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
mtnKMethylthioribose kinase (methionine salvage pathway); Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. (397 aa)    
Predicted Functional Partners:
mtnA
Methylthioribose-1-phosphate isomerase (methionine salvage pathway); Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
 
 0.999
mtnW
2,3-diketo-5-methylthiopentyl-1-phosphate enolase (DK-MTP-1-P 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.
 
  
 0.997
mtnB
Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase); Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Belongs to the aldolase class II family. MtnB subfamily.
 
  
 0.994
mtnD
Acireductone dioxygenase (Ni2+ or Fe2+-requiring); 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.
 
  
 0.993
mtnN
Methylthioadenosine / S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
  
  
 0.993
mtnX
2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphatephosphatase (HK-MTPenyl-1-P phosphatase); Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene).
 
  
 0.981
mtnU
Ketoglutaramate omega-amidase; May be involved in a regulatory step in the methylthioribose (MTR) recycling pathway; Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
  
  
 0.977
mtnE
Methionine-glutamine aminotransferase; Catalyzes the formation of methionine from 2-keto-4- methylthiobutyrate (KMTB).
  
  
 0.974
samT
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
  
 0.821
yxjG
Putative methyltetrahydrofolate methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis YxjH.
   
  
 0.731
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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