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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
aptAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (170 aa)    
Predicted Functional Partners:
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
 0.992
hptA/adkA
Bifunctional protein Hypoxanthine-guanine phosphoribosyltransferase / Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
  
 0.969
gmkA
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP.
  
 
 0.965
purH
Bifunctional enzyme that catalyses the last two steps in de novo purine biosynthesis. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) formyltransferase that catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield 5-formylaminoimidazole-4-carboxamide ribonucleotide (FAICAR) and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase, cyclizing FAICAR to IMP; Belongs to the purH family; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.958
purB
Adenylosuccinate lyase catalyzes step 8 in the pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. It cleaves succinylaminoimidazole carboxamide ribotide into aminoimidazole carboxamide ribotide and fumarate, as well as adenylosuccinate into adenylate and fumarate. Localized in the cytoplasm; High confidence in function and specificity.
  
 0.958
add
Adenosine deaminase; Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
   
 0.951
punA
Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
  
 
 0.939
dgkA1
Deoxyguanosine kinase plays an essential role in generating the deoxyribonucleotide precursors, dGTP and dATP, for DNA metabolism. Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.918
surE
Stationary-phase survival protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
    
 0.915
nutA
5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...]
    
 0.912
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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