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
ALV30217.1Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. (75 aa)    
Predicted Functional Partners:
nuoI
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.
  
  
 0.633
queA
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
       0.625
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
       0.621
ALV29900.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.549
nuoD
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; Belongs to the complex I 49 kDa subunit family.
  
  
 0.534
ALV28813.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 
 0.509
ALV30218.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 
 0.429
Your Current Organism:
Pannonibacter phragmitetus
NCBI taxonomy Id: 121719
Other names: Achromobacter group B, Achromobacter group E, Achromobacter sp. LMG 5410, Achromobacter sp. LMG 5411, Achromobacter sp. LMG 5430, Achromobacter sp. LMG 5431, DSM 14782, LMG 22736, LMG:22736, NCAIM B02025, NCTC 13350, P. phragmitetus, Pannonibacter phragmitetus Borsodi et al. 2003, alpha proteobacterium C6-19, alpha proteobacterium C6/17, alpha proteobacterium C6/8, strain C6/19
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