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
mtnDAcireductone 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. (177 aa)    
Predicted Functional Partners:
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). Belongs to the aldolase class II family. MtnB subfamily.
 
 
 0.994
AOP34989.1
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.984
mtnA
S-methyl-5-thioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
 
 
 0.868
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
     
 0.820
AOP36562.1
3-oxoacyl-ACP reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.762
metH
Methionine synthase; 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.
  
  
 0.714
metF
Methylenetetrahydrofolate reductase [NAD(P)H]; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the methylenetetrahydrofolate reductase family.
   
  
 0.567
speE-2
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.
  
   
 0.523
AOP32493.1
Cys/Met metabolism PLP-dependent enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.498
AOP35680.1
Amine oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.480
Your Current Organism:
Leptospira alstonii
NCBI taxonomy Id: 28452
Other names: ATCC BAA-2439, L. alstonii, Leptospira alstoni, Leptospira alstonii Smythe et al. 2013, Leptospira genomosp. 1, strain 79601
Server load: medium (78%) [HD]