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rpiA rpiA AGA88130.1 AGA88130.1 AGA84939.1 AGA84939.1 AGA84652.1 AGA84652.1 AGA88281.1 AGA88281.1 prs prs AGA86755.1 AGA86755.1 AGA88013.1 AGA88013.1 AGA84940.1 AGA84940.1 metG metG ilvA ilvA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
rpiARibose-5-phosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. (223 aa)    
Predicted Functional Partners:
AGA88130.1
Ribulose-5-phosphate 3-epimerase; PFAM: Ribulose-phosphate 3 epimerase family; TIGRFAM: ribulose-phosphate 3-epimerase; Belongs to the ribulose-phosphate 3-epimerase family.
  
 0.953
AGA84939.1
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
 
 
 0.949
AGA84652.1
Phosphoglucomutase, alpha-D-glucose phosphate-specific; PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; TIGRFAM: phosphoglucomutase, alpha-D-glucose phosphate-specific.
  
 
 0.932
AGA88281.1
Phosphomannomutase; PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.
    
 0.921
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
  
 
 0.920
AGA86755.1
PFAM: Phosphoribosyl transferase domain; TIGRFAM: ribose-phosphate pyrophosphokinase.
  
 
 0.920
AGA88013.1
PFAM: Phosphoribosyl transferase domain; TIGRFAM: ribose-phosphate pyrophosphokinase; Belongs to the ribose-phosphate pyrophosphokinase family.
  
 
 0.920
AGA84940.1
Erythrose-4-phosphate dehydrogenase; Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate.
     
 0.826
metG
Protein containing C-terminal region/beta chain of methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
 
   
 0.630
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
  
 0.623
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
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