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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Score
rutCPyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. (129 aa)    
Predicted Functional Partners:
rutB
Pyrimidine utilization protein B; 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.
 
 
  0.992
rutD
Pyrimidine utilization protein D; 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.
 
 
  0.989
Cseg_1790
PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase.
 
 
  0.918
rutA
Pyrimidine utilization protein A; 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.
 
    0.894
Cseg_2077
PFAM: Tetracycline transcriptional regulator YcdC domain protein; regulatory protein TetR; KEGG: ccs:CCNA_02884 transcriptional regulator, TetR family.
 
     0.648
Cseg_4124
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 
 0.485
Cseg_1789
PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase.
 
    0.473
Cseg_1893
PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase.
 
    0.473
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
   
  0.455
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
 
 0.448
Your Current Organism:
Caulobacter segnis
NCBI taxonomy Id: 509190
Other names: C. segnis ATCC 21756, Caulobacter segnis ATCC 21756, Caulobacter segnis DSM 7131, Caulobacter segnis IFO 13240, Caulobacter segnis str. ATCC 21756, Caulobacter segnis strain ATCC 21756
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