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
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Cooccurrence
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Experiments
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[Homology]
Score
Lcho_2751PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mpt:Mpe_A3709 NADH dehydrogenase (quinone). (523 aa)    
Predicted Functional Partners:
Lcho_2752
PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: mpt:Mpe_A3708 NAD-dependent formate dehydrogenase gamma subunit.
 0.999
Lcho_2750
TIGRFAM: formate dehydrogenase, alpha subunit; PFAM: ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; molybdopterin oxidoreductase; molydopterin dinucleotide-binding region; molybdopterin oxidoreductase Fe4S4 region; KEGG: mpt:Mpe_A3710 NAD-dependent formate dehydrogenase alpha subunit.
 
 0.998
Lcho_2749
Hypothetical protein; KEGG: mca:MCA1389 formate dehydrogenase, delta subunit.
 
 
 0.995
Lcho_1505
KEGG: ajs:Ajs_0961 NADH-quinone oxidoreductase, E subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit.
 0.990
Lcho_1461
PFAM: ferredoxin; KEGG: rfr:Rfer_3857 hydrogen dehydrogenase.
 
 0.974
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).
  
 0.962
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.
  
 0.962
Lcho_1507
NADH-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.
 
 0.959
Lcho_1513
KEGG: mpt:Mpe_A1415 NADH dehydrogenase (quinone); TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 0.951
Lcho_1510
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.
  
 
 0.949
Your Current Organism:
Leptothrix cholodnii
NCBI taxonomy Id: 395495
Other names: L. cholodnii SP-6, Leptothrix cholodnii SP-6, Leptothrix cholodnii str. SP-6, Leptothrix cholodnii strain SP-6
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