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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Daci_0615KEGG: pfl:PFL_1656 acyl carrier protein-related protein. (74 aa)    
Predicted Functional Partners:
Daci_1860
PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mpt:Mpe_A3709 NADH dehydrogenase (quinone).
  
 0.981
Daci_4753
TIGRFAM: non-ribosomal peptide synthase; amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; Thioesterase; condensation domain protein; phosphopantetheine-binding; KEGG: bbt:BBta_6813 arthrofactin synthetase/syringopeptin synthetase C-related non-ribosomal peptide synthetase.
  
 
 0.967
Daci_4756
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; KEGG: aav:Aave_3733 amino acid adenylation domain.
  
 
 0.934
Daci_0687
PFAM: ferredoxin; cytochrome P450; Oxidoreductase FAD-binding domain protein; KEGG: reu:Reut_B5278 ferredoxin:cytochrome P450:oxidoreductase FAD/NAD(P)-binding:oxidoreductase FAD-binding region.
  
 0.907
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.
   
 0.901
rplU
Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
  
 
 0.890
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. 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).
   
 0.879
Daci_3890
KEGG: bpd:BURPS668_A0697 hypothetical protein.
   
 0.861
Daci_0614
PFAM: 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III domain protein; 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; KEGG: mfa:Mfla_2642 3-oxoacyl-(acyl-carrier protein) synthase.
  
  
 0.837
nuoD
NADH dehydrogenase I, 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.
   
 0.836
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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