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
pyrBTIGRFAM: Aspartate carbamoyltransferase, eukaryotic; HAMAP: Aspartate carbamoyltransferase; KEGG: tit:Thit_1339 aspartate carbamoyltransferase; PFAM: Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding; Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. (304 aa)    
Predicted Functional Partners:
pyrC
Dihydroorotase, multifunctional complex type; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate; Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
 0.999
carB
KEGG: thx:Thet_2263 carbamoyl-phosphate synthase large subunit; TIGRFAM: Carbamoyl phosphate synthase, large subunit, glutamine-dependent; PFAM: Carbamoyl phosphate synthetase, large subunit, ATP-binding; Carbamoyl phosphate synthase, large subunit, N-terminal; Carbamoyl phosphate synthetase, large subunit, oligomerisation; MGS-like.
 
 0.999
carA
KEGG: thx:Thet_2264 carbamoyl-phosphate synthase small subunit; TIGRFAM: Carbamoyl phosphate synthase, small subunit; PFAM: Carbamoyl phosphate synthase, small subunit, N-terminal; Glutamine amidotransferase class-I, C-terminal; Belongs to the CarA family.
 
 0.999
pyrR
Bifunctional protein pyrR; Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
 
 0.998
pyrD
Dihydroorotate dehydrogenase family protein; Catalyzes the conversion of dihydroorotate to orotate.
 
  
 0.992
pyrE
Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
 
  
 0.990
pyrF
TIGRFAM: Orotidine 5'-phosphate decarboxylase, subfamily 2, core; HAMAP: Orotidine 5'-phosphate decarboxylase; KEGG: tmt:Tmath_1385 orotidine 5'-phosphate decarboxylase; PFAM: Orotidine 5'-phosphate decarboxylase, core; Belongs to the OMP decarboxylase family. Type 2 subfamily.
  
  
 0.990
AEM79699.1
KEGG: tte:TTE2407 xanthine/uracil permease family protein; TIGRFAM: Xanthine/uracil permease; PFAM: Xanthine/uracil/vitamin C permease.
 
  
 0.964
AEM78354.1
Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. Belongs to the peptidase M38 family.
  
 
 0.951
purA
Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.
 
 
 0.941
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.