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
ADO50401.1KEGG: cro:ROD_37611 thiamine biosynthesis protein; TIGRFAM: thiamine biosynthesis protein ThiS; PFAM: thiamineS protein. (66 aa)    
Predicted Functional Partners:
ADO50400.1
PFAM: UBA/THIF-type NAD/FAD binding protein; MoeZ/MoeB domain protein; KEGG: enc:ECL_00253 hypothetical protein.
  
 0.998
thiG
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.
 
 
 0.997
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.
 
  
 0.972
thiC
Thiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
  
  
 0.963
ADO50403.1
KEGG: enc:ECL_00250 thiamine biosynthesis protein ThiH; TIGRFAM: thiazole biosynthesis protein ThiH; PFAM: biotin and thiamin synthesis associated; Radical SAM domain protein.
 
  
 0.955
ADO49237.1
KEGG: kpn:KPN_00859 molybdopterin biosynthesis protein MoeB; TIGRFAM: molybdopterin synthase sulfurylase MoeB; PFAM: UBA/THIF-type NAD/FAD binding protein; MoeZ/MoeB domain protein.
  
 
 0.841
ADO47857.1
TIGRFAM: phosphomethylpyrimidine kinase; KEGG: kpu:KP1_3768 phosphomethylpyrimidine kinase; PFAM: Phosphomethylpyrimidine kinase type-1.
  
    0.818
ADO48134.1
NLP/P60 protein; KEGG: enc:ECL_01713 GP19; PFAM: NLP/P60 protein; SMART: Mov34/MPN/PAD-1 family protein.
 
 
 0.803
ttcA
PP-loop domain protein; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
  
 
 0.643
tilS
tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family.
  
 
 0.635
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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