close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
AQQ68383.1Coenzyme A pyrophosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (208 aa)    
Predicted Functional Partners:
nnrE
Bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase; 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-spec [...]
  
 0.823
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.
   
    0.600
AQQ68382.1
Metal ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.580
AQQ68386.1
NUDIX hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.574
AQQ68384.1
RND transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.548
rhlE
ATP-dependent RNA helicase; DEAD-box RNA helicase involved in ribosome assembly. Has RNA- dependent ATPase activity and unwinds double-stranded RNA.
   
 0.512
deaD
ATP-dependent RNA helicase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.
   
 0.512
rhlB
ATP-dependent RNA helicase RhlB; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. Belongs to the DEAD box helicase family. RhlB subfamily.
   
 0.512
AQQ67589.1
ATP-dependent RNA helicase DbpA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DEAD box helicase family.
   
 0.512
rnr
Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
   
 0.479
Your Current Organism:
Microbulbifer agarilyticus
NCBI taxonomy Id: 260552
Other names: DSM 19200, JCM 14708, M. agarilyticus, Microbulbifer agarilyticus Miyazaki et al. 2008, Microbulbifer sp. JAMB-A3, Microbulbifer sp. JAMM 0654, Microbulbifer sp. JAMM 0793, strain JAMB A3
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.