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
mtnBRibulose-5-phosphate 4-epimerase; 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. (208 aa)    
Predicted Functional Partners:
mtnC
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; Bifunctional enzyme that catalyzes the enolization of 2,3- diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK- MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
 
 0.999
mtnA
Putative initiation factor 2 subunit; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
 
 0.997
mtnD
Uncharacterized conserved protein, contains double-stranded beta-helix domain; 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.
 
 
 0.990
speE
Spermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
 
   
 0.746
EDM49252.1
COG1070 Sugar (pentulose and hexulose) kinases.
  
 
 0.743
EDM49073.1
5-methyltetrahydrofolate--homocysteine methyltransferase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
  
 0.630
EDM47568.1
Methylthioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
 
 
 0.587
EDM46827.1
Ankyrin-related protein; COG0666 FOG: Ankyrin repeat.
    
 0.585
EDM47617.1
COG0666 FOG: Ankyrin repeat.
    
 0.585
EDM47937.1
Class II aldolase/adducin, N-terminal family protein; Putative enzyme; COG0235 Ribulose-5-phosphate 4-epimerase and related epimerases and aldolases.
  
     0.577
Your Current Organism:
Marinobacter algicola
NCBI taxonomy Id: 443152
Other names: M. algicola DG893, Marinobacter algicola DG893, Marinobacter algicola str. DG893, Marinobacter algicola strain DG893, Marinobacter sp. DG893
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.