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
mqnBFutalosine hydrolase; Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2). (219 aa)    
Predicted Functional Partners:
mqnD
1,4-dihydroxy-6-naphthoate synthase; Catalyzes the conversion of cyclic dehypoxanthine futalosine (cyclic DHFL) into 1,4-dihydroxy-6-naphthoate, a step in the biosynthesis of menaquinone (MK, vitamin K2); Belongs to the MqnA/MqnD family. MqnD subfamily.
 
  
 0.988
mqnC
Dehypoxanthine futalosine cyclase; Radical SAM enzyme that catalyzes the cyclization of dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
  
  
 0.983
mqnE
Aminofutalosine synthase MqnE; Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
 
  
 0.866
mqnA
ABC transporter substrate-binding protein; Catalyzes the dehydration of chorismate into 3-[(1- carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
  
  
 0.856
KZE55464.1
4-hydroxybenzoate octaprenyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UbiA prenyltransferase family.
  
   
 0.753
KZE46809.1
Multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-nucleotidase/3'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family.
    
  0.724
KZE44768.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.713
KZE51522.1
4-hydroxybenzoate decarboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UbiD family.
  
   
 0.708
KZE51517.1
Dihydropyrimidine dehydrogenase subunit B; NADH-dependent; catalyzes the conversion of pyrimidines to 5,6-dihydro compounds in pyrimidine degradation; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.643
mtnK
Methylthioribose kinase; Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
     
 0.638
Your Current Organism:
Brevibacillus parabrevis
NCBI taxonomy Id: 54914
Other names: ATCC 10027, B. parabrevis, Bacillus parabrevis, CIP 103840, DSM 8376, IFO 12334, JCM 8506, LMG 15971, LMG:15971, NBRC 12334, NCIMB 13346, NRRL NRS-605, NRRL NRS-815
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.