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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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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AFE_3010Polyketide synthase, type I, putative; Identified by similarity to GB:AAK26474.1; match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF00698; match to protein family HMM PF02801; match to protein family HMM PF08240; match to protein family HMM PF08659. (2486 aa)    
Predicted Functional Partners:
fabD
Malonyl CoA-acyl carrier protein transacylase; Identified by match to protein family HMM PF00698; match to protein family HMM TIGR00128.
0.998
AFE_3011
8-amino-7-oxononanoate synthase, putative; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202.
 
 0.991
AFE_1502
Ankyrin repeat protein/rhodanese-like domain protein; Identified by match to protein family HMM PF00023; match to protein family HMM PF00581.
  
 0.988
nuoC
NADH-quinone oxidoreductase, C subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family.
   
 0.986
ppiB
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 
 0.978
AFE_0796
3-oxoacyl-(acyl-carrier-protein) synthase, putative; Identified by match to protein family HMM PF00109; match to protein family HMM PF02801; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
0.968
fabF
3-oxoacyl-(acyl-carrier-protein) synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
  
 
 0.963
nuoD
NADH-quinone oxidoreductase, D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
   
 0.960
AFE_2969
Hypothetical protein; Identified by glimmer; putative.
 
 0.952
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
 
 0.950
Your Current Organism:
Acidithiobacillus ferrooxidans
NCBI taxonomy Id: 243159
Other names: A. ferrooxidans ATCC 23270, Acidithiobacillus ferrooxidans ATCC 23270, Acidithiobacillus ferrooxidans str. ATCC 23270
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