STRINGSTRING
tesB tesB pdxS pdxS pdxT pdxT ABK75969.1 ABK75969.1 thrS thrS ABK69978.1 ABK69978.1 ABK70701.1 ABK70701.1 pgsA-2 pgsA-2 pimA pimA ABK71421.1 ABK71421.1 ABK72658.1 ABK72658.1
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
tesBacyl-CoA thioesterase II; Identified by match to protein family HMM PF02551; match to protein family HMM TIGR00189. (283 aa)    
Predicted Functional Partners:
pdxS
Pyridoxine biosynthesis protein; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
  
  
 0.958
pdxT
Glutamine amidotransferase subunit PdxT; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
  
  
 0.955
ABK75969.1
Identified by match to protein family HMM PF01230.
  
    0.816
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
  
    0.794
ABK69978.1
Conserved hypothetical protein; Identified by match to protein family HMM PF01709; match to protein family HMM TIGR01033.
  
    0.750
ABK70701.1
Identified by match to protein family HMM PF00293.
  
 
 0.703
pgsA-2
Phosphatidylinositol synthase; Catalyzes the conjugation of the 1'-hydroxyl group of D-myo- inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid for mycobacteria required for formation of their cell wall. Is essential to the survival of M.smegmatis. Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
    0.660
pimA
Phosphatidylinositol alpha-mannosyltransferase; Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). In contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inos [...]
  
    0.656
ABK71421.1
enoyl-CoA hydratase; Identified by match to protein family HMM PF00378.
 
 
 0.634
ABK72658.1
Lipid A biosynthesis lauroyl acyltransferase; Catalyzes the acylation to the position 6 of the alpha-1,2- linked mannose residue of the phosphatidyl-myo-inositol dimannoside (PIM2) or monomannoside (PIM1).
  
    0.624
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
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