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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
pyrBAspartate carbamoyltransferase catalytic subunit; Catalyzes the transfer of the carbamoyl moiety from carbamoyl phosphate to L- aspartate in pyrimidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. (343 aa)    
Predicted Functional Partners:
pyrC_2
Dihydroorotase; Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
carA
Carbamoyl-phosphate synthase small subunit; Catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
carB
Carbamoyl phosphate synthase large subunit; Four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AOI86721.1
Dihydroorotase; Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
AOI86944.1
Dihydropyrimidinase; Catalyzes the hydrolytic cleavage of imides that range from linear to heterocyclic and that include hydantoins, dihydropyrimidines, and phthalimides; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.990
AOI81696.1
Uracil phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.988
pyrC
Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
  
 
 0.981
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.
 
 
 0.949
pyrD
Dihydroorotate dehydrogenase 2; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
 
  
 0.944
AsnB
Asparagine synthetase B; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.915
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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