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:
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Gene Fusion
Cooccurrence
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[Homology]
Score
yitUPutative phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro. (270 aa)    
Predicted Functional Partners:
ribD
Fused diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
    
 0.979
ribE
Riboflavin synthase (alpha subunit); Catalyzes the dismutation of two molecules of 6,7-dimethyl-8- ribityllumazine, resulting in the formation of riboflavin and 5-amino- 6-(D-ribitylamino)uracil.
     
 0.968
ycsE
Putative phosphatase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro. To a lesser extent, may also catalyze the dephosphorylation of a broad range of substrates such as phosphorylated sugars and triphosphate nucleotides in vitro.
 
 
0.952
ywtE
Putative hydrolase; Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro. Also catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro.
 
 
0.951
ribH
6,7-dimethyl-8-ribityllumazine synthase, beta subunit; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4- dihydroxy-2-butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4-dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates.
     
 0.944
yizC
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
     
 0.885
yutF
Putative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family.
   
  
 0.756
ribC
Bifunctional riboflavin kinase FAD synthase; Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
  
 
 0.755
ribAB
Fused GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the N-terminal section; belongs to the DHBP synthase family.
     
 0.717
yitV
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
    0.612
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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