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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ADQ03844.1KEGG: ate:Athe_0371 thiamine biosynthesis protein ThiF; TIGRFAM: thiamine biosynthesis protein ThiF; PFAM: UBA/THIF-type NAD/FAD binding protein. (203 aa)    
Predicted Functional Partners:
ADQ03842.1
Thiazole biosynthesis family protein; 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.
 
  
 0.975
thiE
Thiamine-phosphate pyrophosphorylase; 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.
   
 0.968
ADQ03841.1
KEGG: ate:Athe_0368 thiamine biosynthesis protein ThiS; TIGRFAM: thiamine biosynthesis protein ThiS; PFAM: thiamineS protein.
 
  0.967
ADQ03740.1
PFAM: thiamineS protein; KEGG: ate:Athe_0194 thiamineS protein.
  
  0.911
thiI
Thiamine biosynthesis/tRNA modification protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
     
 0.901
ADQ03843.1
PFAM: biotin and thiamin synthesis associated; Radical SAM domain protein; KEGG: csc:Csac_0252 thiamine biosynthesis protein ThiH.
 
  
 0.871
thiC
KEGG: ate:Athe_0373 thiamine biosynthesis protein ThiC; TIGRFAM: thiamine biosynthesis protein ThiC; PFAM: thiamine biosynthesis protein ThiC.
     
 0.824
ADQ03847.1
KEGG: ate:Athe_0381 phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1.
  
  
 0.671
ADQ04911.1
KEGG: ate:Athe_1615 cysteine synthase A; TIGRFAM: cysteine synthase A; cysteine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
   
 
 0.509
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
       0.494
Your Current Organism:
Caldicellulosiruptor owensensis
NCBI taxonomy Id: 632518
Other names: C. owensensis OL, Caldicellulosiruptor owensensis DSM 13100, Caldicellulosiruptor owensensis OL, Caldicellulosiruptor owensensis str. OL, Caldicellulosiruptor owensensis strain OL
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.