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
AGA91976.1ADP-ribose pyrophosphatase; PFAM: NUDIX domain; Belongs to the Nudix hydrolase family. (175 aa)    
Predicted Functional Partners:
AGA90838.1
ADP-ribose pyrophosphatase; PFAM: NUDIX domain.
  
  
 
0.925
nnrE
yjeF-like protein, hydroxyethylthiazole kinase-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate d [...]
  
 0.906
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); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
  
 
 0.901
AGA92264.1
PFAM: Phosphoribosyl transferase domain; TIGRFAM: ribose-phosphate pyrophosphokinase; Belongs to the ribose-phosphate pyrophosphokinase family.
  
 
 0.901
AGA89580.1
Phosphomannomutase; PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.
    
  0.900
AGA91732.1
PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.
   
 
  0.900
birA
birA, biotin-(acetyl-CoA-carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
   
    0.612
gpmI
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.
      0.594
AGA91975.1
Putative exonuclease of the beta-lactamase fold involved in RNA processing; PFAM: Metallo-beta-lactamase superfamily.
       0.563
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
     
 0.557
Your Current Organism:
Thioflavicoccus mobilis
NCBI taxonomy Id: 765912
Other names: T. mobilis 8321, Thioflavicoccus mobilis 8321, Thioflavicoccus mobilis ATCC 700959, Thioflavicoccus mobilis str. 8321, Thioflavicoccus mobilis strain 8321
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