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
rbsKRibokinase; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. (306 aa)    
Predicted Functional Partners:
deoC
Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
   
 0.984
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.
  
 0.933
AEX85228.1
PFAM: Transketolase, thiamine diphosphate binding domain; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
  
 0.927
AEX86323.1
PFAM: Ribose/Galactose Isomerase; TIGRFAM: ribose 5-phosphate isomerase B; sugar-phosphate isomerases, RpiB/LacA/LacB family.
  
 
 0.922
AEX84537.1
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.
  
 
 0.908
AEX85017.1
Phosphomannomutase; PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.
  
 
 0.908
AEX85787.1
PFAM: Inosine-uridine preferring nucleoside hydrolase.
  
 0.889
pdxS
Pyridoxal 5''-phosphate synthase, synthase subunit Pdx1; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
     
 0.818
pdxT
Pyridoxal 5''-phosphate synthase, glutaminase subunit Pdx2; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
     
 0.817
AEX85114.1
Hypothetical protein.
       0.773
Your Current Organism:
Marinitoga piezophila
NCBI taxonomy Id: 443254
Other names: M. piezophila KA3, Marinitoga piezophila KA3, Marinitoga piezophila str. KA3, Marinitoga piezophila strain KA3, Thermotogales sp. KA3
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