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:
a 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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
Plim_0871PFAM: alpha/beta hydrolase fold; KEGG: reh:H16_A3666 lysophospholipase. (290 aa)    
Predicted Functional Partners:
Plim_3862
NADH-quinone oxidoreductase, F subunit.
   
 
 0.855
Plim_3860
NADH dehydrogenase (ubiquinone) 24 kDa subunit.
   
   0.830
Plim_3863
Ferredoxin.
   
 
 0.798
Plim_1442
PFAM: NAD-dependent epimerase/dehydratase; NmrA family protein; KEGG: sus:Acid_7528 NAD-dependent epimerase/dehydratase.
  
   0.727
nuoD
NADH dehydrogenase (quinone); 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.
   
   0.700
nuoD-2
NADH dehydrogenase (quinone); 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.
   
   0.700
Plim_0462
TIGRFAM: polyketide-type polyunsaturated fatty acid synthase PfaA; PFAM: Beta-ketoacyl synthase; KR domain protein; Acyl transferase; short-chain dehydrogenase/reductase SDR; KEGG: gur:Gura_2012 erythronolide synthase.
   
 
 0.697
nuoB
NADH-quinone oxidoreductase, B 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.
   
   0.658
nuoB-2
NADH-quinone oxidoreductase, B 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.
   
   0.658
nuoC
NADH (or F420H2) dehydrogenase, subunit C; 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.
   
   0.657
Your Current Organism:
Planctopirus limnophila
NCBI taxonomy Id: 521674
Other names: P. limnophila DSM 3776, Planctomyces limnophilus ATCC 43296, Planctomyces limnophilus DSM 3776, Planctomyces limnophilus str. DSM 3776, Planctomyces limnophilus strain DSM 3776, Planctopirus limnophila DSM 3776, Planctopirus limnophilus DSM 3776
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