STRINGSTRING
STRING protein interaction network
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 to 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
hcnA2Fe-2S iron-sulfur cluster binding domain protein; A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain (104 aa)    
Predicted Functional Partners:
hcnC
Fad dependent oxidoreductase family protein; A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain
 
  
 0.997
hcnB
Pyridine nucleotide-disulfide oxidoreductase family protein; A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain
 
  
 0.989
fdxH
Nitrate-inducible formate dehydrogenase beta subunit; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers
  
 0.958
nuoD
Bifunctional nadh:ubiquinone oxidoreductase subunit c/d; 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
  
 
 0.862
rhlA
Alpha/beta hydrolase fold family protein; Required for rhamnolipid surfactant production . Supplies the acyl moieties for rhamnolipid biosynthesis by competing with the enzymes of the type II fatty acid synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein (ACP) pathway intermediates. Catalyzes the formation of one molecule of beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta- hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid component of rhamnolipid. In vitro results establish that RhlA is highly selective for 10-carbon acyl-ACP [...]
      
 0.846
fdnI
formate-DH-gamm: formate dehydrogenase, gamma subunit
  
 0.809
DR97_672
annotation not available
 
   
 0.798
anr
Crp/fnr family transcriptional regulator, anaerobic regulatory protein; Transcriptional activator of anaerobic gene expression
      
 0.754
DR97_669
annotation not available
 
   
 0.701
NasA
Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily
  
 0.682
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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