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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
DR97_5245Molybdopterin oxidoreductase fe4s4 domain protein; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family (769 aa)    
Predicted Functional Partners:
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
 0.999
fdhE
Formate dehydrogenase accessory protein fdhe; Necessary for formate dehydrogenase activity
  
 
 0.993
fdnI
formate-DH-gamm: formate dehydrogenase, gamma subunit
  
 0.992
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
  
 
 0.950
fdnG
Formate dehydrogenase-o major subunit; formate-DH-alph: formate dehydrogenase, alpha subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family
 
 0.882
napF
Ferredoxin-type protein napf; Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm
  
  
 0.877
DR97_5244
Putative ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions
 
  
 0.863
ModR
Molybdenum transport regulator; modE_repress: ModE molybdate transport repressor domain protein
     
 0.835
nuoE
Nadh-quinone oxidoreductase subunit e; 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 (By similarity)
  
 0.832
nuoF
Nadh oxidoreductase (quinone), f 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 (By similarity)
  
 0.831
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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