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
gabDNAD-dependent succinate-semialdehyde dehydrogenase; Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method: Protein Homology. (486 aa)    
Predicted Functional Partners:
AQS83658.1
4-aminobutyrate--2-oxoglutarate transaminase; 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.
 
 0.925
AQS85606.1
Succinate dehydrogenase flavoprotein subunit; Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-depe [...]
   
 0.923
AQS83510.1
Succinate-semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.915
AQS84374.1
Succinate-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.
  
  
 
0.914
AQS85607.1
Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
   
 
 0.910
AQS85604.1
Succinate dehydrogenase, cytochrome b556 subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.904
AQS84889.1
acetyl-CoA hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.903
AQS85605.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.901
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
      0.899
gltA
Citrate (Si)-synthase; 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 cit [...]
  
 0.846
Your Current Organism:
Acetobacter aceti
NCBI taxonomy Id: 435
Other names: A. aceti, ATCC 15973, Acetimonas aceti, Acetobacter (subgen. Acetobacter) aceti, Acetobacter aceti aceti, Acetobacter aceti orleanensis, Acetobacter aceti subsp. aceti, Acetobacter aceti var. muciparum, Acetobacter ketogenum, Acetobacter lafarianum, Bacillus aceticus, Bacteriopsis aceti, Bacterium aceti, Bacterium acetigenoidum, Bacterium hansenianum, CCUG 18122, CIP 103111, DSM 3508, ICMP 8807, IFO 14818, JCM 7641, Micrococcus aceti, Mycoderma aceti souches non visqueuses (membraneuses), NBRC 14818, NCCB 23001, NCIB 8621, NCIB:8621, NCIMB 8621
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.