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
hoxFProbable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity. (602 aa)    
Predicted Functional Partners:
nuoG
Putative NADH-ubiquinone oxidoreductase chain G; 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. Belongs to the complex I 75 kDa subunit family.
 
 0.999
hoxU
Probable hydrogen dehydrogenase, gamma subunit. Homology to hoxU of A. eutrophus of 40% (pir|B35385(PIR). Binds 3 4Fe-4S clusters per subunit (Potential). Pfam: 2Fe-2S iron-sulfur cluster binding domain no signal peptide no TMHs; High confidence in function and specificity.
 
 0.999
napG
Probable ferredoxin-type protein napG. Homology to napG of E. coli of 57% (sprot|NAPG_ECOLI). Involved in electron transfer in a wide variety of metabolic reactions. InterPro: MauM/NapG family ferredoxin-type protein (IPR004494); 7 Fe ferredoxin (IPR000813); 4Fe-4S ferredoxin; iron-sulfur binding domain (IPR001450) Pfam: 4Fe-4S binding domain Tigrfam: mauM_napG: MauM/NapG family ferredoxin-type protein no signal peptide no TMHs; High confidence in function and specificity.
  
 0.999
azo0211
Conserved hypothetical protein.
  
 0.998
azo0495
Putative NADH dehydrogenase; 33%; Specificity unclear.
   
 0.998
nuoB1
Conserved hypothetical NADH-quinone oxidoreductase chain B; 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).
  
 0.998
nuoA
Putative NADH-ubiquinone oxidoreductase chain A; 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 subunit 3 family.
  
 0.998
nuoB2
Putative NADH-ubiquinone oxidoreductase chain B; 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).
  
 0.998
nuoC
Respiratory-chain NADH dehydrogenase, chain C probable; 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.
  
 0.998
nuoD
Putative NADH-ubiquinone oxidoreductase chain 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; Belongs to the complex I 49 kDa subunit family.
  
 0.998
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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