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
acpSPhosphopantetheine--protein transferase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. (130 aa)    
Predicted Functional Partners:
AGB24659.1
3-oxoacyl-(acyl-carrier protein) reductase; PFAM: MaoC like domain; Acyl transferase domain; Domain of unknown function (DUF1729); Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain.
 
  
 0.988
coaE
dephospho-CoA kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family.
    
 0.914
AGB26046.1
Polyketide synthase family protein; PFAM: Phosphopantetheine attachment site; Acyl transferase domain; KR domain; Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain.
  
 0.863
AGB26047.1
Polyketide synthase family protein; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain.
  
 0.863
AGB26048.1
Polyketide synthase family protein; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain.
  
 0.863
AGB26341.1
Beta-ketoacyl synthase family protein; PFAM: Phosphopantetheine attachment site; Thioesterase domain; Acyl transferase domain; Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain.
 
 0.857
AGB26045.1
Polyketide synthase family protein; PFAM: Phosphopantetheine attachment site; Acyl transferase domain; Beta-ketoacyl synthase, N-terminal domain; Condensation domain; Beta-ketoacyl synthase, C-terminal domain; TIGRFAM: non-ribosomal peptide synthase domain TIGR01720.
  
 0.844
AGB20799.1
Amino acid adenylation enzyme/thioester reductase family protein,thioester reductase-like protein; PFAM: Male sterility protein; Phosphopantetheine attachment site; Condensation domain; AMP-binding enzyme; TIGRFAM: amino acid adenylation domain; non-ribosomal peptide synthase domain TIGR01720; thioester reductase domain.
  
 0.831
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
  
 
 0.816
nnrE
yjeF-like protein, hydroxyethylthiazole kinase-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate d [...]
    
  0.751
Your Current Organism:
Mycobacterium sp. JS623
NCBI taxonomy Id: 212767
Other names: M. sp. JS623
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.