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
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Cooccurrence
Coexpression
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[Homology]
Score
thiCThiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 aa)    
Predicted Functional Partners:
thiG
Thiazole synthase; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
 
  
 0.992
thiD
Catalyzes the formation hydroxymethylpyrimidine phosphate from hydroxymethylpyrimidine and the formation of of 4-amino-2-methyl-5-diphosphomethylpyrimidine from hydroxymethylpyrimidine phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.989
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family.
  
 0.986
thiH
In Escherichia coli this enzyme functions in thiamine biosynthesis along with thiFSGI and iscS; with ThiFSG catalyzes the formation of thiazole phosphate from tyrosine, cysteine and 1-deoxy-D-xylulose-5-phosphate; forms a complex with ThiG; contains an iron-sulfur center; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.985
thiF
Molybdopterin biosynthesis protein MoeB; ATP-dependent adenylate transferase, transfers adenyl moiety to the MoeD subunit of molybdopterin synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.965
thiS
Thiamine biosynthesis protein ThiS; With ThiF, ThiG, and ThiO catalyzes the formation of the thiazole moiety of thiamine pyrophosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.964
purM
Phosphoribosylaminoimidazole synthetase; Catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.818
purK
Phosphoribosylaminoimidazole carboxylase; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
     
  0.800
moeB
Molybdopterin-synthase adenylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.741
thiM
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family.
  
  
 0.688
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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