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
aroKShikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. (170 aa)    
Predicted Functional Partners:
Afer_1717
PFAM: 3-dehydroquinate synthase; KEGG: saq:Sare_1253 3-dehydroquinate synthase.
  
 0.998
aroE
Shikimate 5-dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
 
 0.997
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
 
 
 0.955
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.
 
  
 0.924
Afer_1157
PFAM: Prephenate dehydrogenase; KEGG: krh:KRH_15220 prephenate dehydrogenase.
 
  
 0.716
Afer_1988
PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: ace:Acel_1078 glutamate synthase (NADH) large subunit.
       0.678
rpoZ
DNA-directed RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
  
  
 0.578
topA
DNA topoisomerase I; 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 supe [...]
  
  
 0.573
Afer_0224
Diguanylate cyclase; KEGG: xca:xccb100_3008 putative sensor protein; TIGRFAM: diguanylate cyclase; PFAM: GGDEF domain containing protein; SMART: GGDEF domain containing protein.
       0.570
pheT
KEGG: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit.
     
 0.552
Your Current Organism:
Acidimicrobium ferrooxidans
NCBI taxonomy Id: 525909
Other names: A. ferrooxidans DSM 10331, Acidimicrobium ferrooxidans DSM 10331, Acidimicrobium ferrooxidans ICP, Acidimicrobium ferrooxidans str. DSM 10331, Acidimicrobium ferrooxidans strain DSM 10331
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.