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
mtnX2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate phosphatase; Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene). (220 aa)    
Predicted Functional Partners:
mtnW
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1- phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P); Belongs to the RuBisCO large chain family. Type IV subfamily.
 
 
 0.996
mtnD
Acireductone dioxygenase; Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
 
 
 0.995
mtnB
Methylthioribulose-1-phosphate dehydratase; Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
 
  
 0.992
mtnK
Methylthioribose kinase; Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
 
  
 0.801
KOO50534.1
Homocysteine methyltransferase; Catalyzes the formation of 5,10-methylenetetrahydrofolate from 5-methyltetrahydrofolate and S-adenosyl-L-homocysteine and methionine from S-adenosyl-L-methionine and L-homocysteine; expressed in B. subtilis under methionine starvation conditions; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.760
KOO50488.1
Aminotransferase; Produces methionine from 2-keto-4-methylthiobutyrate and glutamine in vitro; mutations do not affect methionine salvage in vivo however; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.754
KOO50493.1
LacI family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.659
mtnA
Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.
 
  
 0.628
KOO50519.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.528
KOO37099.1
O-acetylhomoserine aminocarboxypropyltransferase; Catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.517
Your Current Organism:
Bacillus koreensis
NCBI taxonomy Id: 284581
Other names: B. koreensis, Bacillus koreensis Lim et al. 2006, Bacillus sp. BR030, DSM 16467, KCTC 3914, strain BR030
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.