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rutF rutF rutA rutA rutB rutB rutD rutD rutE rutE ABP62447.1 ABP62447.1 deoA deoA deoD deoD ppnP ppnP upp upp ABP62617.1 ABP62617.1
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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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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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rutFFlavin reductase domain protein, FMN-binding protein; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway; Belongs to the non-flavoprotein flavin reductase family. RutF subfamily. (164 aa)    
Predicted Functional Partners:
rutA
Luciferase family protein; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate.
 
 
 0.993
rutB
Isochorismatase hydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily.
 
 
 0.991
rutD
Alpha/beta hydrolase fold protein; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family.
 
  
 0.933
rutE
Nitroreductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted.
  
  
 0.915
ABP62447.1
N-isopropylammelide isopropylaminohydrolase; PFAM: amidohydrolase; Amidohydrolase 3; KEGG: ecj:JW0328 cytosine deaminase.
  
  
  0.912
deoA
Thymidine phosphorylase; The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.
    
  0.900
deoD
TIGRFAM: purine nucleoside phosphorylase; PFAM: purine or other phosphorylase, family 1; KEGG: spt:SPA4384 purine nucleoside phosphorylase.
     
  0.900
ppnP
Protein of unknown function DUF1255; Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
     
  0.900
upp
Uracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate.
     
  0.900
ABP62617.1
Uridine phosphorylase; Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Belongs to the PNP/UDP phosphorylase family.
     
  0.900
Your Current Organism:
Enterobacter sp. 638
NCBI taxonomy Id: 399742
Other names: E. sp. 638
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