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
ORW93641.1Phosphomethylpyrimidine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (550 aa)    
Predicted Functional Partners:
thiD
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.994
thiG
Thiazole synthase; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
  
 0.971
thiE
Thiamine-phosphate diphosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family.
 
  
 0.867
ORW93639.1
Alpha/beta hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.865
moeB1
Molybdopterin biosynthesis-like protein MoeZ; The proteins in this cluster have high sequence similarity to MoeB and are possibly involved in the synthesis of molybdopterin, but there has been no biochemical or physiological characterization. There is also no genetic linkage to other molybdopterin cofactor synthesis proteins. These proteins are similar to a Pseudomonas stutzeri protein which is essential to pyridine-2,6-bis(thiocarboxylic acid) synthesis that possibly activates a substrate by adenylation; Derived by automated computational analysis using gene prediction method: Protein [...]
 
  
 0.859
thiS
Thiamine biosynthesis protein ThiS; With ThiF, ThiG, and ThiO catalyzes the formation of the thiazole moiety of thiamine pyrophosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.805
fbiC
2-phospho-L-lactate guanylyltransferase; 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase; catalyzes radical-mediated transfer of hydroxybenzyl group from 4-hydroxyphenylpyruvate (HPP) to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO); functions in F420 biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.799
pamO_1
Monooxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.748
ORW89355.1
Cyclodehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.667
bioB
Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
 
  
 0.652
Your Current Organism:
Mycolicibacter terrae
NCBI taxonomy Id: 1788
Other names: ATCC 15755, CCUG 27847, CIP 104321, DSM 43227, JCM 12143, LMG 10394, LMG:10394, M. terrae, Mycobacterium terrae
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.