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
pyrDDihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. (334 aa)    
Predicted Functional Partners:
fre
NAD(P)H-flavin reductase; catalyzes the reversible oxidation/reduction of NAD(P) and flavine mononucleotide; in Salmonella and E. coli this protein also reduces aquacob(III)alamin to cob(II)alamin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.998
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).
  
 0.996
pyrC
Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
 
 
 0.988
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.
 
 0.982
pyrF
Orotidine 5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP); Belongs to the OMP decarboxylase family. Type 1 subfamily.
  
 
 0.976
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
 0.946
guaB
Inosine-5-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
 
 0.943
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.
 
  
 0.941
pheT
phenylalanine--tRNA ligase; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.931
KPD23525.1
Aspartate carbamoyltransferase; Catalyzes the conversion of carbamoyl phosphate and l-aspartate to yield orthophosphate and n-carbamoyl-l-aspartate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
  
 
 0.861
Your Current Organism:
Idiomarina zobellii
NCBI taxonomy Id: 86103
Other names: ATCC BAA-313, I. zobellii, Idiomarina zobellii Ivanova et al. 2000, KMM 231, marine bacterium KM231
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