• Version:
  • 11.0 (preview - - version 10.5 still available here)
STRINGSTRING
deoA protein (Thermococcus kodakarensis) - STRING interaction network
"deoA" - AMP phosphorylase in Thermococcus kodakarensis
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
deoAAMP phosphorylase; Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO (503 aa)    
Predicted Functional Partners:
TK1479
Uridine phosphorylase; Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (277 aa)
   
 
  0.933
TK0185
Ribose 1,5-bisphosphate isomerase; Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Only accepts the alpha-anomer of D-ribose 1,5-bisphosphate as substrate, being inactive on the beta-anomer. Displays a strict substrate specificity, since other phosphorylated sugars such as R5P, ribose, G16P, G6P, G1P, FBP, F6P,and PRPP, are not substrates. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO (322 aa)
         
  0.912
thi4
Thiamine thiazole synthase; Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur; Belongs to the THI4 family (251 aa)
         
  0.905
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use CTP and GTP as substrates in addition to ATP (280 aa)
 
     
  0.852
TK2029
ADP-dependent ribose-1-phosphate kinase; Involved in nucleoside degradation. Phosphorylates ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate. Can also act on deoxyribose 1-phosphate (dR1P), but is most active with R1P. ADP is the most preferred phosphate donor, followed by GDP and UDP; Belongs to the carbohydrate kinase PfkB family (294 aa)
         
  0.805
rbcL
Ribulose bisphosphate carboxylase; Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase (444 aa)
 
     
  0.799
TK0557
Nucleoside-triphosphatase THEP1; Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency (180 aa)
           
  0.714
kae1
tRNA N6-adenosine threonylcarbamoyltransferase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity (325 aa)
         
  0.712
sorA
Superoxide reductase; Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide; Belongs to the desulfoferrodoxin family (115 aa)
           
  0.711
TK1252
annotation not available (477 aa)
         
  0.701
Your Current Organism:
Thermococcus kodakarensis
NCBI taxonomy Id: 69014
Other names: Pyrococcus sp. (strain KOD1), Pyrococcus sp. KOD1, T. kodakarensis KOD1, Thermococcus kodakaraensis KOD1, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1, Thermococcus kodakarensis str. KOD1, Thermococcus kodakarensis strain KOD1
Server load: low (8%) [HD]