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
EDY22401.1Hypothetical protein. (151 aa)    
Predicted Functional Partners:
EDY22402.1
TIGRFAM: NADH-quinone oxidoreductase, F subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: sus:Acid_0113 NADH-quinone oxidoreductase, F subunit.
       0.773
EDY22403.1
PFAM: ferredoxin; molybdopterin oxidoreductase; KEGG: sru:SRU_0400 NADH dehydrogenase I, G subunit.
       0.773
nuoH
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. This subunit may bind ubiquinone.
       0.722
nuoI
4Fe-4S ferredoxin iron-sulfur binding domain protein; 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.
       0.722
EDY22406.1
NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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.
       0.722
nuoK
NADH-ubiquinone oxidoreductase chain 4L; 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 4L family.
       0.722
EDY22408.1
KEGG: noc:Noc_2929 hypothetical protein.
       0.638
EDY22409.1
KEGG: fra:Francci3_0549 NADH dehydrogenase subunit L.
       0.493
EDY22410.1
KEGG: dsy:DSY2580 NADH dehydrogenase I chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
       0.420
EDY22411.1
KEGG: cbe:Cbei_2987 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
       0.420
Your Current Organism:
Chthoniobacter flavus
NCBI taxonomy Id: 497964
Other names: C. flavus Ellin428, Chthoniobacter flavus Ellin428, Chthoniobacter flavus str. Ellin428, Chthoniobacter flavus strain Ellin428, bacterium Ellin428
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