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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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AGA85108.1Putative nucleoside-diphosphate sugar epimerase; PFAM: Semialdehyde dehydrogenase, NAD binding domain. (213 aa)    
Predicted Functional Partners:
AGA84854.1
Hypothetical protein.
   
 0.977
AGA87770.1
Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
  
 
 0.952
AGA87768.1
PFAM: Cytochrome C1 family.
   
 
 0.947
AGA88542.1
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: Thioesterase domain; Phosphopantetheine attachment site; AMP-binding enzyme.
  
 0.925
AGA87017.1
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein.
   
 
 0.912
AGA88795.1
Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.857
AGA84867.1
Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16).
   
 
 0.832
AGA84868.1
Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16).
   
 
 0.832
AGA87018.1
PFAM: domain; FAD binding domain; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
   
 
 0.831
pcm
protein-L-isoaspartate and D-aspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
   
   0.831
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
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