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
RSP_3675Esterase/lipase/thioesterase; IMG reference gene:2512957209; PFAM: alpha/beta hydrolase fold. (305 aa)    
Predicted Functional Partners:
RSP_3676
Transcriptional regulator, GntR family; IMG reference gene:2512957210; PFAM: Bacterial regulatory proteins, gntR family; FCD domain.
    0.966
RSP_3674
Carbohydrate ABC transporter substrate-binding protein, CUT1 family; IMG reference gene:2512957208; PFAM: Bacterial extracellular solute-binding protein.
 
     0.874
mtnP
Methylthioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates; Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
 
    0.859
nuoCD
NADH dehydrogenase subunit C; 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 N-terminal section; belongs to the complex I 30 kDa subunit family.
   
   0.853
RSP_3670
Putative oxidoreductase myo-inositol 2-dehydrogenase; IMG reference gene:2512957204; PFAM: Oxidoreductase family, NAD-binding Rossmann fold.
 
  
 0.812
RSP_3671
D-tagatose 3-epimerase; IMG reference gene:2512957205; PFAM: Xylose isomerase-like TIM barrel.
 
     0.790
RSP_3673
Carbohydrate ABC transporter membrane protein 1, CUT1 family; IMG reference gene:2512957207; PFAM: Binding-protein-dependent transport system inner membrane component.
 
     0.672
RSP_3672
Carbohydrate ABC transporter membrane protein 2, CUT1 family; IMG reference gene:2512957206; PFAM: Binding-protein-dependent transport system inner membrane component.
 
     0.664
fbcF
Ubiquinol-cytochrome C reductase, iron-sulfur protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
   
   0.655
nuoG1
NADH dehydrogenase gamma subunit; IMG reference gene:2512955096; PFAM: 2Fe-2S iron-sulfur cluster binding domain; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; Molybdopterin oxidoreductase Fe4S4 domain; TIGRFAM: NADH-quinone oxidoreductase, chain G.
   
 
 0.631
Your Current Organism:
Rhodobacter sphaeroides 241
NCBI taxonomy Id: 272943
Other names: R. sphaeroides 2.4.1, Rhodobacter sphaeroides 2.4.1, Rhodobacter sphaeroides ATCC 17023, Rhodobacter sphaeroides ATH 2.4.1, Rhodobacter sphaeroides str. 2.4.1, Rhodobacter sphaeroides strain 2.4.1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.