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
AMK54487.1Pyruvate:ferredoxin (flavodoxin) oxidoreductase; 'Pfam: Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; SMART: Domain of unknown function; Pfam: Pyruvate ferredoxin/flavodoxin oxidoreductase; Pfam: Domain of unknown function; TIGRFAM: pyruv_ox_red: pyruvate:ferredoxin (flavodoxin) oxidoreductase; Pfam: 4Fe-4S dicluster domain'. (1185 aa)    
Predicted Functional Partners:
AMK54559.1
Hypothetical protein; 'Pfam: 4Fe-4S dicluster domain; TIGRFAM: FeFe_hydrog_B1: (FeFe) hydrogenase, group B1/B3; Pfam: Iron only hydrogenase large subunit, C-terminal domain'.
  
 
 0.997
ldh
L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family.
  
 0.993
ldh-2
L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate.
  
 0.993
topA
DNA topoisomerase; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA superc [...]
  
   0.989
AMK54708.1
Hypothetical protein; PRINTS: DnaJ domain signature; Pfam: DnaJ domain; SMART: DnaJ molecular chaperone homology domain; Pfam: DnaJ C terminal domain.
  
 
 0.987
AMK55771.1
Hypothetical protein.
  
 
 0.987
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
 
 0.987
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
   
 
 0.985
AMK55477.1
Hypothetical protein; Pfam: Phosphopantetheine attachment site.
  
 0.984
AMK53887.1
'TIGRFAM: pyruv_kin: pyruvate kinase; Pfam: Pyruvate kinase, barrel domain; Pfam: Pyruvate kinase, alpha/beta domain; PRINTS: Pyruvate kinase family signature'; Belongs to the pyruvate kinase family.
  
 0.975
Your Current Organism:
Faecalibaculum rodentium
NCBI taxonomy Id: 1702221
Other names: Allobaculum sp. Alo17, Erysipelotrichaceae bacterium Alo17, F. rodentium, Faecalibaculum rodentium Chang et al. 2016 emend. Cox et al. 2017, JCM 30274, KCTC 15484, strain ALO17
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