STRINGSTRING
JT27_05930 protein (Alcaligenes faecalis) - STRING interaction network
"JT27_05930" - Aldehyde dehydrogenase in Alcaligenes faecalis
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
JT27_05930Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (475 aa)    
Predicted Functional Partners:
JT27_09530
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 [...] (592 aa)
   
  0.921
JT27_09540
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (137 aa)
     
    0.912
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 (238 aa)
   
 
  0.911
JT27_19210
Acetyl-CoA hydrolase; Derived by automated computational analysis using gene prediction method- Protein Homology (507 aa)
   
 
  0.909
JT27_07705
4-hydroxy-2-oxo-heptane-1,7-dioate aldolase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the HpcH/HpaI aldolase family (268 aa)
   
 
  0.906
JT27_01290
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the HpcH/HpaI aldolase family (254 aa)
   
 
  0.906
JT27_09535
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (127 aa)
     
 
    0.905
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate (329 aa)
   
  0.845
fumC
Fumarate hydratase class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily (465 aa)
     
  0.835
gltA
Citrate 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 citrate [...] (434 aa)
   
 
  0.833
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
Server load: low (8%) [HD]