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AFA_04870 protein (Alcaligenes faecalis) - STRING interaction network
"AFA_04870" - Succinate dehydrogenase assembly factor 2 in Alcaligenes faecalis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
AFA_04870Succinate dehydrogenase assembly factor 2; Derived by automated computational analysis using gene prediction method- Protein Homology (86 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)
   
 
  0.906
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)
   
 
  0.897
JT27_09540
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (137 aa)
 
   
  0.872
JT27_09535
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (127 aa)
 
        0.850
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)
   
        0.823
JT27_16045
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (177 aa)
   
          0.746
JT27_06530
Membrane protein; Derived by automated computational analysis using gene prediction method- Protein Homology (74 aa)
   
          0.683
JT27_13990
Thiol-disulfide isomerase; Derived by automated computational analysis using gene prediction method- Protein Homology (129 aa)
   
        0.648
JT27_16575
Glycosyltransferase; Derived by automated computational analysis using gene prediction method- Protein Homology (586 aa)
   
          0.639
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs (138 aa)
     
        0.616
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
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