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
AMG69226.1Cyd operon protein YbgT; Derived by automated computational analysis using gene prediction method: Protein Homology. (35 aa)    
Predicted Functional Partners:
cydA
Cytochrome d terminal oxidase subunit 1; Part of the aerobic respiratory chain; catalyzes the ubiquinol to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.976
AMG69225.1
Cytochrome d ubiquinol oxidase subunit 2; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.975
AMG69839.1
Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.772
AMG69838.1
Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.765
sdhC
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.499
sdhA
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
     
  0.499
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.499
nuoN
NADH:ubiquinone oxidoreductase subunit N; 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 2 family.
     
  0.499
AMG70386.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.499
AMG70387.1
NADH:ubiquinone oxidoreductase subunit L; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.499
Your Current Organism:
Morganella morganii
NCBI taxonomy Id: 582
Other names: ATCC 25830, ATCC 8076H, Bacillus morgani, CCUG 6328, CIP 103763, CIP A231, DSM 30164, IFO 3848, LMG 7874, LMG:7874, M. morganii, NBRC 3848, NCCB 73065, NCIB 235, NCIB:235, NCTC 235, Organism N 1, Proteus morganii, Salmonella morgani
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