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
cyoEProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (294 aa)    
Predicted Functional Partners:
AMG70968.1
Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
cyoC
Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.999
cyoD
Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.999
AMG70967.1
Cytochrome ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
   
 
 0.929
AMG69434.1
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.684
AMG70972.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.626
nuoC
NADH:ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
  
 0.545
nuoK
NADH:ubiquinone oxidoreductase subunit K; 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.
   
  
 0.529
nuoB
NADH dehydrogenase; 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.
   
  
 0.529
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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