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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
pncB2Nicotinate phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family. (440 aa)    
Predicted Functional Partners:
PncA
Pyrazinamidase/nicotinamidase.
 
 0.998
nadC
Nicotinate-nucleotide pyrophosphorylase; Belongs to the NadC/ModD family.
   
 0.977
madD
Putative nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
 
 0.971
CinA
Competence-damage protein cinA.
  
 
 0.927
RY70_463
Phosphohydrolase.
    
 0.908
RY70_1653
Putative 5'-nucleotidase.
    
 0.905
RY70_423
Hypothetical protein.
       0.709
CapA
PGA biosynthesis protein.
  
    0.706
nadE
Glutamine-dependent NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
 
  
 0.682
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.
       0.590
Your Current Organism:
Bifidobacterium bifidum
NCBI taxonomy Id: 1681
Other names: AS 1.2212, ATCC 29521, Actinobacterium bifidum, Actinomyces bifidus, Actinomyces parabifidus, B. bifidum, BCRC 14615, Bacillus bifidus, Bacillus bifidus communis, Bacterium bifidum, Bacteroides bifidus, Bifidibacterium bifidum, CCRC 14615, CCRC:14615, CCUG 18364, CCUG 45217, CIP 56.7, Cohnistreptothrix bifidus, DSM 20456, IFO 14252, KCTC 3202, LMG 11041, LMG 8810, LMG:11041, LMG:8810, Lactobacillus bifidus type II, Lactobacillus parabifidus, NBRC 100015, NBRC 14252, NCFB 2715, NCIMB 702715, NCTC 13001, Nocardia bifida, Tissieria bifida, strain Ti
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