STRINGSTRING
STRING protein interaction network
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.
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
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
ALB63259.14-aminobutyrate aminotransferase; Catalyzes the formation of succinate semialdehyde and glutamate from 4-aminobutanoate and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (431 aa)    
Predicted Functional Partners:
gabD
Succinate-semialdehyde dehydrogenase; Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.952
ALB62766.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.943
ALB61809.1
Methylmalonate-semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.936
ALB63260.1
Gamma-glutamyl-gamma-aminobutyrate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.934
patD
Gamma-aminobutyraldehyde dehydrogenase; Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
 
 0.932
ALB64624.1
Gamma-hydroxybutyrate dehydrogenase; Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1- sulfonate (DHPS); Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily.
     
  0.928
fadB
Multifunctional fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
   
 0.925
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
   
 0.925
panD
Aspartate decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
     
 0.916
ALB64445.1
4-aminobutyrate aminotransferase; Catalyzes the formation of succinate semialdehyde and glutamate from 4-aminobutanoate and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
  
  
 
0.903
Your Current Organism:
Cronobacter condimenti
NCBI taxonomy Id: 1073999
Other names: C. condimenti 1330, Cronobacter condimenti 1330, Cronobacter condimenti LMG 26250, Cronobacter sp. 040407/32
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