STRINGSTRING
dut dut tdk tdk PC1_4101 PC1_4101 thyA thyA tmk tmk ndk ndk PC1_0360 PC1_0360 dcd dcd PC1_1083 PC1_1083 PC1_2775 PC1_2775 PC1_3893 PC1_3893
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
dutDeoxyuridine 5'-triphosphate nucleotidohydrolase Dut; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. (152 aa)    
Predicted Functional Partners:
tdk
PFAM: thymidine kinase; KEGG: eca:ECA2327 thymidine kinase.
   
 
 0.971
PC1_4101
Phosphopantothenoylcysteine decarboxylase/phosphopantothenate/cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
 
  
 0.968
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
 0.967
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family.
  
 
 0.946
ndk
Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
   
 
 0.932
PC1_0360
KEGG: eca:ECA0375 anaerobic ribonucleoside triphosphate reductase; TIGRFAM: anaerobic ribonucleoside-triphosphate reductase; PFAM: formate C-acetyltransferase glycine radical; ATP-cone domain protein.
    
 0.927
dcd
Deoxycytidine triphosphate deaminase; Catalyzes the deamination of dCTP to dUTP.
    
 0.927
PC1_1083
PFAM: 5'-Nucleotidase domain protein; metallophosphoesterase; KEGG: eca:ECA1184 bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Belongs to the 5'-nucleotidase family.
     
  0.900
PC1_2775
Metal dependent phosphohydrolase; Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates.
    
  0.900
PC1_3893
TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase; KEGG: eca:ECA4103 putative hydrolase.
    
  0.900
Your Current Organism:
Pectobacterium carotovorum
NCBI taxonomy Id: 561230
Other names: P. carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum str. PC1, Pectobacterium carotovorum subsp. carotovorum strain PC1
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.