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
addAdenosine deaminase; Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. (339 aa)    
Predicted Functional Partners:
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
   
 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.
  
 
 0.935
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
  
 0.584
CAZ98906.1
5'nucleotidase, substrate binding 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 and of a C-terminal alpha/beta fold domain with three conserved arginines which are involved in substrate binding and may also play a role in transition-state stabilization. This lipoprotein corresponds only to this latter domain; Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane probably associated with the phosphatase subunit; Func [...]
    
 0.573
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 [...]
    
 0.573
surE
Stationary-phase survival protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
    
 0.563
CAZ96640.1
5'-nucleotidase; Nucleotidase that shows high phosphatase activity toward three nucleoside 5'-monophosphates, UMP, dUMP, and dTMP, and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Is strictly specific to substrates with 5'-phosphates and shows no activity against nucleoside 2'- or 3'-monophosphates. Might be involved in the pyrimidine nucleotide substrate cycles; Uses Divalent metal cation as cofactors. Highest activity with manganese followed by magnesium and cobalt; Belongs to the HAD-like hydrolase superfamily; Localized in the cytoplasm; Hi [...]
   
 0.547
rpeA
Ribulose-phosphate 3-epimerase converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Pentose phosphate pathway; Adopts a a TIM barrel fold; Localized in the cytoplasm; High confidence in function and specificity.
  
    0.540
CAZ94840.1
The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership.
       0.529
CAZ94836.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.493
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
Server load: low (24%) [HD]