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.
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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
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[Homology]
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ADU49667.1KEGG: cai:Caci_5918 hypothetical protein; SPTR: Putative uncharacterized protein. (87 aa)    
Predicted Functional Partners:
nuoD
NADH dehydrogenase subunit 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 a menaquinone. 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.
  
 0.964
nuoD-2
NADH dehydrogenase subunit 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 a menaquinone. 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.
  
 0.964
nuoB
NADH dehydrogenase subunit B; 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 a menaquinone. 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.
  
 0.962
nuoB-2
NADH dehydrogenase subunit B; 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 a menaquinone. 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.
  
 0.962
ADU49668.1
FAD dependent oxidoreductase; COGs: COG0665 Glycine/D-amino acid oxidase (deaminating); InterPro IPR000759: IPR006076; KEGG: sco:SCO6289 secreted oxidoreductase; PFAM: FAD dependent oxidoreductase; SPTR: Secreted oxidoreductase; PFAM: FAD dependent oxidoreductase.
 
    0.960
ADU49666.1
FAD-dependent pyridine nucleotide-disulfide oxidoreductase; COGs: COG0446 NAD(FAD)-dependent dehydrogenase; InterPro IPR013027: IPR017224: IPR007419; KEGG: sco:SCO6291 secreted oxidase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; BFD domain protein [2Fe-2S]-binding domain protein; SPTR: Putative secreted oxidase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; BFD-like [2Fe-2S] binding domain.
 
   
 0.959
nuoC
NADH 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 a menaquinone. 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.
  
 0.957
ADU47256.1
COGs: COG0852 NADH:ubiquinone oxidoreductase 27 kD subunit; InterPro IPR001268; KEGG: tcu:Tcur_4386 NADH (or F420H2) dehydrogenase, subunit C; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: Putative NADH dehydrogenase; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit.
  
 0.957
ADU47235.1
NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
  
 0.956
ADU48709.1
Formate dehydrogenase beta subunit; COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterPro IPR001949: IPR011538: IPR019554: IPR019575; KEGG: msm:MSMEG_0160 formate dehydrogenase, beta subunit; PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; PRIAM: NADH dehydrogenase (quinone); SPTR: NADH oxidoreductase (Quinone), F subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; Respiratory-chain NADH dehydrogenase 51 Kd subunit; SLBB [...]
  
 0.956
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
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