: ATCC 29905, CCUG 35382, CCUG 39507, CDC PR1, CIP 104989, DSM 13387, LMG 16708, LMG:16708, NCTC 13145, P. vulgaris, strain PR 1
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