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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AMS42329.1Citrate lyase; Pfam:pfam03328 HpcH/HpaI aldolase/citrate lyase family; Belongs to the HpcH/HpaI aldolase family. (293 aa)    
Predicted Functional Partners:
AMS42330.1
MaoC family dehydratase; Pfam:pfam01575 MaoC like domain.
 
  
 0.968
AMS39823.1
ATP-binding protein; Pfam:pfam03328 HpcH/HpaI aldolase/citrate lyase family; Belongs to the HpcH/HpaI aldolase family.
  
  
 
0.919
AMS39379.1
Class II aldolase/adducin family protein; Pfam:pfam00596 Class II Aldolase and Adducin N-terminal domain.
   
  
 0.802
AMS42331.1
Pfam:pfam10098 Uncharacterized protein conserved in bacteria (DUF2336).
       0.610
AMS39941.1
Succinate dehydrogenase; Pfam:pfam00890 FAD binding domain; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
  
 0.537
AMS39762.1
Pfam:pfam01642 Methylmalonyl-CoA mutase.
  
  
 0.503
AMS40219.1
Carnitine dehydratase; Pfam:pfam02515 CoA-transferase family III; Belongs to the CoA-transferase III family.
 
  
 0.483
AMS39462.1
Malic enzyme; Pfam:pfam01515 Phosphate acetyl/butaryl transferase.
  
  
 0.442
AMS42802.1
Malic enzyme; Pfam:pfam01515 Phosphate acetyl/butaryl transferase.
  
  
 0.442
nnrD
Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
      
 0.415
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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