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
thiDSimilar to Escherichia coli phosphomethylpyrimidine kinase ThiD or B2103 SW:THID_ECOLI (P76422) (266 aa) fasta scores: E(): 5.5e-30, 44.9% id in 265 aa. (272 aa)    
Predicted Functional Partners:
thiE
Putative thiamin-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.
 
 0.999
thiC
Thiamine biosynthesis protein; 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. Belongs to the ThiC family.
  
 
 0.996
thiG
Thiazole biosynthesis protein; 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.
 
  
 0.975
DIP0032
Conserved hypothetical protein; Similar to Streptomyces coelicolor hypothetical 6.6 kDa protein SC6E10.02 TR:Q9S2N5 (EMBL:AL109661) (66 aa) fasta scores: E(): 1.1e-06, 36.36% id in 66 aa.
  
    0.943
DIP0034
Similar to Escherichia coli adenylyltransferase ThiF or B3992 SW:THIF_ECOLI (P30138) (251 aa) fasta scores: E(): 1.1e-21, 35.86% id in 237 aa.
 
  
 0.926
thiO
Similar to Rhizobium etli putative thiamine biosynthesis oxidoreductase ThiO SW:THIO_RHIET (O34292) (327 aa) fasta scores: E(): 5.4e-09, 31.67% id in 341 aa.
  
  
 0.892
thiL
Thiamine-monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
    
 0.819
DIP0492
Putative molybdopterin biosynthesis protein; Similar to Synechococcus sp MTP-synthase sulfurylase MoeB TR:O54307 (EMBL:Y16560) (391 aa) fasta scores: E(): 1.1e-37, 39.56% id in 369 aa.
 
  
 0.686
cas9
Conserved hypothetical protein; CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans- encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. [...]
      
 0.617
pknB
Similar to Mycobacterium leprae probable serine/threonine-protein kinase PknB or ML0016 SW:PKNB_MYCLE (P54744) (622 aa) fasta scores: E(): 5.7e-58, 43.26% id in 661 aa.
     
 0.596
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.