STRINGSTRING
UMN179_01700 protein (Gallibacterium anatis) - STRING interaction network
"UMN179_01700" - Cystathionine beta-lyase in Gallibacterium anatis
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:
some 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 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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
UMN179_01700Cystathionine beta-lyase (397 aa)    
Predicted Functional Partners:
UMN179_00504
Cystathionine gamma-synthase (371 aa)
   
 
0.985
UMN179_01888
Bifunctional aspartokinase I/homoserine dehydrogenase I (815 aa)
   
  0.960
UMN179_00850
Bifunctional aspartate kinase II/homoserine dehydrogenase II (808 aa)
   
  0.960
UMN179_00519
Cysteine synthase A (316 aa)
  0.921
metE
S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation (757 aa)
   
 
  0.895
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate (314 aa)
   
 
  0.866
UMN179_00139
Methylenetetrahydrofolate reductase (296 aa)
   
  0.856
UMN179_01496
O-acetylhomoserine aminocarboxypropyltransferase (422 aa)
 
 
0.849
UMN179_02453
Methyltransferase (381 aa)
   
 
  0.847
ilvA
Threonine dehydratase; 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 (516 aa)
 
 
  0.831
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
Server load: low (10%) [HD]