STRINGSTRING
Daci_5176 Daci_5176 Daci_5168 Daci_5168 nuoI nuoI Daci_5174 Daci_5174 Daci_5436 Daci_5436
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:
Daci_5176TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: aav:Aave_1267 NADH-quinone oxidoreductase, E subunit. (163 aa)
Daci_5168KEGG: ajs:Ajs_0969 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (491 aa)
nuoINADH-quinone oxidoreductase, chain I; 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. (169 aa)
Daci_5174NADH-quinone 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. (707 aa)
Daci_5436PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: aav:Aave_3613 4Fe-4S ferredoxin, iron-sulfur binding domain protein. (87 aa)
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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