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
Databases
Textmining
[Homology]
Score
AIA73486.1Succinate-semialdehyde dehydrogenase; In Escherichia coli this enzyme appears to be an NAD+/NADP+-dependent succinate semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (460 aa)    
Predicted Functional Partners:
sdhA
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
   
 0.924
AIA73976.1
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.
  
 0.914
AIA74109.1
4-aminobutyrate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
 
 0.914
AIA75086.1
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.
  
 0.914
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.909
AIA75389.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.904
AIA75390.1
Succinate dehydrogenase; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
   
 
 0.903
AIA76435.1
Protein CsiD; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.903
pckA
Hypothetical protein; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
  
 
 0.866
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
  
 0.852
Your Current Organism:
Halomonas campaniensis
NCBI taxonomy Id: 213554
Other names: ATCC BAA-966, DSM 15293, H. campaniensis, Halomonas campaniae, Halomonas campaniensis Romano et al. 2005, Halomonas campisalis subsp. campaniae, strain 5AG
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