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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rutBEnzyme of alternative pyrimidine degradation pathway; 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. (248 aa)    
Predicted Functional Partners:
rutA
Putative luciferase family protein, putative flavin-dependent oxidoreductase; 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.
 
 
 0.995
rutD
Putative enzyme of alternative pyrimidine degradation pathway, putative alpha/beta hydrolase; 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.
 
 0.993
rutC
Enzyme of alternative pyrimidine degradation pathway; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation.
 
 
 0.993
rutF
Flavin reductase domain protein, FMN-binding; 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.
 
 
 0.986
rutF-2
flavin:NADH oxidoreductase, putative alternative pyrimidine degradation enzyme; 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.
 
 
 0.956
ACS41746.1
glutamyl-tRNA(Gln) amidotransferase (subunit A); Function of strongly homologous gene; enzyme.
     0.921
ACS39514.1
Putative transcriptional regulator, TetR/AcrR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.
 
     0.592
ACS40697.1
Conserved hypothetical protein; Homologs of previously reported genes of unknown function.
  
  
 0.537
nnrE
Putative carbohydrate kinase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of [...]
   
    0.532
nadE
NAD(+) synthase (glutamine-hydrolyzing) with a nitrilase-like domain; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
  
 
 0.419
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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